Proteins > Mitogen-activated protein kinase 14
Page last updated: 2024-08-07 17:10:17
Mitogen-activated protein kinase 14
A mitogen-activated protein kinase 14 that is encoded in the genome of human. [PRO:CNA, UniProtKB:Q16539]
Synonyms
MAP kinase 14;
MAPK 14;
EC 2.7.11.24;
Cytokine suppressive anti-inflammatory drug-binding protein;
CSAID-binding protein;
CSBP;
MAP kinase MXI2;
MAX-interacting protein 2;
Mitogen-activated protein kinase p38 alpha;
MA
Research
Bioassay Publications (217)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 7 (3.23) | 18.2507 |
2000's | 103 (47.47) | 29.6817 |
2010's | 96 (44.24) | 24.3611 |
2020's | 11 (5.07) | 2.80 |
Compounds (366)
Drugs with Inhibition Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
1-anilino-8-naphthalenesulfonate | Homo sapiens (human) | IC50 | 1.2000 | 1 | 1 |
rtki cpd | Homo sapiens (human) | IC50 | 0.5600 | 1 | 1 |
benzbromarone | Homo sapiens (human) | IC50 | 1.2350 | 1 | 0 |
bithionol | Homo sapiens (human) | IC50 | 0.3180 | 1 | 0 |
celecoxib | Homo sapiens (human) | IC50 | 0.8100 | 1 | 1 |
fenbendazole | Homo sapiens (human) | IC50 | 3.1880 | 1 | 0 |
hexachlorophene | Homo sapiens (human) | IC50 | 0.0876 | 1 | 0 |
iodoquinol | Homo sapiens (human) | IC50 | 0.3640 | 1 | 0 |
kynurenic acid | Homo sapiens (human) | Ki | 1,300.0000 | 1 | 1 |
olomoucine | Homo sapiens (human) | IC50 | 63.5000 | 1 | 2 |
pd 153035 | Homo sapiens (human) | IC50 | 6.3000 | 1 | 1 |
pd 169316 | Homo sapiens (human) | IC50 | 0.0890 | 1 | 1 |
ag 1879 | Homo sapiens (human) | IC50 | 4.2300 | 1 | 1 |
sb 220025 | Homo sapiens (human) | IC50 | 2.5880 | 6 | 7 |
sb 239063 | Homo sapiens (human) | IC50 | 0.0415 | 4 | 4 |
sb 202190 | Homo sapiens (human) | IC50 | 0.0625 | 17 | 17 |
sb 216995 | Homo sapiens (human) | IC50 | 16.7657 | 5 | 6 |
sk&f 86002 | Homo sapiens (human) | IC50 | 2.1217 | 5 | 6 |
imatinib | Homo sapiens (human) | IC50 | 61.2333 | 3 | 3 |
ici 204,219 | Homo sapiens (human) | IC50 | 0.3530 | 1 | 0 |
zm 336372 | Homo sapiens (human) | IC50 | 1.0900 | 2 | 2 |
pyrazolanthrone | Homo sapiens (human) | IC50 | 15.0750 | 1 | 2 |
3,3',4',5-tetrachlorosalicylanilide | Homo sapiens (human) | IC50 | 2.1760 | 1 | 0 |
tribromsalan | Homo sapiens (human) | IC50 | 0.7150 | 1 | 0 |
4-octylphenol | Homo sapiens (human) | IC50 | 15.0160 | 1 | 0 |
nafenopin | Homo sapiens (human) | IC50 | 3.7405 | 1 | 0 |
pirfenidone | Homo sapiens (human) | IC50 | 165.4000 | 1 | 1 |
closantel | Homo sapiens (human) | IC50 | 0.6560 | 1 | 0 |
staurosporine | Homo sapiens (human) | IC50 | 0.5052 | 2 | 2 |
mifepristone | Homo sapiens (human) | IC50 | 83.0610 | 1 | 0 |
nelfinavir | Homo sapiens (human) | IC50 | 18.2240 | 1 | 0 |
3,4-dihydro-2(1h)-quinolinone | Homo sapiens (human) | IC50 | 0.0007 | 2 | 2 |
epigallocatechin gallate | Homo sapiens (human) | IC50 | 2.2100 | 1 | 1 |
gallocatechol | Homo sapiens (human) | IC50 | 4.4150 | 1 | 2 |
cephalotaxine | Homo sapiens (human) | IC50 | 0.2000 | 1 | 1 |
epicatechin | Homo sapiens (human) | IC50 | 78.5500 | 1 | 2 |
hesperetin | Homo sapiens (human) | IC50 | 54.6000 | 1 | 1 |
u 74006f | Homo sapiens (human) | IC50 | 7.4060 | 1 | 0 |
epicatechin gallate | Homo sapiens (human) | IC50 | 1.4700 | 1 | 1 |
mk 0663 | Homo sapiens (human) | IC50 | 0.5300 | 1 | 1 |
perifosine | Homo sapiens (human) | IC50 | 1.2000 | 1 | 1 |
birb 796 | Homo sapiens (human) | IC50 | 0.0674 | 18 | 18 |
birb 796 | Homo sapiens (human) | Ki | 0.0186 | 4 | 4 |
nevadensin | Homo sapiens (human) | IC50 | 20.1000 | 1 | 2 |
sb 203580 | Homo sapiens (human) | IC50 | 15.3271 | 73 | 75 |
sb 203580 | Homo sapiens (human) | Ki | 0.0375 | 2 | 2 |
4'-o-methylepigallocatechin | Homo sapiens (human) | IC50 | 39.1600 | 1 | 1 |
sorafenib | Homo sapiens (human) | IC50 | 0.6228 | 8 | 8 |
1-phenyl-3-methyl-4-benzoyl-5-pyrazolone | Homo sapiens (human) | IC50 | 100.0000 | 2 | 2 |
1-(3-tert-butyl-1-methylpyrazol-5-yl)-3-(4-chlorophenyl)urea | Homo sapiens (human) | IC50 | 12.8648 | 3 | 3 |
pd 166326 | Homo sapiens (human) | IC50 | 0.1400 | 1 | 1 |
hts 466284 | Homo sapiens (human) | IC50 | 25.8700 | 2 | 2 |
diethylstilbestrol | Homo sapiens (human) | IC50 | 32.9030 | 1 | 0 |
repsox | Homo sapiens (human) | IC50 | 16.0000 | 1 | 1 |
N-(3-cyano-4,5,6,7-tetrahydro-1-benzothiophen-2-yl)-1-naphthalenecarboxamide | Homo sapiens (human) | IC50 | 15.8489 | 1 | 1 |
dieldrin | Homo sapiens (human) | IC50 | 43.1930 | 1 | 0 |
u 0126 | Homo sapiens (human) | IC50 | 55.0000 | 1 | 1 |
rwj 67657 | Homo sapiens (human) | IC50 | 1.0000 | 1 | 1 |
vx-745 | Homo sapiens (human) | IC50 | 1.8567 | 15 | 16 |
vx-745 | Homo sapiens (human) | Ki | 0.0008 | 1 | 1 |
dasatinib | Homo sapiens (human) | IC50 | 0.1000 | 3 | 3 |
quercetin | Homo sapiens (human) | IC50 | 2.8800 | 1 | 2 |
3,7-dimethoxy-5,3',4'-trihydroxyflavone | Homo sapiens (human) | IC50 | 10.0000 | 1 | 2 |
acacetin | Homo sapiens (human) | IC50 | 27.8900 | 1 | 2 |
apigenin | Homo sapiens (human) | IC50 | 10.2667 | 1 | 3 |
luteolin | Homo sapiens (human) | IC50 | 10.1500 | 1 | 2 |
quercitrin | Homo sapiens (human) | IC50 | 24.1500 | 1 | 2 |
luteolin-7-glucoside | Homo sapiens (human) | IC50 | 44.7750 | 1 | 2 |
chrysoeriol | Homo sapiens (human) | IC50 | 33.6000 | 1 | 1 |
quercetin 3-o-glucopyranoside | Homo sapiens (human) | IC50 | 41.4333 | 1 | 3 |
rutin | Homo sapiens (human) | IC50 | 65.9000 | 1 | 1 |
kaempferol | Homo sapiens (human) | IC50 | 18.7500 | 1 | 2 |
genistein | Homo sapiens (human) | IC50 | 61.4000 | 1 | 1 |
montelukast | Homo sapiens (human) | IC50 | 0.8560 | 1 | 0 |
apigenin dimethylether | Homo sapiens (human) | IC50 | 27.8000 | 1 | 1 |
chrysin | Homo sapiens (human) | IC50 | 25.8500 | 1 | 2 |
diosmetin | Homo sapiens (human) | IC50 | 25.9000 | 1 | 2 |
fisetin | Homo sapiens (human) | IC50 | 2.6500 | 1 | 2 |
hispidulin | Homo sapiens (human) | IC50 | 26.7000 | 1 | 2 |
3-methylquercetin | Homo sapiens (human) | IC50 | 13.2000 | 1 | 2 |
kaempferide | Homo sapiens (human) | IC50 | 42.7000 | 1 | 2 |
morin | Homo sapiens (human) | IC50 | 19.1000 | 1 | 2 |
myricetin | Homo sapiens (human) | IC50 | 1.9400 | 1 | 2 |
orientin | Homo sapiens (human) | IC50 | 46.9500 | 1 | 2 |
patuletin | Homo sapiens (human) | IC50 | 38.6000 | 1 | 2 |
isotretinoin | Homo sapiens (human) | IC50 | 2.5290 | 1 | 0 |
kn 93 | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
ombuine | Homo sapiens (human) | IC50 | 29.6900 | 1 | 2 |
5,7-dihydroxy-4',6-dimethoxyflavone | Homo sapiens (human) | IC50 | 32.4000 | 1 | 1 |
jaceosidin | Homo sapiens (human) | IC50 | 19.0000 | 1 | 2 |
5,4'-dihydroxy-7,3'-dimethoxyflavone | Homo sapiens (human) | IC50 | 30.1500 | 1 | 2 |
2-tert-butyl-9-fluoro-3,6-dihydro-7h-benz(h)imidazo(4,5-f)isoquinoline-7-one | Homo sapiens (human) | IC50 | 11.0000 | 1 | 1 |
ml 3403 | Homo sapiens (human) | IC50 | 0.7748 | 6 | 6 |
d 4476 | Homo sapiens (human) | IC50 | 8.4885 | 4 | 4 |
cyc 116 | Homo sapiens (human) | Ki | 10.0000 | 1 | 1 |
4-[4-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1H-imidazol-5-yl]pyridine | Homo sapiens (human) | IC50 | 0.0400 | 1 | 1 |
a 770041 | Homo sapiens (human) | IC50 | 25.0000 | 1 | 1 |
vk 19911 | Homo sapiens (human) | IC50 | 0.1009 | 7 | 7 |
vk 19911 | Homo sapiens (human) | Ki | 0.0600 | 1 | 1 |
[4-(2-amino-4-bromoanilino)-2-chlorophenyl]-(2-methylphenyl)methanone | Homo sapiens (human) | IC50 | 0.0282 | 6 | 6 |
rwj 68354 | Homo sapiens (human) | IC50 | 0.0385 | 5 | 4 |
gw843682x | Homo sapiens (human) | IC50 | 15.0000 | 1 | 1 |
sb-505124 | Homo sapiens (human) | IC50 | 0.6072 | 5 | 5 |
sb 242235 | Homo sapiens (human) | IC50 | 0.0572 | 4 | 4 |
sb 242235 | Homo sapiens (human) | Ki | 0.0360 | 1 | 1 |
sd 0006 | Homo sapiens (human) | IC50 | 0.1100 | 1 | 1 |
scio-469 | Homo sapiens (human) | IC50 | 0.0320 | 5 | 5 |
sb 210313 | Homo sapiens (human) | IC50 | 0.9067 | 3 | 3 |
3,5-bis(2-fluorobenzylidene)piperidin-4-one | Homo sapiens (human) | IC50 | 92.0000 | 1 | 1 |
ct52923 | Homo sapiens (human) | IC50 | 30.0000 | 1 | 1 |
tofacitinib | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
4-n-butyl-1-(4-(2-methylphenyl)-4-oxo-1-butyl)-piperidine hydrogen chloride | Homo sapiens (human) | Ki | 1.0000 | 1 | 1 |
tak-715 | Homo sapiens (human) | IC50 | 0.1236 | 4 | 4 |
ly2090314 | Homo sapiens (human) | IC50 | 20.0000 | 1 | 1 |
ly-2157299 | Homo sapiens (human) | IC50 | 0.4736 | 5 | 5 |
N-(3-cyanophenyl)-2'-methyl-5'-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-4-carboxamide | Homo sapiens (human) | IC50 | 1.5000 | 3 | 3 |
N-(3-cyanophenyl)-2'-methyl-5'-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-4-carboxamide | Homo sapiens (human) | Ki | 0.7771 | 6 | 7 |
gw 799388 | Homo sapiens (human) | IC50 | 7.2800 | 1 | 1 |
sotrastaurin | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
ps 540446 | Homo sapiens (human) | IC50 | 0.0130 | 2 | 2 |
pha 665752 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
l 783277 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
r 1487 | Homo sapiens (human) | IC50 | 0.0100 | 1 | 1 |
danusertib | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
nvp-aew541 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
fr 180204 | Homo sapiens (human) | Ki | 0.3100 | 1 | 1 |
6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamide | Homo sapiens (human) | IC50 | 0.1000 | 1 | 1 |
6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamide | Homo sapiens (human) | Ki | 0.0217 | 3 | 4 |
cc-930 | Homo sapiens (human) | IC50 | 3.4000 | 2 | 2 |
gw 2580 | Homo sapiens (human) | IC50 | 16.0000 | 1 | 1 |
tak 285 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
crizotinib | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
5-(5,6-dimethoxy-1-benzimidazolyl)-3-[(2-methylsulfonylphenyl)methoxy]-2-thiophenecarbonitrile | Homo sapiens (human) | IC50 | 15.8489 | 1 | 1 |
4-[2-(2-chloro-4-fluoroanilino)-5-methyl-4-pyrimidinyl]-N-[(1S)-1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide | Homo sapiens (human) | Ki | 4.0000 | 1 | 1 |
motesanib | Homo sapiens (human) | IC50 | 1.0880 | 1 | 11 |
in 1130 | Homo sapiens (human) | IC50 | 1.1167 | 6 | 6 |
4-(3-cyclohexyl-5-(4-fluoro-phenyl)-3h-imidazol-4-yl)pyrimidin-2-ylamine | Homo sapiens (human) | IC50 | 0.1146 | 2 | 2 |
5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
N-(2,4-dimethoxyphenyl)-N-[2-[4-(4-methyl-1-piperazinyl)anilino]-4-pyrimidinyl]carbamic acid (2,6-dimethylphenyl) ester | Homo sapiens (human) | IC50 | 0.6496 | 2 | 5 |
azd 1152-hqpa | Homo sapiens (human) | Ki | 10.0000 | 1 | 1 |
2-({2-[(3-hydroxyphenyl)amino]pyrimidin-4-yl}amino)benzamide | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
4-methyl-3-(2-(2-morpholinoethylamino)quinazolin-6-yl)-n-(3-(trifluoromethyl)phenyl)benzamide | Homo sapiens (human) | IC50 | 0.0030 | 1 | 1 |
tannins | Homo sapiens (human) | IC50 | 0.3750 | 1 | 0 |
pamapimod | Homo sapiens (human) | IC50 | 0.0140 | 2 | 2 |
pha 848125 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
ph 797804 | Homo sapiens (human) | IC50 | 0.0460 | 4 | 6 |
ph 797804 | Homo sapiens (human) | Ki | 0.0044 | 2 | 2 |
amg 458 | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
arry-614 | Homo sapiens (human) | IC50 | 0.0040 | 1 | 1 |
bms 777607 | Homo sapiens (human) | IC50 | 2.0000 | 1 | 1 |
ponatinib | Homo sapiens (human) | IC50 | 0.0100 | 1 | 1 |
N-cyclopropyl-3-{4-[(cyclopropylmethyl)carbamoyl]phenyl}-4-methylbenzamide | Homo sapiens (human) | IC50 | 0.0919 | 4 | 4 |
N-cyclopropyl-3-{4-[(cyclopropylmethyl)carbamoyl]phenyl}-4-methylbenzamide | Homo sapiens (human) | Ki | 0.0115 | 6 | 7 |
N-(2,6-difluorophenyl)-5-[3-[2-[5-ethyl-2-methoxy-4-[4-(4-methylsulfonyl-1-piperazinyl)-1-piperidinyl]anilino]-4-pyrimidinyl]-2-imidazo[1,2-a]pyridinyl]-2-methoxybenzamide | Homo sapiens (human) | IC50 | 11.0000 | 1 | 1 |
entrectinib | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
4-[6-[4-(methoxycarbonylamino)phenyl]-4-(4-morpholinyl)-1-pyrazolo[3,4-d]pyrimidinyl]-1-piperidinecarboxylic acid methyl ester | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
skepinone-l | Homo sapiens (human) | IC50 | 0.0091 | 8 | 4 |
pha 793887 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
tak-632 | Homo sapiens (human) | IC50 | 0.6000 | 1 | 1 |
3-((4-(6-methylpyridin-2-yl)-5-(quinolin-6-yl)-1h-imidazol-2-yl)methyl)benzamide | Homo sapiens (human) | IC50 | 0.5400 | 1 | 1 |
arry-371797 | Homo sapiens (human) | IC50 | 0.0045 | 1 | 1 |
nms p937 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
nms-p118 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
encorafenib | Homo sapiens (human) | IC50 | 2.2000 | 1 | 0 |
lfm a13 | Homo sapiens (human) | IC50 | 500.0000 | 1 | 1 |
urmc-099 | Homo sapiens (human) | IC50 | 12.0500 | 1 | 1 |
ew-7197 | Homo sapiens (human) | IC50 | 2.3960 | 5 | 5 |
4-[[9-[(3R)-3-oxolanyl]-8-(2,4,6-trifluoroanilino)-2-purinyl]amino]-1-cyclohexanol | Homo sapiens (human) | IC50 | 3.0000 | 1 | 1 |
ly3009120 | Homo sapiens (human) | IC50 | 0.0610 | 1 | 1 |
nms-e973 | Homo sapiens (human) | IC50 | 0.0100 | 1 | 1 |
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
fasudil | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sb 202190 | Homo sapiens (human) | Kd | 0.0114 | 2 | 2 |
sk&f 86002 | Homo sapiens (human) | Kd | 0.1800 | 1 | 1 |
imatinib | Homo sapiens (human) | Kd | 13.2906 | 4 | 4 |
troglitazone | Homo sapiens (human) | EC50 | 1.0000 | 1 | 1 |
triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
staurosporine | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
picropodophyllin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gefitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
lestaurtinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
perifosine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vatalanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
ruboxistaurin | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
canertinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
birb 796 | Homo sapiens (human) | EC50 | 0.0180 | 1 | 1 |
birb 796 | Homo sapiens (human) | Kd | 0.0013 | 17 | 18 |
cyc 202 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
sb 203580 | Homo sapiens (human) | EC50 | 0.0600 | 2 | 2 |
sb 203580 | Homo sapiens (human) | Kd | 0.0128 | 6 | 6 |
enzastaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
erlotinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
lapatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
sorafenib | Homo sapiens (human) | Kd | 5.2717 | 6 | 6 |
1-(3-tert-butyl-1-methylpyrazol-5-yl)-3-(4-chlorophenyl)urea | Homo sapiens (human) | EC50 | 5.9000 | 1 | 1 |
1-(3-tert-butyl-1-methylpyrazol-5-yl)-3-(4-chlorophenyl)urea | Homo sapiens (human) | Kd | 1.5482 | 10 | 10 |
pd 173955 | Homo sapiens (human) | Kd | 0.0670 | 1 | 1 |
s 1033 | Homo sapiens (human) | EC50 | 4.6000 | 1 | 1 |
s 1033 | Homo sapiens (human) | Kd | 0.6157 | 3 | 3 |
xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
bms 387032 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
sf 2370 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tandutinib | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
vx-745 | Homo sapiens (human) | Kd | 0.0029 | 4 | 4 |
dasatinib | Homo sapiens (human) | EC50 | 0.4700 | 1 | 1 |
dasatinib | Homo sapiens (human) | Kd | 0.3587 | 7 | 7 |
ha 1100 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
7-epi-hydroxystaurosporine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
zd 6474 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1h-imidazol-2-yl)benzamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
imd 0354 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alvocidib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
bosutinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
su 11248 | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
jnj-7706621 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
vx680 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
cyc 116 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
trk 820 | Homo sapiens (human) | EC50 | 0.0052 | 1 | 1 |
ekb 569 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
axitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
4-[4-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1H-imidazol-5-yl]pyridine | Homo sapiens (human) | Kd | 0.0110 | 1 | 1 |
temsirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pd 184352 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
on 01910 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
vk 19911 | Homo sapiens (human) | Kd | 0.0135 | 2 | 2 |
av 412 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
telatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
y-39983 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cp 547632 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms345541 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
lenvatinib | Homo sapiens (human) | Kd | 0.2170 | 1 | 1 |
pd 0325901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
midostaurin | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
px-866 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ripasudil | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
osi 930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ki 20227 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
scio-469 | Homo sapiens (human) | Kd | 0.0042 | 2 | 2 |
cp 724714 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
pi103 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
hmn-214 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tivozanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
hki 272 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
tofacitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
cediranib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pazopanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
su 14813 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
bibw 2992 | Homo sapiens (human) | Kd | 1.1735 | 2 | 2 |
binimetinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sotrastaurin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
aee 788 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
saracatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vx 702 | Homo sapiens (human) | Kd | 0.0054 | 2 | 2 |
crenolanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tg100-115 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
cc 401 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms 599626 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
exel-7647 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
pha 665752 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
azd 7762 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
regorafenib | Homo sapiens (human) | Kd | 0.7050 | 1 | 1 |
6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-one | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
brivanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
mp470 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
rgb 286638 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
at 7519 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bms-690514 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bi 2536 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
inno-406 | Homo sapiens (human) | Kd | 0.5360 | 1 | 1 |
r 1487 | Homo sapiens (human) | Kd | 0.0002 | 1 | 1 |
nvp-ast487 | Homo sapiens (human) | Kd | 0.0730 | 2 | 2 |
kw 2449 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
danusertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
abt 869 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
azd 8931 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
arq 197 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd 1152 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
pf 00299804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ridaforolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ch 4987655 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamide | Homo sapiens (human) | Kd | 0.0090 | 1 | 1 |
cc-930 | Homo sapiens (human) | Kd | 0.7290 | 1 | 1 |
gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
tak 285 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
idelalisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
crizotinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
chir-265 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
motesanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
fostamatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
trametinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mln8054 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
pf-562,271 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
GDC-0879 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
jnj-26483327 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ly2603618 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tg100801 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dactolisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
bgt226 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 461364 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
azd 1152-hqpa | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
nvp-tae684 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
enmd 2076 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
e 7050 | Homo sapiens (human) | Kd | 1.1110 | 1 | 1 |
2-amino-8-ethyl-4-methyl-6-(1H-pyrazol-5-yl)-7-pyrido[2,3-d]pyrimidinone | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tak-901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pamapimod | Homo sapiens (human) | Kd | 0.0013 | 2 | 2 |
gdc-0973 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
buparlisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd 1480 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd8330 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 848125 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
fedratinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
gsk690693 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
14-methyl-20-oxa-5,7,14,26-tetraazatetracyclo(19.3.1.1(2,6).1(8,12))heptacosa-1(25),2(26),3,5,8(27),9,11,16,21,23-decaene | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd5438 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pf 04217903 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gdc 0941 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
icotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ph 797804 | Homo sapiens (human) | Kd | 0.0038 | 2 | 2 |
kx-01 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
plx 4720 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
mk 5108 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cx 4945 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
arry-614 | Homo sapiens (human) | Kd | 0.0420 | 1 | 1 |
tak 593 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mln 8237 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sgx 523 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bms 754807 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms 777607 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sgi 1776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pci 32765 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
ponatinib | Homo sapiens (human) | Kd | 0.1540 | 1 | 1 |
amg 900 | Homo sapiens (human) | Kd | 0.7350 | 1 | 1 |
mk-1775 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
AMG-208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
quizartinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
at13148 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tak 733 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
mk 2206 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sns 314 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
lucitanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pf-04691502 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
n-(cyanomethyl)-4-(2-((4-(4-morpholinyl)phenyl)amino)-4-pyrimidinyl)benzamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dcc-2036 | Homo sapiens (human) | Kd | 2.7630 | 1 | 1 |
cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
defactinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ly2584702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
incb-018424 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
poziotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
asp3026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
entrectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pexidartinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
TAK-580 | Homo sapiens (human) | Kd | 0.3580 | 1 | 1 |
gsk 2126458 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
emd1214063 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1838705a | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
pf 3758309 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
gdc 0980 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd2014 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
(5-(2,4-bis((3s)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
plx4032 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1363089 | Homo sapiens (human) | Kd | 15.1600 | 2 | 2 |
arry-334543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
kin-193 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk 2461 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bay 869766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
as 703026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
baricitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dabrafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pki 587 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
n-(3-fluoro-4-((1-methyl-6-(1h-pyrazol-4-yl)-1h-indazol-5 yl)oxy)phenyl)-1-(4-fluorophenyl)-6-methyl-2-oxo-1,2-dihydropyridine-3-carboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ribociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk-8033 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 793887 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sb 1518 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
abemaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk-8776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
afuresertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1070916 | Homo sapiens (human) | Kd | 8.5000 | 1 | 1 |
jnj38877605 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dinaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gilteritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
glpg0634 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms-911543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
gsk2141795 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd8186 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
byl719 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cep-32496 | Homo sapiens (human) | Kd | 0.5660 | 1 | 1 |
rociletinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ceritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd1208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
vx-509 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
debio 1347 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
volitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
osimertinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
at 9283 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
otssp167 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
chir 258 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
nintedanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pp242 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
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Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
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[no title available]Journal of medicinal chemistry, , 10-12, Volume: 60, Issue:19, 2017
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Structure-based design, synthesis and biological evaluation of N-pyrazole, N'-thiazole urea inhibitors of MAP kinase p38α.European journal of medicinal chemistry, , Volume: 48, 2012
Design and synthesis of novel p38α MAP kinase inhibitors: discovery of pyrazole-benzyl ureas bearing 2-molpholinopyrimidine moiety.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 22, Issue:15, 2012
Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD).Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 21, Issue:23, 2011
Design and synthesis of inhaled p38 inhibitors for the treatment of chronic obstructive pulmonary disease.Journal of medicinal chemistry, , Nov-24, Volume: 54, Issue:22, 2011
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
X-ray crystal structure of JNK2 complexed with the p38alpha inhibitor BIRB796: insights into the rational design of DFG-out binding MAP kinase inhibitors.Bioorganic & medicinal chemistry letters, , Sep-01, Volume: 20, Issue:17, 2010
Biochemical and biophysical characterization of unique switch pocket inhibitors of p38α.Bioorganic & medicinal chemistry letters, , Oct-01, Volume: 20, Issue:19, 2010
The design, synthesis, and evaluation of 8 hybrid DFG-out allosteric kinase inhibitors: a structural analysis of the binding interactions of Gleevec, Nexavar, and BIRB-796.Bioorganic & medicinal chemistry, , Aug-01, Volume: 18, Issue:15, 2010
Optimization of alpha-ketoamide based p38 inhibitors through modifications to the region that binds to the allosteric site.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 20, Issue:16, 2010
Displacement assay for the detection of stabilizers of inactive kinase conformations.Journal of medicinal chemistry, , Jan-14, Volume: 53, Issue:1, 2010
Discovery and characterization of the N-phenyl-N'-naphthylurea class of p38 kinase inhibitors.Bioorganic & medicinal chemistry letters, , May-01, Volume: 19, Issue:9, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The design and synthesis of novel alpha-ketoamide-based p38 MAP kinase inhibitors.Bioorganic & medicinal chemistry letters, , Mar-15, Volume: 18, Issue:6, 2008
Biphenyl amide p38 kinase inhibitors 4: DFG-in and DFG-out binding modes.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 18, Issue:15, 2008
Trimethylsilylpyrazoles as novel inhibitors of p38 MAP kinase: a new use of silicon bioisosteres in medicinal chemistry.Bioorganic & medicinal chemistry letters, , Jan-15, Volume: 17, Issue:2, 2007
Design, synthesis, and biological evaluation of phenylamino-substituted 6,11-dihydro-dibenzo[b,e]oxepin-11-ones and dibenzo[a,d]cycloheptan-5-ones: novel p38 MAP kinase inhibitors.Journal of medicinal chemistry, , Dec-28, Volume: 49, Issue:26, 2006
Features of selective kinase inhibitors.Chemistry & biology, , Volume: 12, Issue:6, 2005
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
The kinetics of binding to p38MAP kinase by analogues of BIRB 796.Bioorganic & medicinal chemistry letters, , Sep-15, Volume: 13, Issue:18, 2003
Thermal denaturation: a method to rank slow binding, high-affinity P38alpha MAP kinase inhibitors.Journal of medicinal chemistry, , Oct-23, Volume: 46, Issue:22, 2003
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site.Nature structural biology, , Volume: 9, Issue:4, 2002
Pyrazole urea-based inhibitors of p38 MAP kinase: from lead compound to clinical candidate.Journal of medicinal chemistry, , Jul-04, Volume: 45, Issue:14, 2002
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Kinase Inhibitors as Underexplored Antiviral Agents.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
[no title available]European journal of medicinal chemistry, , Apr-05, Volume: 215, 2021
Discovery of potent p38α MAPK inhibitors through a funnel like workflow combining in silico screening and in vitro validation.European journal of medicinal chemistry, , Nov-15, Volume: 182, 2019
Design and molecular modeling of novel P38α MAPK inhibitors targeting breast cancer, synthesized from oxygen heterocyclic natural compounds.Bioorganic & medicinal chemistry, , 04-01, Volume: 27, Issue:7, 2019
Pyridinylimidazoles as dual glycogen synthase kinase 3β/p38α mitogen-activated protein kinase inhibitors.European journal of medicinal chemistry, , Aug-01, Volume: 175, 2019
[no title available]European journal of medicinal chemistry, , Dec-01, Volume: 183, 2019
Synthesis and molecular docking studies of new furochromone derivatives as p38α MAPK inhibitors targeting human breast cancer MCF-7 cells.Bioorganic & medicinal chemistry, , 04-15, Volume: 25, Issue:8, 2017
Non-kinase targets of protein kinase inhibitors.Nature reviews. Drug discovery, , Volume: 16, Issue:6, 2017
[no title available]Journal of medicinal chemistry, , 10-12, Volume: 60, Issue:19, 2017
Syntheses and structure-activity relationships for some triazolyl p38α MAPK inhibitors.Bioorganic & medicinal chemistry letters, , Mar-01, Volume: 24, Issue:5, 2014
Metabolically stable dibenzo[b,e]oxepin-11(6H)-ones as highly selective p38 MAP kinase inhibitors: optimizing anti-cytokine activity in human whole blood.Journal of medicinal chemistry, , Nov-14, Volume: 56, Issue:21, 2013
Tri-substituted imidazole analogues of SB203580 as inducers for cardiomyogenesis of human embryonic stem cells.Bioorganic & medicinal chemistry letters, , Jun-01, Volume: 23, Issue:11, 2013
Dibenzosuberones as p38 mitogen-activated protein kinase inhibitors with low ATP competitiveness and outstanding whole blood activity.Journal of medicinal chemistry, , Jan-10, Volume: 56, Issue:1, 2013
Design, synthesis, and biological evaluation of novel disubstituted dibenzosuberones as highly potent and selective inhibitors of p38 mitogen activated protein kinase.Journal of medicinal chemistry, , Jun-28, Volume: 55, Issue:12, 2012
Targeting the hinge glycine flip and the activation loop: novel approach to potent p38α inhibitors.Journal of medicinal chemistry, , Sep-13, Volume: 55, Issue:17, 2012
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Indolin-2-one p38α inhibitors I: design, profiling and crystallographic binding mode.Bioorganic & medicinal chemistry letters, , Jul-15, Volume: 21, Issue:14, 2011
The Discovery of VX-745: A Novel and Selective p38α Kinase Inhibitor.ACS medicinal chemistry letters, , Oct-13, Volume: 2, Issue:10, 2011
One-pot synthesis of 4,6-diaryl-2-oxo(imino)-1,2-dihydropyridine-3-carbonitrile; a New Scaffold for p38alpha MAP kinase inhibition.Journal of combinatorial chemistry, , Jul-12, Volume: 12, Issue:4, 2010
Biochemical and biophysical characterization of unique switch pocket inhibitors of p38α.Bioorganic & medicinal chemistry letters, , Oct-01, Volume: 20, Issue:19, 2010
In silico search for multi-target anti-inflammatories in Chinese herbs and formulas.Bioorganic & medicinal chemistry, , Mar-15, Volume: 18, Issue:6, 2010
Optimization of alpha-ketoamide based p38 inhibitors through modifications to the region that binds to the allosteric site.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 20, Issue:16, 2010
Unexpected reaction of 2-alkylsulfanylimidazoles to imidazol-2-ones: pyridinylimidazol-2-ones as novel potent p38alpha mitogen-activated protein kinase inhibitors.Journal of medicinal chemistry, , Jun-24, Volume: 53, Issue:12, 2010
Through the "gatekeeper door": exploiting the active kinase conformation.Journal of medicinal chemistry, , Apr-08, Volume: 53, Issue:7, 2010
3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of p38alpha mitogen activated protein kinase and casein kinase 1delta.Journal of medicinal chemistry, , Dec-10, Volume: 52, Issue:23, 2009
Aza-analogue dibenzepinone scaffolds as p38 mitogen-activated protein kinase inhibitors: design, synthesis, and biological data of inhibitors with improved physicochemical properties.Journal of medicinal chemistry, , Mar-26, Volume: 52, Issue:6, 2009
Discovery of N-substituted pyridinones as potent and selective inhibitors of p38 kinase.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 19, Issue:20, 2009
Biphenyl amide p38 kinase inhibitors 1: Discovery and binding mode.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 18, Issue:1, 2008
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The design and synthesis of novel alpha-ketoamide-based p38 MAP kinase inhibitors.Bioorganic & medicinal chemistry letters, , Mar-15, Volume: 18, Issue:6, 2008
Design, synthesis, and biological evaluation of novel Tri- and tetrasubstituted imidazoles as highly potent and specific ATP-mimetic inhibitors of p38 MAP kinase: focus on optimized interactions with the enzyme's surface-exposed front region.Journal of medicinal chemistry, , Jul-24, Volume: 51, Issue:14, 2008
Isoxazolone based inhibitors of p38 MAP kinases.Journal of medicinal chemistry, , Apr-24, Volume: 51, Issue:8, 2008
Drugs designed to inhibit human p38 mitogen-activated protein kinase activation treat Toxoplasma gondii and Encephalitozoon cuniculi infection.Antimicrobial agents and chemotherapy, , Volume: 51, Issue:12, 2007
Synthesis, biological testing, and binding mode prediction of 6,9-diarylpurin-8-ones as p38 MAP kinase inhibitors.Journal of medicinal chemistry, , May-03, Volume: 50, Issue:9, 2007
From five- to six-membered rings: 3,4-diarylquinolinone as lead for novel p38MAP kinase inhibitors.Journal of medicinal chemistry, , Mar-22, Volume: 50, Issue:6, 2007
The development of novel C-2, C-8, and N-9 trisubstituted purines as inhibitors of TNF-alpha production.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 16, Issue:16, 2006
Design, synthesis, and biological evaluation of phenylamino-substituted 6,11-dihydro-dibenzo[b,e]oxepin-11-ones and dibenzo[a,d]cycloheptan-5-ones: novel p38 MAP kinase inhibitors.Journal of medicinal chemistry, , Dec-28, Volume: 49, Issue:26, 2006
Identification of novel p38alpha MAP kinase inhibitors using fragment-based lead generation.Journal of medicinal chemistry, , Jan-27, Volume: 48, Issue:2, 2005
Two classes of p38alpha MAP kinase inhibitors having a common diphenylether core but exhibiting divergent binding modes.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 15, Issue:23, 2005
Rapid computational identification of the targets of protein kinase inhibitors.Journal of medicinal chemistry, , Jun-16, Volume: 48, Issue:12, 2005
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
The molecular basis for coxib inhibition of p38alpha MAP kinase.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 15, Issue:15, 2005
Tetrasubstituted imidazole inhibitors of cytokine release: probing substituents in the N-1 position.Journal of medicinal chemistry, , Dec-02, Volume: 47, Issue:25, 2004
Development of orally bioavailable bicyclic pyrazolones as inhibitors of tumor necrosis factor-alpha production.Journal of medicinal chemistry, , May-20, Volume: 47, Issue:11, 2004
A novel series of p38 MAP kinase inhibitors for the potential treatment of rheumatoid arthritis.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 14, Issue:21, 2004
Novel, potent and selective anilinoquinazoline and anilinopyrimidine inhibitors of p38 MAP kinase.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 14, Issue:21, 2004
The development of new bicyclic pyrazole-based cytokine synthesis inhibitors.Bioorganic & medicinal chemistry letters, , Oct-04, Volume: 14, Issue:19, 2004
Benzimidazolone p38 inhibitors.Bioorganic & medicinal chemistry letters, , Feb-23, Volume: 14, Issue:4, 2004
Kinase inhibitors: not just for kinases anymore.Journal of medicinal chemistry, , Apr-10, Volume: 46, Issue:8, 2003
Novel substituted pyridinyl imidazoles as potent anticytokine agents with low activity against hepatic cytochrome P450 enzymes.Journal of medicinal chemistry, , Jul-17, Volume: 46, Issue:15, 2003
Synthesis and pharmacological characterization of a potent, orally active p38 kinase inhibitor.Bioorganic & medicinal chemistry letters, , Jun-17, Volume: 12, Issue:12, 2002
From imidazoles to pyrimidines: new inhibitors of cytokine release.Journal of medicinal chemistry, , Jun-20, Volume: 45, Issue:13, 2002
Identification of novel inhibitors of the transforming growth factor beta1 (TGF-beta1) type 1 receptor (ALK5).Journal of medicinal chemistry, , Feb-28, Volume: 45, Issue:5, 2002
Imidazole inhibitors of cytokine release: probing substituents in the 2 position.Journal of medicinal chemistry, , Oct-10, Volume: 45, Issue:21, 2002
Pyrazole urea-based inhibitors of p38 MAP kinase: from lead compound to clinical candidate.Journal of medicinal chemistry, , Jul-04, Volume: 45, Issue:14, 2002
p38 kinase inhibitors for the treatment of arthritis and osteoporosis: thienyl, furyl, and pyrrolyl ureas.Bioorganic & medicinal chemistry letters, , Jan-08, Volume: 11, Issue:1, 2001
Phenoxypyrimidine inhibitors of p38alpha kinase: synthesis and statistical evaluation of the p38 inhibitory potencies of a series of 1-(piperidin-4-yl)-4-(4-fluorophenyl)-5-(2-phenoxypyrimidin-4-yl) imidazoles.Bioorganic & medicinal chemistry letters, , May-07, Volume: 11, Issue:9, 2001
Discovery of a new class of p38 kinase inhibitors.Bioorganic & medicinal chemistry letters, , Sep-18, Volume: 10, Issue:18, 2000
1-Phenyl-5-pyrazolyl ureas: potent and selective p38 kinase inhibitors.Bioorganic & medicinal chemistry letters, , Sep-18, Volume: 10, Issue:18, 2000
Design and synthesis of potent, selective, and orally bioavailable tetrasubstituted imidazole inhibitors of p38 mitogen-activated protein kinase.Journal of medicinal chemistry, , Jun-17, Volume: 42, Issue:12, 1999
Structural basis of inhibitor selectivity in MAP kinases.Structure (London, England : 1993), , Sep-15, Volume: 6, Issue:9, 1998
Pyrroles and other heterocycles as inhibitors of p38 kinase.Bioorganic & medicinal chemistry letters, , Oct-06, Volume: 8, Issue:19, 1998
Potent inhibitors of the MAP kinase p38.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 8, Issue:23, 1998
1-substituted 4-aryl-5-pyridinylimidazoles: a new class of cytokine suppressive drugs with low 5-lipoxygenase and cyclooxygenase inhibitory potency.Journal of medicinal chemistry, , Sep-27, Volume: 39, Issue:20, 1996
[no title available],
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
[no title available]Journal of medicinal chemistry, , 11-11, Volume: 64, Issue:21, 2021
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Design and synthesis of potent 1,2,4-trisubstituted imidazolinone derivatives with dual p38αMAPK and ERK1/2 inhibitory activity.European journal of medicinal chemistry, , Apr-13, Volume: 94, 2015
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The design, synthesis, and evaluation of 8 hybrid DFG-out allosteric kinase inhibitors: a structural analysis of the binding interactions of Gleevec, Nexavar, and BIRB-796.Bioorganic & medicinal chemistry, , Aug-01, Volume: 18, Issue:15, 2010
Application of a novel [3+2] cycloaddition reaction to prepare substituted imidazoles and their use in the design of potent DFG-out allosteric B-Raf inhibitors.Bioorganic & medicinal chemistry, , Jan-01, Volume: 18, Issue:1, 2010
Displacement assay for the detection of stabilizers of inactive kinase conformations.Journal of medicinal chemistry, , Jan-14, Volume: 53, Issue:1, 2010
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The selectivity of protein kinase inhibitors: a further update.The Biochemical journal, , Dec-15, Volume: 408, Issue:3, 2007
Identification of genotype-correlated sensitivity to selective kinase inhibitors by using high-throughput tumor cell line profiling.Proceedings of the National Academy of Sciences of the United States of America, , Dec-11, Volume: 104, Issue:50, 2007
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Mapping the Efficiency and Physicochemical Trajectories of Successful Optimizations.Journal of medicinal chemistry, , 08-09, Volume: 61, Issue:15, 2018
Displacement assay for the detection of stabilizers of inactive kinase conformations.Journal of medicinal chemistry, , Jan-14, Volume: 53, Issue:1, 2010
Rational design of inhibitors that bind to inactive kinase conformations.Nature chemical biology, , Volume: 2, Issue:7, 2006
General model for estimation of the inhibition of protein kinases using Monte Carlo simulations.Journal of medicinal chemistry, , May-06, Volume: 47, Issue:10, 2004
The kinetics of binding to p38MAP kinase by analogues of BIRB 796.Bioorganic & medicinal chemistry letters, , Sep-15, Volume: 13, Issue:18, 2003
Thermal denaturation: a method to rank slow binding, high-affinity P38alpha MAP kinase inhibitors.Journal of medicinal chemistry, , Oct-23, Volume: 46, Issue:22, 2003
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site.Nature structural biology, , Volume: 9, Issue:4, 2002
Pyrazole urea-based inhibitors of p38 MAP kinase: from lead compound to clinical candidate.Journal of medicinal chemistry, , Jul-04, Volume: 45, Issue:14, 2002
Novel and potent transforming growth factor beta type I receptor kinase domain inhibitor: 7-amino 4-(2-pyridin-2-yl-5,6-dihydro-4H-pyrrolo[1,2-b]pyrazol-3-yl)-quinolines.Bioorganic & medicinal chemistry letters, , Jul-05, Volume: 14, Issue:13, 2004
Synthesis and activity of new aryl- and heteroaryl-substituted pyrazole inhibitors of the transforming growth factor-beta type I receptor kinase domain.Journal of medicinal chemistry, , Sep-11, Volume: 46, Issue:19, 2003
A Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Assay Identifies Nilotinib as an Inhibitor of Inflammation in Acute Myeloid Leukemia.Journal of medicinal chemistry, , 09-22, Volume: 65, Issue:18, 2022
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of 2-((3-Amino-4-methylphenyl)amino)-N-(2-methyl-5-(3-(trifluoromethyl)benzamido)phenyl)-4-(methylamino)pyrimidine-5-carboxamide (CHMFL-ABL-053) as a Potent, Selective, and Orally Available BCR-ABL/SRC/p38 Kinase Inhibitor for Chronic Myeloid LeJournal of medicinal chemistry, , Mar-10, Volume: 59, Issue:5, 2016
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
N-(3-Cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)amides as potent, selective, inhibitors of JNK2 and JNK3.Bioorganic & medicinal chemistry letters, , Mar-01, Volume: 17, Issue:5, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
[no title available]Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Why Some Targets Benefit from beyond Rule of Five Drugs.Journal of medicinal chemistry, , 11-27, Volume: 62, Issue:22, 2019
Design, synthesis and biological evaluation of novel benzimidazole amidines as potent multi-target inhibitors for the treatment of non-small cell lung cancer.European journal of medicinal chemistry, , Jan-01, Volume: 143, 2018
Selectivity data: assessment, predictions, concordance, and implications.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
A new target for an old drug: identifying mitoxantrone as a nanomolar inhibitor of PIM1 kinase via kinome-wide selectivity modeling.Journal of medicinal chemistry, , Mar-28, Volume: 56, Issue:6, 2013
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The Discovery of VX-745: A Novel and Selective p38α Kinase Inhibitor.ACS medicinal chemistry letters, , Oct-13, Volume: 2, Issue:10, 2011
Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders.Journal of medicinal chemistry, , Mar-25, Volume: 53, Issue:6, 2010
Discovery of N-substituted pyridinones as potent and selective inhibitors of p38 kinase.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 19, Issue:20, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The design and synthesis of novel alpha-ketoamide-based p38 MAP kinase inhibitors.Bioorganic & medicinal chemistry letters, , Mar-15, Volume: 18, Issue:6, 2008
The development of novel C-2, C-8, and N-9 trisubstituted purines as inhibitors of TNF-alpha production.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 16, Issue:16, 2006
p38 MAP kinase inhibitors. Part 6: 2-arylpyridazin-3-ones as templates for inhibitor design.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 16, Issue:22, 2006
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Hybrid-designed inhibitors of p38 MAP kinase utilizing N-arylpyridazinones.Journal of medicinal chemistry, , Jan-30, Volume: 46, Issue:3, 2003
Synthesis and structure-activity relationship of aminobenzophenones. A novel class of p38 MAP kinase inhibitors with high antiinflammatory activity.Journal of medicinal chemistry, , Dec-18, Volume: 46, Issue:26, 2003
[no title available],
[no title available]European journal of medicinal chemistry, , Dec-01, Volume: 183, 2019
Design, synthesis and biological evaluation of novel benzimidazole amidines as potent multi-target inhibitors for the treatment of non-small cell lung cancer.European journal of medicinal chemistry, , Jan-01, Volume: 143, 2018
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of 2-((3-Amino-4-methylphenyl)amino)-N-(2-methyl-5-(3-(trifluoromethyl)benzamido)phenyl)-4-(methylamino)pyrimidine-5-carboxamide (CHMFL-ABL-053) as a Potent, Selective, and Orally Available BCR-ABL/SRC/p38 Kinase Inhibitor for Chronic Myeloid LeJournal of medicinal chemistry, , Mar-10, Volume: 59, Issue:5, 2016
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Hybrid compound design to overcome the gatekeeper T338M mutation in cSrc.Journal of medicinal chemistry, , Jul-09, Volume: 52, Issue:13, 2009
A new screening assay for allosteric inhibitors of cSrc.Nature chemical biology, , Volume: 5, Issue:6, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
2-aminothiazole as a novel kinase inhibitor template. Structure-activity relationship studies toward the discovery of N-(2-chloro-6-methylphenyl)-2-[[6-[4-(2-hydroxyethyl)-1- piperazinyl)]-2-methyl-4-pyrimidinyl]amino)]-1,3-thiazole-5-carboxamide (dasatinJournal of medicinal chemistry, , Nov-16, Volume: 49, Issue:23, 2006
Discovery of N-(2-chloro-6-methyl- phenyl)-2-(6-(4-(2-hydroxyethyl)- piperazin-1-yl)-2-methylpyrimidin-4- ylamino)thiazole-5-carboxamide (BMS-354825), a dual Src/Abl kinase inhibitor with potent antitumor activity in preclinical assays.Journal of medicinal chemistry, , Dec-30, Volume: 47, Issue:27, 2004
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.Proceedings of the National Academy of Sciences of the United States of America, , Dec-18, Volume: 104, Issue:51, 2007
Novel substituted pyridinyl imidazoles as potent anticytokine agents with low activity against hepatic cytochrome P450 enzymes.Journal of medicinal chemistry, , Jul-17, Volume: 46, Issue:15, 2003
A Casein kinase 1/Checkpoint kinase 1 pyrazolo-pyridine protein kinase inhibitor as novel activator of the p53 pathway.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 23, Issue:20, 2013
3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of p38alpha mitogen activated protein kinase and casein kinase 1delta.Journal of medicinal chemistry, , Dec-10, Volume: 52, Issue:23, 2009
The selectivity of protein kinase inhibitors: a further update.The Biochemical journal, , Dec-15, Volume: 408, Issue:3, 2007
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.Proceedings of the National Academy of Sciences of the United States of America, , Dec-18, Volume: 104, Issue:51, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of N-phenyl-4-(thiazol-5-yl)pyrimidin-2-amine aurora kinase inhibitors.Journal of medicinal chemistry, , Jun-10, Volume: 53, Issue:11, 2010
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
High-Throughput Screening Platform in Postnatal Heart Cells and Chemical Probe Toolbox to Assess Cardiomyocyte Proliferation.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Elements and modulation of functional dynamics.Journal of medicinal chemistry, , Oct-09, Volume: 57, Issue:19, 2014
The Discovery of VX-745: A Novel and Selective p38α Kinase Inhibitor.ACS medicinal chemistry letters, , Oct-13, Volume: 2, Issue:10, 2011
Synthesis, crystal structure, and activity of pyrazole-based inhibitors of p38 kinase.Journal of medicinal chemistry, , Nov-15, Volume: 50, Issue:23, 2007
Synthesis and structure-activity relationship of aminobenzophenones. A novel class of p38 MAP kinase inhibitors with high antiinflammatory activity.Journal of medicinal chemistry, , Dec-18, Volume: 46, Issue:26, 2003
Phenoxypyrimidine inhibitors of p38alpha kinase: synthesis and statistical evaluation of the p38 inhibitory potencies of a series of 1-(piperidin-4-yl)-4-(4-fluorophenyl)-5-(2-phenoxypyrimidin-4-yl) imidazoles.Bioorganic & medicinal chemistry letters, , May-07, Volume: 11, Issue:9, 2001
The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase.Chemistry & biology, , Volume: 4, Issue:6, 1997
Benzimidazolone p38 inhibitors.Bioorganic & medicinal chemistry letters, , Feb-23, Volume: 14, Issue:4, 2004
Imidazopyrimidines, potent inhibitors of p38 MAP kinase.Bioorganic & medicinal chemistry letters, , Feb-10, Volume: 13, Issue:3, 2003
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[no title available],
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Synthesis and biological evaluation of 5-(fluoro-substituted-6-methylpyridin-2-yl)-4-([1,2,4]triazolo[1,5-a]pyridin-6-yl)imidazoles as inhibitors of transforming growth factor-β type I receptor kinase.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 25, Issue:22, 2015
Discovery of N-((4-([1,2,4]triazolo[1,5-a]pyridin-6-yl)-5-(6-methylpyridin-2-yl)-1H-imidazol-2-yl)methyl)-2-fluoroaniline (EW-7197): a highly potent, selective, and orally bioavailable inhibitor of TGF-β type I receptor kinase as cancer immunotherapeutic/Journal of medicinal chemistry, , May-22, Volume: 57, Issue:10, 2014
4-([1,2,4]Triazolo[1,5-a]pyridin-6-yl)-5(3)-(6-methylpyridin-2-yl)imidazole and -pyrazole derivatives as potent and selective inhibitors of transforming growth factor-β type I receptor kinase.Bioorganic & medicinal chemistry, , May-01, Volume: 22, Issue:9, 2014
Synthesis and biological evaluation of 2-benzylamino-4(5)-(6-methylpyridin-2-yl)-5(4)-([1,2,4]triazolo[1,5-a]-pyridin-6-yl)thiazoles as transforming growth factor-β type 1 receptor kinase inhibitors.European journal of medicinal chemistry, , Volume: 57, 2012
Synthesis and biological evaluation of 1-substituted-3(5)-(6-methylpyridin-2-yl)-4-(quinolin-6-yl)pyrazoles as transforming growth factor-β type 1 receptor kinase inhibitors.Bioorganic & medicinal chemistry, , Apr-15, Volume: 19, Issue:8, 2011
Biphenyl amide p38 kinase inhibitors 4: DFG-in and DFG-out binding modes.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 18, Issue:15, 2008
Benzimidazolone p38 inhibitors.Bioorganic & medicinal chemistry letters, , Feb-23, Volume: 14, Issue:4, 2004
Pyrimidinylimidazole inhibitors of p38: cyclic N-1 imidazole substituents enhance p38 kinase inhibition and oral activity.Bioorganic & medicinal chemistry letters, , Nov-05, Volume: 11, Issue:21, 2001
Mapping the Efficiency and Physicochemical Trajectories of Successful Optimizations.Journal of medicinal chemistry, , 08-09, Volume: 61, Issue:15, 2018
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Design and synthesis of piperazine-indole p38 alpha MAP kinase inhibitors with improved pharmacokinetic profiles.Bioorganic & medicinal chemistry letters, , Feb-01, Volume: 20, Issue:3, 2010
Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders.Journal of medicinal chemistry, , Mar-25, Volume: 53, Issue:6, 2010
Displacement assay for the detection of stabilizers of inactive kinase conformations.Journal of medicinal chemistry, , Jan-14, Volume: 53, Issue:1, 2010
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Phenoxypyrimidine inhibitors of p38alpha kinase: synthesis and statistical evaluation of the p38 inhibitory potencies of a series of 1-(piperidin-4-yl)-4-(4-fluorophenyl)-5-(2-phenoxypyrimidin-4-yl) imidazoles.Bioorganic & medicinal chemistry letters, , May-07, Volume: 11, Issue:9, 2001
Pyrimidinylimidazole inhibitors of CSBP/p38 kinase demonstrating decreased inhibition of hepatic cytochrome P450 enzymes.Bioorganic & medicinal chemistry letters, , Nov-17, Volume: 8, Issue:22, 1998
1-substituted 4-aryl-5-pyridinylimidazoles: a new class of cytokine suppressive drugs with low 5-lipoxygenase and cyclooxygenase inhibitory potency.Journal of medicinal chemistry, , Sep-27, Volume: 39, Issue:20, 1996
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Prevention of organ allograft rejection by a specific Janus kinase 3 inhibitor.Science (New York, N.Y.), , Oct-31, Volume: 302, Issue:5646, 2003
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
[no title available]European journal of medicinal chemistry, , Apr-05, Volume: 215, 2021
Structure-based design, synthesis, and biological evaluation of imidazo[1,2-b]pyridazine-based p38 MAP kinase inhibitors.Bioorganic & medicinal chemistry, , 02-01, Volume: 26, Issue:3, 2018
Novel inhibitor of p38 MAP kinase as an anti-TNF-alpha drug: discovery of N-[4-[2-ethyl-4-(3-methylphenyl)-1,3-thiazol-5-yl]-2-pyridyl]benzamide (TAK-715) as a potent and orally active anti-rheumatoid arthritis agent.Journal of medicinal chemistry, , Sep-22, Volume: 48, Issue:19, 2005
Substituted 3-imidazo[1,2-a]pyridin-3-yl- 4-(1,2,3,4-tetrahydro-[1,4]diazepino-[6,7,1-hi]indol-7-yl)pyrrole-2,5-diones as highly selective and potent inhibitors of glycogen synthase kinase-3.Journal of medicinal chemistry, , Jul-29, Volume: 47, Issue:16, 2004
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Synthesis and evaluation of the epithelial-to- mesenchymal inhibitory activity of indazole-derived imidazoles as dual ALK5/p38α MAP inhibitors.European journal of medicinal chemistry, , Apr-15, Volume: 216, 2021
Synthesis and evaluation of the HIF-1α inhibitory activity of 3(5)-substituted-4-(quinolin-4-yl)- and 4-(2-phenylpyridin-4-yl)pyrazoles as inhibitors of ALK5.Bioorganic & medicinal chemistry letters, , 01-15, Volume: 30, Issue:2, 2020
Design, synthesis, and antifibrosis evaluation of 4-(benzo-[c][1,2,5]thiadiazol-5-yl)-3(5)-(6-methyl- pyridin-2-yl)pyrazole and 3(5)-(6-methylpyridin- 2-yl)-4-(thieno-[3,2,-c]pyridin-2-yl)pyrazole derivatives.European journal of medicinal chemistry, , Oct-15, Volume: 180, 2019
Synthesis and biological evaluation of novel benzo[c][1,2,5]thiadiazol-5-yl and thieno[3,2-c]- pyridin-2-yl imidazole derivatives as ALK5 inhibitors.Bioorganic & medicinal chemistry letters, , 08-15, Volume: 29, Issue:16, 2019
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Synthesis and biological evaluation of 5-(fluoro-substituted-6-methylpyridin-2-yl)-4-([1,2,4]triazolo[1,5-a]pyridin-6-yl)imidazoles as inhibitors of transforming growth factor-β type I receptor kinase.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 25, Issue:22, 2015
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery of potent p38α MAPK inhibitors through a funnel like workflow combining in silico screening and in vitro validation.European journal of medicinal chemistry, , Nov-15, Volume: 182, 2019
Biphenyl amide p38 kinase inhibitors 1: Discovery and binding mode.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 18, Issue:1, 2008
Biphenyl amide p38 kinase inhibitors 2: Optimisation and SAR.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 18, Issue:1, 2008
Biphenyl amide p38 kinase inhibitors 4: DFG-in and DFG-out binding modes.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 18, Issue:15, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes.Journal of medicinal chemistry, , Oct-22, Volume: 52, Issue:20, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders.Journal of medicinal chemistry, , Mar-25, Volume: 53, Issue:6, 2010
Discovery of potent p38α MAPK inhibitors through a funnel like workflow combining in silico screening and in vitro validation.European journal of medicinal chemistry, , Nov-15, Volume: 182, 2019
Discovery of 4-(5-(cyclopropylcarbamoyl)-2-methylphenylamino)-5-methyl-N-propylpyrrolo[1,2-f][1,2,4]triazine-6-carboxamide (BMS-582949), a clinical p38α MAP kinase inhibitor for the treatment of inflammatory diseases.Journal of medicinal chemistry, , Sep-23, Volume: 53, Issue:18, 2010
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Identification of genotype-correlated sensitivity to selective kinase inhibitors by using high-throughput tumor cell line profiling.Proceedings of the National Academy of Sciences of the United States of America, , Dec-11, Volume: 104, Issue:50, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazoles: identification of a potent Aurora kinase inhibitor with a favorable antitumor kinase inhibition profile.Journal of medicinal chemistry, , Nov-30, Volume: 49, Issue:24, 2006
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders.Journal of medicinal chemistry, , Mar-25, Volume: 53, Issue:6, 2010
p38alpha mitogen-activated protein kinase inhibitors: optimization of a series of biphenylamides to give a molecule suitable for clinical progression.Journal of medicinal chemistry, , Oct-22, Volume: 52, Issue:20, 2009
Fibrogenic Disorders in Human Diseases: From Inflammation to Organ Dysfunction.Journal of medicinal chemistry, , 11-21, Volume: 61, Issue:22, 2018
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of CC-930, an orally active anti-fibrotic JNK inhibitor.Bioorganic & medicinal chemistry letters, , Feb-01, Volume: 22, Issue:3, 2012
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Inhibition of colony-stimulating-factor-1 signaling in vivo with the orally bioavailable cFMS kinase inhibitor GW2580.Proceedings of the National Academy of Sciences of the United States of America, , Nov-01, Volume: 102, Issue:44, 2005
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Design and synthesis of novel human epidermal growth factor receptor 2 (HER2)/epidermal growth factor receptor (EGFR) dual inhibitors bearing a pyrrolo[3,2-d]pyrimidine scaffold.Journal of medicinal chemistry, , Dec-08, Volume: 54, Issue:23, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Structure based drug design of crizotinib (PF-02341066), a potent and selective dual inhibitor of mesenchymal-epithelial transition factor (c-MET) kinase and anaplastic lymphoma kinase (ALK).Journal of medicinal chemistry, , Sep-22, Volume: 54, Issue:18, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
AMG 706, an oral, multikinase inhibitor that selectively targets vascular endothelial growth factor, platelet-derived growth factor, and kit receptors, potently inhibits angiogenesis and induces regression in tumor xenografts.Cancer research, , Sep-01, Volume: 66, Issue:17, 2006
Discovery of N-((4-([1,2,4]triazolo[1,5-a]pyridin-6-yl)-5-(6-methylpyridin-2-yl)-1H-imidazol-2-yl)methyl)-2-fluoroaniline (EW-7197): a highly potent, selective, and orally bioavailable inhibitor of TGF-β type I receptor kinase as cancer immunotherapeutic/Journal of medicinal chemistry, , May-22, Volume: 57, Issue:10, 2014
4-([1,2,4]Triazolo[1,5-a]pyridin-6-yl)-5(3)-(6-methylpyridin-2-yl)imidazole and -pyrazole derivatives as potent and selective inhibitors of transforming growth factor-β type I receptor kinase.Bioorganic & medicinal chemistry, , May-01, Volume: 22, Issue:9, 2014
Synthesis and biological evaluation of 2-benzylamino-4(5)-(6-methylpyridin-2-yl)-5(4)-([1,2,4]triazolo[1,5-a]-pyridin-6-yl)thiazoles as transforming growth factor-β type 1 receptor kinase inhibitors.European journal of medicinal chemistry, , Volume: 57, 2012
Synthesis and biological evaluation of 1-substituted-3(5)-(6-methylpyridin-2-yl)-4-(quinoxalin-6-yl)pyrazoles as transforming growth factor-β type 1 receptor kinase inhibitors.European journal of medicinal chemistry, , Volume: 46, Issue:9, 2011
Synthesis and biological evaluation of 1-substituted-3(5)-(6-methylpyridin-2-yl)-4-(quinolin-6-yl)pyrazoles as transforming growth factor-β type 1 receptor kinase inhibitors.Bioorganic & medicinal chemistry, , Apr-15, Volume: 19, Issue:8, 2011
Synthesis and biological evaluation of trisubstituted imidazole derivatives as inhibitors of p38alpha mitogen-activated protein kinase.Bioorganic & medicinal chemistry letters, , Jul-15, Volume: 18, Issue:14, 2008
Ligand-protein interactions of selective casein kinase 1δ inhibitors.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
Structural basis for the interaction between casein kinase 1 delta and a potent and selective inhibitor.Journal of medicinal chemistry, , Jan-26, Volume: 55, Issue:2, 2012
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Discovery, synthesis, and in vivo activity of a new class of pyrazoloquinazolines as selective inhibitors of aurora B kinase.Journal of medicinal chemistry, , May-03, Volume: 50, Issue:9, 2007
Discovery of 6-(2,4-difluorophenoxy)-2-[3-hydroxy-1-(2-hydroxyethyl)propylamino]-8-methyl-8H-pyrido[2,3-d]pyrimidin-7-one (pamapimod) and 6-(2,4-difluorophenoxy)-8-methyl-2-(tetrahydro-2H-pyran-4-ylamino)pyrido[2,3-d]pyrimidin-7(8H)-one (R1487) as orally Journal of medicinal chemistry, , Apr-14, Volume: 54, Issue:7, 2011
Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders.Journal of medicinal chemistry, , Mar-25, Volume: 53, Issue:6, 2010
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Identification of N,1,4,4-tetramethyl-8-{[4-(4-methylpiperazin-1-yl)phenyl]amino}-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide (PHA-848125), a potent, orally available cyclin dependent kinase inhibitor.Journal of medicinal chemistry, , Aug-27, Volume: 52, Issue:16, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
[no title available]Journal of medicinal chemistry, , 10-12, Volume: 60, Issue:19, 2017
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of PH-797804, a highly selective and potent inhibitor of p38 MAP kinase.Bioorganic & medicinal chemistry letters, , Jul-01, Volume: 21, Issue:13, 2011
Substituted N-aryl-6-pyrimidinones: a new class of potent, selective, and orally active p38 MAP kinase inhibitors.Bioorganic & medicinal chemistry letters, , Jul-01, Volume: 21, Issue:13, 2011
Discovery of 5-substituted-N-arylpyridazinones as inhibitors of p38 MAP kinase.Bioorganic & medicinal chemistry letters, , May-15, Volume: 20, Issue:10, 2010
Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders.Journal of medicinal chemistry, , Mar-25, Volume: 53, Issue:6, 2010
[no title available]European journal of medicinal chemistry, , Apr-05, Volume: 215, 2021
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of N-(4-(2-amino-3-chloropyridin-4-yloxy)-3-fluorophenyl)-4-ethoxy-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide (BMS-777607), a selective and orally efficacious inhibitor of the Met kinase superfamily.Journal of medicinal chemistry, , Mar-12, Volume: 52, Issue:5, 2009
Homogeneous Assay for Target Engagement Utilizing Bioluminescent Thermal Shift.ACS medicinal chemistry letters, , Jun-14, Volume: 9, Issue:6, 2018
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of potent p38α MAPK inhibitors through a funnel like workflow combining in silico screening and in vitro validation.European journal of medicinal chemistry, , Nov-15, Volume: 182, 2019
p38alpha mitogen-activated protein kinase inhibitors: optimization of a series of biphenylamides to give a molecule suitable for clinical progression.Journal of medicinal chemistry, , Oct-22, Volume: 52, Issue:20, 2009
Biphenyl amide p38 kinase inhibitors 3: Improvement of cellular and in vivo activity.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 18, Issue:15, 2008
Biphenyl amide p38 kinase inhibitors 4: DFG-in and DFG-out binding modes.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 18, Issue:15, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of Entrectinib: A New 3-Aminoindazole As a Potent Anaplastic Lymphoma Kinase (ALK), c-ros Oncogene 1 Kinase (ROS1), and Pan-Tropomyosin Receptor Kinases (Pan-TRKs) inhibitor.Journal of medicinal chemistry, , Apr-14, Volume: 59, Issue:7, 2016
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
[no title available]Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Dibenzosuberones as p38 mitogen-activated protein kinase inhibitors with low ATP competitiveness and outstanding whole blood activity.Journal of medicinal chemistry, , Jan-10, Volume: 56, Issue:1, 2013
Design, synthesis, and biological evaluation of novel disubstituted dibenzosuberones as highly potent and selective inhibitors of p38 mitogen activated protein kinase.Journal of medicinal chemistry, , Jun-28, Volume: 55, Issue:12, 2012
[no title available],
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Optimization of 6,6-dimethyl pyrrolo[3,4-c]pyrazoles: Identification of PHA-793887, a potent CDK inhibitor suitable for intravenous dosing.Bioorganic & medicinal chemistry, , Mar-01, Volume: 18, Issue:5, 2010
Synthesis and evaluation of the epithelial-to- mesenchymal inhibitory activity of indazole-derived imidazoles as dual ALK5/p38α MAP inhibitors.European journal of medicinal chemistry, , Apr-15, Volume: 216, 2021
Design, synthesis, and antifibrosis evaluation of 4-(benzo-[c][1,2,5]thiadiazol-5-yl)-3(5)-(6-methyl- pyridin-2-yl)pyrazole and 3(5)-(6-methylpyridin- 2-yl)-4-(thieno-[3,2,-c]pyridin-2-yl)pyrazole derivatives.European journal of medicinal chemistry, , Oct-15, Volume: 180, 2019
Synthesis and biological evaluation of novel benzo[c][1,2,5]thiadiazol-5-yl and thieno[3,2-c]- pyridin-2-yl imidazole derivatives as ALK5 inhibitors.Bioorganic & medicinal chemistry letters, , 08-15, Volume: 29, Issue:16, 2019
Synthesis and biological evaluation of 5-(fluoro-substituted-6-methylpyridin-2-yl)-4-([1,2,4]triazolo[1,5-a]pyridin-6-yl)imidazoles as inhibitors of transforming growth factor-β type I receptor kinase.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 25, Issue:22, 2015
Discovery of N-((4-([1,2,4]triazolo[1,5-a]pyridin-6-yl)-5-(6-methylpyridin-2-yl)-1H-imidazol-2-yl)methyl)-2-fluoroaniline (EW-7197): a highly potent, selective, and orally bioavailable inhibitor of TGF-β type I receptor kinase as cancer immunotherapeutic/Journal of medicinal chemistry, , May-22, Volume: 57, Issue:10, 2014
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Enables
This protein enables 10 target(s):
Target | Category | Definition |
protein serine/threonine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925] |
MAP kinase activity | molecular function | Catalysis of the reaction: protein + ATP = protein phosphate + ADP. This reaction is the phosphorylation of proteins. Mitogen-activated protein kinase; a family of protein kinases that perform a crucial step in relaying signals from the plasma membrane to the nucleus. They are activated by a wide range of proliferation- or differentiation-inducing signals; activation is strong with agonists such as polypeptide growth factors and tumor-promoting phorbol esters, but weak (in most cell backgrounds) by stress stimuli. [GOC:ma, ISBN:0198547684] |
MAP kinase kinase activity | molecular function | Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in a MAP kinase (MAPK) substrate. [ISBN:0198547684] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
protein phosphatase binding | molecular function | Binding to a protein phosphatase. [GOC:jl] |
mitogen-activated protein kinase p38 binding | molecular function | Binding to mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation. [GOC:curators, PMID:17827184] |
NFAT protein binding | molecular function | Binding to NFAT (nuclear factor of activated T cells) proteins, a family of transcription factors. NFAT proteins have crucial roles in the development and function of the immune system. [PMID:15928679] |
protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
Located In
This protein is located in 11 target(s):
Target | Category | Definition |
spindle pole | cellular component | Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules. [GOC:clt] |
extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
nuclear speck | cellular component | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. [http://www.cellnucleus.com/] |
secretory granule lumen | cellular component | The volume enclosed by the membrane of a secretory granule. [GOC:rph] |
glutamatergic synapse | cellular component | A synapse that uses glutamate as a neurotransmitter. [GOC:dos] |
ficolin-1-rich granule lumen | cellular component | Any membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
Active In
This protein is active in 3 target(s):
Target | Category | Definition |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Involved In
This protein is involved in 64 target(s):
Target | Category | Definition |
DNA damage checkpoint signaling | biological process | A signal transduction process that contributes to a DNA damage checkpoint. [GOC:mah] |
cell morphogenesis | biological process | The developmental process in which the size or shape of a cell is generated and organized. [GOC:clt, GOC:dph, GOC:go_curators, GOC:tb] |
cartilage condensation | biological process | The condensation of mesenchymal cells that have been committed to differentiate into chondrocytes. [ISBN:0878932437] |
angiogenesis | biological process | Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels. [ISBN:0878932453] |
osteoblast differentiation | biological process | The process whereby a relatively unspecialized cell acquires the specialized features of an osteoblast, a mesodermal or neural crest cell that gives rise to bone. [CL:0000062, GO_REF:0000034, GOC:jid] |
placenta development | biological process | The process whose specific outcome is the progression of the placenta over time, from its formation to the mature structure. The placenta is an organ of metabolic interchange between fetus and mother, partly of embryonic origin and partly of maternal origin. [GOC:add, ISBN:068340007X] |
response to dietary excess | biological process | The physiological process in which dietary excess is sensed by the central nervous system, resulting in a reduction in food intake and increased energy expenditure. [GOC:pg, GOC:pr, PMID:12161655] |
chondrocyte differentiation | biological process | The process in which a chondroblast acquires specialized structural and/or functional features of a chondrocyte. A chondrocyte is a polymorphic cell that forms cartilage. [GOC:dph] |
negative regulation of inflammatory response to antigenic stimulus | biological process | Any process that stops, prevents, or reduces the frequency, rate, or extent of an inflammatory response to an antigenic stimulus. [GOC:add] |
glucose metabolic process | biological process | The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. [ISBN:0198506732] |
regulation of transcription by RNA polymerase II | biological process | Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II. [GOC:go_curators, GOC:txnOH] |
transcription by RNA polymerase II | biological process | The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs). [GOC:jl, GOC:txnOH, ISBN:0321000382] |
apoptotic process | biological process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263] |
chemotaxis | biological process | The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). [ISBN:0198506732] |
signal transduction | biological process | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11] |
cell surface receptor signaling pathway | biological process | The series of molecular signals initiated by an extracellular ligand binding to a receptor located on the cell surface. The pathway ends with regulation of a downstream cellular process, e.g. transcription. [GOC:signaling] |
cell surface receptor protein serine/threonine kinase signaling pathway | biological process | The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses serine/threonine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling] |
skeletal muscle tissue development | biological process | The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are: the fusion of myoblasts to form myotubes that increase in size by further fusion to them of myoblasts, the formation of myofibrils within their cytoplasm and the establishment of functional neuromuscular junctions with motor neurons. At this stage they can be regarded as mature muscle fibers. [GOC:mtg_muscle] |
positive regulation of gene expression | biological process | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). [GOC:txnOH-2018] |
positive regulation of myotube differentiation | biological process | Any process that activates, maintains or increases the frequency, rate or extent of myotube differentiation. Myotube differentiation is the process in which a relatively unspecialized cell acquires specialized features of a myotube cell. Myotubes are multinucleated cells that are formed when proliferating myoblasts exit the cell cycle, differentiate and fuse. [GOC:dph, GOC:tb] |
peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |
fatty acid oxidation | biological process | The removal of one or more electrons from a fatty acid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. [ISBN:0198506732, MetaCyc:FAO-PWY] |
platelet activation | biological process | A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. [http://www.graylab.ac.uk/omd/] |
regulation of ossification | biological process | Any process that modulates the frequency, rate or extent of ossification, the formation of bone or of a bony substance or the conversion of fibrous tissue or of cartilage into bone or a bony substance. [GOC:go_curators] |
osteoclast differentiation | biological process | The process in which a relatively unspecialized monocyte acquires the specialized features of an osteoclast. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue. [CL:0000092, GOC:add, ISBN:0781735149, PMID:12161749] |
stress-activated protein kinase signaling cascade | biological process | The series of molecular signals in which a stress-activated protein kinase (SAPK) cascade relays a signal. [GOC:mah] |
positive regulation of cyclase activity | biological process | Any process that activates or increases the activity of a cyclase. [GOC:mah] |
lipopolysaccharide-mediated signaling pathway | biological process | The series of molecular signals initiated by the binding of a lipopolysaccharide (LPS) to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. Lipopolysaccharides are major components of the outer membrane of Gram-negative bacteria, making them prime targets for recognition by the immune system. [GOC:mah, GOC:signaling, PMID:15379975] |
response to muramyl dipeptide | biological process | Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan. [GOC:add] |
positive regulation of interleukin-12 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-12 production. [GOC:mah] |
response to insulin | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. [GOC:mah, ISBN:0198506732] |
negative regulation of hippo signaling | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of hippo signaling. [GOC:bf] |
intracellular signal transduction | biological process | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. [GOC:bf, GOC:jl, GOC:signaling, ISBN:3527303782] |
cellular response to vascular endothelial growth factor stimulus | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vascular endothelial growth factor stimulus. [GOC:BHF, GOC:rl, PMID:18440775] |
response to muscle stretch | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a myofibril being extended beyond its slack length. [GOC:BHF, GOC:vk, PMID:14583192] |
p38MAPK cascade | biological process | A MAPK cascade containing at least the p38MAPK (MAPK14) MAP kinase, or Hog1 in yeast. It starts with the activation of a MAP3K, and the consecutive activation of a MPK2K and of p38MAPK. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier. The p38MAPK cascade is activated by stress signals, including hyperosmolarity, as well as by G protein-coupled receptors, growth factors, and cytokines, and results in cellular responses such as cell proliferation, cell differentiation, apoptosis and inflammation. [PMID:20811974, PMID:23125017, PMID:32794416] |
positive regulation of protein import into nucleus | biological process | Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus. [GOC:jl] |
signal transduction in response to DNA damage | biological process | A cascade of processes induced by the detection of DNA damage within a cell. [GOC:go_curators] |
positive regulation of erythrocyte differentiation | biological process | Any process that activates or increases the frequency, rate or extent of erythrocyte differentiation. [GOC:go_curators] |
positive regulation of myoblast differentiation | biological process | Any process that activates or increases the frequency, rate or extent of myoblast differentiation. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers. [CL:0000056, GOC:go_curators, GOC:mtg_muscle] |
positive regulation of transcription by RNA polymerase II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
glucose import | biological process | The directed movement of the hexose monosaccharide glucose into a cell or organelle. [GOC:ai] |
positive regulation of glucose import | biological process | Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. [GOC:ai, GOC:dph, GOC:tb] |
vascular endothelial growth factor receptor signaling pathway | biological process | The series of molecular signals initiated by a ligand binding to a vascular endothelial growth factor receptor (VEGFR) on the surface of the target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:ceb, GOC:signaling] |
stem cell differentiation | biological process | The process in which a relatively unspecialized cell acquires specialized features of a stem cell. A stem cell is a cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized cells. [CL:0000034, GOC:isa_complete] |
striated muscle cell differentiation | biological process | The process in which a relatively unspecialized cell acquires specialized features of a striated muscle cell; striated muscle fibers are divided by transverse bands into striations, and cardiac and voluntary muscle are types of striated muscle. [CL:0000737, GOC:ai] |
positive regulation of muscle cell differentiation | biological process | Any process that activates or increases the frequency, rate or extent of muscle cell differentiation. [CL:0000187, GOC:ai] |
stress-activated MAPK cascade | biological process | A MAPK cascade that starts with the activation of a stress-activated MAP kinase cascade. [GOC:ai, PMID:15936270] |
positive regulation of cardiac muscle cell proliferation | biological process | Any process that activates or increases the frequency, rate or extent of cardiac muscle cell proliferation. [GOC:dph, GOC:rph] |
bone development | biological process | The process whose specific outcome is the progression of bone over time, from its formation to the mature structure. Bone is the hard skeletal connective tissue consisting of both mineral and cellular components. [GOC:dph] |
3'-UTR-mediated mRNA stabilization | biological process | An mRNA stabilization process in which one or more RNA-binding proteins associate with the 3'-untranslated region (UTR) of an mRNA. [GOC:mah, PMID:19029303] |
cellular response to lipoteichoic acid | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipoteichoic acid stimulus; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:mah] |
cellular response to tumor necrosis factor | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus. [GOC:mah] |
cellular response to ionizing radiation | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ionizing radiation stimulus. Ionizing radiation is radiation with sufficient energy to remove electrons from atoms and may arise from spontaneous decay of unstable isotopes, resulting in alpha and beta particles and gamma rays. Ionizing radiation also includes X-rays. [GOC:mah] |
cellular response to UV-B | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-B radiation stimulus. UV-B radiation (UV-B light) spans the wavelengths 280 to 315 nm. [GOC:mah] |
negative regulation of canonical Wnt signaling pathway | biological process | Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes. [GOC:dph, GOC:tb] |
positive regulation of brown fat cell differentiation | biological process | Any process that increases the rate, frequency, or extent of brown fat cell differentiation. Brown fat cell differentiation is the process in which a relatively unspecialized cell acquires specialized features of a brown adipocyte, an animal connective tissue cell involved in adaptive thermogenesis. Brown adipocytes contain multiple small droplets of triglycerides and a high number of mitochondria. [GOC:BHF] |
cellular senescence | biological process | A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. [GOC:BHF, PMID:28682291] |
stress-induced premature senescence | biological process | A cellular senescence process associated with the dismantling of a cell as a response to environmental factors such as hydrogen peroxide or X-rays. [GOC:BHF] |
cellular response to virus | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a virus. [GOC:dos] |
regulation of synaptic membrane adhesion | biological process | Any process that modulates the frequency, rate or extent of adhesion between pre- and post-synaptic membranes. [GOC:dos] |
regulation of cytokine production involved in inflammatory response | biological process | Any process that modulates the frequency, rate or extent of cytokine production involved in inflammatory response. [GOC:TermGenie] |
positive regulation of myoblast fusion | biological process | Any process that activates or increases the frequency, rate or extent of myoblast fusion. [GOC:BHF, GOC:rl, GOC:TermGenie, PMID:21364645] |
positive regulation of reactive oxygen species metabolic process | biological process | Any process that activates or increases the frequency, rate or extent of reactive oxygen species metabolic process. [GOC:mah] |