Proteins > Glycogen synthase kinase-3 alpha
Page last updated: 2024-08-07 16:46:31
Glycogen synthase kinase-3 alpha
A glycogen synthase kinase-3 alpha that is encoded in the genome of human. [PRO:DNx, UniProtKB:P49840]
Synonyms
GSK-3 alpha;
EC 2.7.11.26;
Serine/threonine-protein kinase GSK3A;
2.7.11.1
Research
Bioassay Publications (55)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 26 (47.27) | 29.6817 |
2010's | 25 (45.45) | 24.3611 |
2020's | 4 (7.27) | 2.80 |
Compounds (284)
Drugs with Inhibition Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
indirubin-3'-monoxime | Homo sapiens (human) | IC50 | 0.0220 | 3 | 3 |
nsc 664704 | Homo sapiens (human) | IC50 | 0.0230 | 1 | 1 |
2,4-thiazolidinedione | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
maleic anhydride | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
hydantoins | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
indirubin | Homo sapiens (human) | IC50 | 1.5000 | 3 | 3 |
indigo | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
maleimide | Homo sapiens (human) | IC50 | 6.0000 | 1 | 1 |
succinimide | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
staurosporine | Homo sapiens (human) | IC50 | 0.0103 | 5 | 5 |
4-cyclopentene-1,3-dione | Homo sapiens (human) | IC50 | 12.0000 | 1 | 1 |
n-methylmaleimide | Homo sapiens (human) | IC50 | 5.0000 | 1 | 1 |
n-benzylmaleimide | Homo sapiens (human) | IC50 | 1.0000 | 1 | 1 |
cyc 202 | Homo sapiens (human) | IC50 | 95.0000 | 2 | 2 |
sb 216763 | Homo sapiens (human) | IC50 | 0.0477 | 3 | 3 |
sb 216763 | Homo sapiens (human) | Ki | 0.0091 | 1 | 1 |
n-(4-methoxybenzyl)-n'-(5-nitro-1,3-thiazol-2-yl)urea | Homo sapiens (human) | IC50 | 35.0520 | 2 | 2 |
7-n-butyl-6-(4'-hydroxyphenyl)-5h-pyrrolo(2,3b)pyrazine | Homo sapiens (human) | IC50 | 0.8239 | 4 | 4 |
6-bromoindirubin-3'-oxime | Homo sapiens (human) | IC50 | 0.0620 | 5 | 5 |
repsox | Homo sapiens (human) | IC50 | 16.0000 | 1 | 1 |
rhodanine | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
7-butyl-6-(4-methoxyphenyl)-5H-pyrrolo[2,3-b]pyrazine | Homo sapiens (human) | IC50 | 0.9120 | 1 | 1 |
4-benzyl-2-methyl-1,2,4-thiadiazolidine-3,5-dione | Homo sapiens (human) | IC50 | 4.5000 | 2 | 2 |
sb 415286 | Homo sapiens (human) | IC50 | 0.1040 | 3 | 3 |
sb 415286 | Homo sapiens (human) | Ki | 0.0308 | 1 | 1 |
alsterpaullone | Homo sapiens (human) | IC50 | 0.0043 | 3 | 3 |
quercetin | Homo sapiens (human) | IC50 | 2.1000 | 1 | 1 |
apigenin | Homo sapiens (human) | IC50 | 1.4000 | 1 | 1 |
luteolin | Homo sapiens (human) | IC50 | 0.8000 | 1 | 1 |
kaempferol | Homo sapiens (human) | IC50 | 3.5000 | 1 | 1 |
harmine | Homo sapiens (human) | IC50 | 10.0000 | 3 | 3 |
chrysin | Homo sapiens (human) | IC50 | 7.2000 | 1 | 1 |
fisetin | Homo sapiens (human) | IC50 | 0.4200 | 1 | 1 |
alvocidib | Homo sapiens (human) | IC50 | 0.5250 | 2 | 2 |
su 9516 | Homo sapiens (human) | IC50 | 0.3500 | 1 | 1 |
jnj-7706621 | Homo sapiens (human) | IC50 | 0.0410 | 1 | 1 |
GSK3-XIII | Homo sapiens (human) | Ki | 0.0240 | 1 | 1 |
cyc 116 | Homo sapiens (human) | Ki | 10.0000 | 1 | 1 |
manzamine a | Homo sapiens (human) | IC50 | 25.0000 | 1 | 1 |
1-azakenpaullone | Homo sapiens (human) | IC50 | 0.0180 | 1 | 1 |
2-[(3-iodophenyl)methylthio]-5-pyridin-4-yl-1,3,4-oxadiazole | Homo sapiens (human) | IC50 | 4.1950 | 2 | 2 |
jnj 10198409 | Homo sapiens (human) | IC50 | 13.0000 | 1 | 1 |
chir 99021 | Homo sapiens (human) | IC50 | 0.0089 | 2 | 2 |
ly2090314 | Homo sapiens (human) | IC50 | 0.0013 | 3 | 3 |
leucettamine b | Homo sapiens (human) | IC50 | 11.3500 | 2 | 2 |
5-(5,6-dimethoxy-1-benzimidazolyl)-3-[(2-methylsulfonylphenyl)methoxy]-2-thiophenecarbonitrile | Homo sapiens (human) | IC50 | 15.8489 | 1 | 1 |
gsk 269962a | Homo sapiens (human) | IC50 | 1.2600 | 1 | 1 |
sb 772077-b | Homo sapiens (human) | IC50 | 9.1000 | 1 | 1 |
abt-348 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
dinaciclib | Homo sapiens (human) | IC50 | 0.4140 | 1 | 1 |
chir 98014 | Homo sapiens (human) | IC50 | 0.0070 | 1 | 1 |
palinurin | Homo sapiens (human) | IC50 | 1.6109 | 1 | 2 |
vx-970 | Homo sapiens (human) | Ki | 0.0330 | 1 | 1 |
vx-787 | Homo sapiens (human) | Ki | 1.6000 | 1 | 1 |
CCT251545 | Homo sapiens (human) | IC50 | 0.4620 | 1 | 1 |
CCT251545 | Homo sapiens (human) | Ki | 0.2310 | 1 | 1 |
((5z)5-(1,3-benzodioxol-5-yl)methylene-2-phenylamino-3,5-dihydro-4h-imidazol-4-one) | Homo sapiens (human) | IC50 | 0.2100 | 1 | 1 |
ro 3306 | Homo sapiens (human) | Ki | 0.5000 | 1 | 1 |
7-bromoindirubin-3'-oxime | Homo sapiens (human) | IC50 | 32.0000 | 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 | 10.0000 | 1 | 1 |
imatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
staurosporine | Homo sapiens (human) | Kd | 0.1400 | 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 | 11.5333 | 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 | 9.0687 | 3 | 3 |
canertinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
birb 796 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
cyc 202 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
enzastaurin | Homo sapiens (human) | Kd | 5.1230 | 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 | 15.0000 | 4 | 4 |
pd 173955 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
s 1033 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms 387032 | Homo sapiens (human) | Kd | 0.0830 | 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 | 10.0000 | 2 | 2 |
dasatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
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 | 1.1903 | 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 | 0.1600 | 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 | 2 |
ekb 569 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
axitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
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 | 1 |
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 | 1.1030 | 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 | 30.0000 | 1 | 1 |
pd 0325901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
midostaurin | Homo sapiens (human) | Kd | 9.3750 | 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 | 30.0000 | 1 | 1 |
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 | 20.0000 | 2 | 2 |
binimetinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sotrastaurin | Homo sapiens (human) | Kd | 1.2010 | 1 | 1 |
aee 788 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
saracatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
vx 702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
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 | 1 |
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 | 30.0000 | 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 | 16.2500 | 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 | 0.0070 | 1 | 1 |
np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
at 7519 | Homo sapiens (human) | Kd | 0.0280 | 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 | 30.0000 | 1 | 1 |
nvp-ast487 | Homo sapiens (human) | Kd | 9.2500 | 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 | 1 |
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 | 30.0000 | 1 | 1 |
cc-930 | Homo sapiens (human) | Kd | 30.0000 | 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 | 0.8450 | 1 | 1 |
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 | 1 |
bgt226 | Homo sapiens (human) | Kd | 3.4030 | 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 | 30.0000 | 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 | 22.5430 | 1 | 1 |
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 | 2.7375 | 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 | 0.5790 | 1 | 1 |
azd5438 | Homo sapiens (human) | Kd | 0.0550 | 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 | 30.0000 | 1 | 1 |
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 | 17.3010 | 1 | 1 |
cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
arry-614 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
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 | 1 |
ponatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
amg 900 | Homo sapiens (human) | Kd | 30.0000 | 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 | 1 |
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 | 30.0000 | 1 | 1 |
cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
defactinib | Homo sapiens (human) | Kd | 1.4620 | 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 | 30.0000 | 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 | 2.0880 | 1 | 1 |
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 | 2 |
gsk 1363089 | Homo sapiens (human) | Kd | 20.0000 | 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 | 0.0290 | 1 | 1 |
sb 1518 | Homo sapiens (human) | Kd | 5.1880 | 1 | 1 |
abemaciclib | Homo sapiens (human) | Kd | 0.0130 | 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 | 30.0000 | 1 | 1 |
jnj38877605 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dinaciclib | Homo sapiens (human) | Kd | 1.4750 | 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 | 5.2590 | 1 | 1 |
bms-911543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
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 | 30.0000 | 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 | 1 |
vx-509 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
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 | 0.0060 | 1 | 1 |
otssp167 | Homo sapiens (human) | Kd | 0.0870 | 1 | 1 |
chir 258 | Homo sapiens (human) | Kd | 20.0000 | 3 | 4 |
osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
((5z)5-(1,3-benzodioxol-5-yl)methylene-2-phenylamino-3,5-dihydro-4h-imidazol-4-one) | Homo sapiens (human) | Kd | 0.5500 | 1 | 1 |
nintedanib | Homo sapiens (human) | Kd | 15.2150 | 2 | 2 |
bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pp242 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
3'-Substituted 7-halogenoindirubins, a new class of cell death inducing agents.Journal of medicinal chemistry, , Jul-27, Volume: 49, Issue:15, 2006
Mechanism of CDK5/p25 binding by CDK inhibitors.Journal of medicinal chemistry, , Feb-10, Volume: 48, Issue:3, 2005
Structural basis for the synthesis of indirubins as potent and selective inhibitors of glycogen synthase kinase-3 and cyclin-dependent kinases.Journal of medicinal chemistry, , Feb-12, Volume: 47, Issue:4, 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
3'-Substituted 7-halogenoindirubins, a new class of cell death inducing agents.Journal of medicinal chemistry, , Jul-27, Volume: 49, Issue:15, 2006
Structural basis for the synthesis of indirubins as potent and selective inhibitors of glycogen synthase kinase-3 and cyclin-dependent kinases.Journal of medicinal chemistry, , Feb-12, Volume: 47, Issue:4, 2004
Generation of new protein kinase inhibitors utilizing cytochrome p450 mutant enzymes for indigoid synthesis.Journal of medicinal chemistry, , Jun-03, Volume: 47, Issue:12, 2004
Discovery of a Potent Dual SLK/STK10 Inhibitor Based on a Maleimide Scaffold.Journal of medicinal chemistry, , 09-23, Volume: 64, Issue:18, 2021
ASR352, A potent anticancer agent: Synthesis, preliminary SAR, and biological activities against colorectal cancer bulk, 5-fluorouracil/oxaliplatin resistant and stem cells.European journal of medicinal chemistry, , Jan-01, Volume: 161, 2019
Novel quinazoline derivatives bearing various 6-benzamide moieties as highly selective and potent EGFR inhibitors.Bioorganic & medicinal chemistry, , 05-01, Volume: 26, Issue:8, 2018
Indolinone based LRRK2 kinase inhibitors with a key hydrogen bond.Bioorganic & medicinal chemistry letters, , Oct-01, Volume: 24, Issue:19, 2014
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 of 2-pyrimidyl-5-amidothiophenes as potent inhibitors for AKT: synthesis and SAR studies.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 16, Issue:16, 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
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
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
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
Synthesis and biological evaluation of selective and potent cyclin-dependent kinase inhibitors.European journal of medicinal chemistry, , Volume: 56, 2012
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Novel 9-oxo-thiazolo[5,4-f]quinazoline-2-carbonitrile derivatives as dual cyclin-dependent kinase 1 (CDK1)/glycogen synthase kinase-3 (GSK-3) inhibitors: synthesis, biological evaluation and molecular modeling studies.European journal of medicinal chemistry, , Volume: 43, Issue:7, 2008
Lessons Learned from Past Cyclin-Dependent Kinase Drug Discovery Efforts.Journal of medicinal chemistry, , 05-12, Volume: 65, Issue:9, 2022
Pharmacological inhibitors of glycogen synthase kinase 3.Trends in pharmacological sciences, , Volume: 25, Issue:9, 2004
Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription.Chemistry & biology, , Volume: 7, Issue:10, 2000
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
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
1-Aryl-3-(4-methoxybenzyl)ureas as potentially irreversible glycogen synthase kinase 3 inhibitors: Synthesis and biological evaluation.Bioorganic & medicinal chemistry letters, , 07-01, Volume: 29, Issue:13, 2019
Synthesis and biological evaluation of glycogen synthase kinase 3 (GSK-3) inhibitors: an fast and atom efficient access to 1-aryl-3-benzylureas.Bioorganic & medicinal chemistry letters, , Sep-15, Volume: 21, Issue:18, 2011
Recent development of CDK inhibitors: An overview of CDK/inhibitor co-crystal structures.European journal of medicinal chemistry, , Feb-15, Volume: 164, 2019
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
3D QSAR studies on GSK-3 inhibition by aloisines.Bioorganic & medicinal chemistry letters, , Jan-17, Volume: 15, Issue:2, 2005
Aloisines, a new family of CDK/GSK-3 inhibitors. SAR study, crystal structure in complex with CDK2, enzyme selectivity, and cellular effects.Journal of medicinal chemistry, , Jan-16, Volume: 46, Issue:2, 2003
Acridone alkaloids from Glycosmis chlorosperma as DYRK1A inhibitors.Journal of natural products, , May-23, Volume: 77, Issue:5, 2014
Soluble 3',6-substituted indirubins with enhanced selectivity toward glycogen synthase kinase -3 alter circadian period.Journal of medicinal chemistry, , Oct-23, Volume: 51, Issue:20, 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
3'-Substituted 7-halogenoindirubins, a new class of cell death inducing agents.Journal of medicinal chemistry, , Jul-27, Volume: 49, Issue:15, 2006
Structural basis for the synthesis of indirubins as potent and selective inhibitors of glycogen synthase kinase-3 and cyclin-dependent kinases.Journal of medicinal chemistry, , Feb-12, Volume: 47, Issue:4, 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
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
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
Pharmacological inhibitors of glycogen synthase kinase 3.Trends in pharmacological sciences, , Volume: 25, Issue:9, 2004
3-Anilino-4-arylmaleimides: potent and selective inhibitors of glycogen synthase kinase-3 (GSK-3).Bioorganic & medicinal chemistry letters, , Mar-12, Volume: 11, Issue:5, 2001
Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription.Chemistry & biology, , Volume: 7, Issue:10, 2000
Pivotal role of glycogen synthase kinase-3: A therapeutic target for Alzheimer's disease.European journal of medicinal chemistry, , Jan-01, Volume: 107, 2016
9-cyano-1-azapaullone (cazpaullone), a glycogen synthase kinase-3 (GSK-3) inhibitor activating pancreatic beta cell protection and replication.Journal of medicinal chemistry, , Apr-10, Volume: 51, Issue:7, 2008
Pharmacological inhibitors of glycogen synthase kinase 3.Trends in pharmacological sciences, , Volume: 25, Issue:9, 2004
Synthesis, biological evaluation and molecular modeling studies of imidazo[1,2-a]pyridines derivatives as protein kinase inhibitors.European journal of medicinal chemistry, , Nov-10, Volume: 123, 2016
Synthesis of new pyridazino[4,5-b]indol-4-ones and pyridazin-3(2H)-one analogs as DYRK1A inhibitors.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 24, Issue:21, 2014
Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B.Journal of medicinal chemistry, , Nov-08, Volume: 55, Issue:21, 2012
Discovery of Journal of medicinal chemistry, , 09-09, Volume: 64, Issue:17, 2021
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
Crystal structure of a human cyclin-dependent kinase 6 complex with a flavonol inhibitor, fisetin.Journal of medicinal chemistry, , Feb-10, Volume: 48, Issue:3, 2005
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
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
1-Acyl-1H-[1,2,4]triazole-3,5-diamine analogues as novel and potent anticancer cyclin-dependent kinase inhibitors: synthesis and evaluation of biological activities.Journal of medicinal chemistry, , Jun-30, Volume: 48, Issue:13, 2005
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
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
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
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
Synthesis, Binding Mode, and Antihyperglycemic Activity of Potent and Selective (5-Imidazol-2-yl-4-phenylpyrimidin-2-yl)[2-(2-pyridylamino)ethyl]amine Inhibitors of Glycogen Synthase Kinase 3.Journal of medicinal chemistry, , 10-26, Volume: 60, Issue:20, 2017
Pharmacological inhibitors of glycogen synthase kinase 3.Trends in pharmacological sciences, , Volume: 25, Issue:9, 2004
Discovery of novel glycogen synthase kinase-3α inhibitors: Structure-based virtual screening, preliminary SAR and biological evaluation for treatment of acute myeloid leukemia.European journal of medicinal chemistry, , Jun-01, Volume: 171, 2019
Pharmacokinetics, metabolism, and excretion of the glycogen synthase kinase-3 inhibitor LY2090314 in rats, dogs, and humans: a case study in rapid clearance by extensive metabolism with low circulating metabolite exposure.Drug metabolism and disposition: the biological fate of chemicals, , Volume: 41, Issue:4, 2013
Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B.Journal of medicinal chemistry, , Nov-08, Volume: 55, Issue:21, 2012
Synthesis and preliminary biological evaluation of new derivatives of the marine alkaloid leucettamine B as kinase inhibitors.European journal of medicinal chemistry, , Volume: 45, Issue:2, 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
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
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
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
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
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
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
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
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery of Journal of medicinal chemistry, , 09-09, Volume: 64, Issue:17, 2021
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Potent and orally bioavailable CDK8 inhibitors: Design, synthesis, structure-activity relationship analysis and biological evaluation.European journal of medicinal chemistry, , Mar-15, Volume: 214, 2021
Discovery of potent, orally bioavailable, small-molecule inhibitors of WNT signaling from a cell-based pathway screen.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 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
Enables
This protein enables 8 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] |
signaling receptor binding | molecular function | Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function. [GOC:bf, GOC:ceb, ISBN:0198506732] |
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] |
protein kinase A catalytic subunit binding | molecular function | Binding to one or both of the catalytic subunits of protein kinase A. [GOC:mah] |
tau protein binding | molecular function | Binding to tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. [GOC:jid] |
tau-protein kinase activity | molecular function | Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein. [EC:2.7.11.26, MetaCyc:TAU-PROTEIN-KINASE-RXN] |
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 6 target(s):
Target | Category | Definition |
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] |
neuronal cell body | cellular component | The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites. [GOC:go_curators] |
apical dendrite | cellular component | A dendrite that emerges near the apical pole of a neuron. In bipolar neurons, apical dendrites are located on the opposite side of the soma from the axon. [NIF_Subcellular:sao273773228] |
postsynapse | cellular component | The part of a synapse that is part of the post-synaptic cell. [GOC:dos] |
proximal dendrite | cellular component | The dendrite of the dendritic tree that is closest to the neuronal cell body (the soma). [GOC:aruk, GOC:bc, PMID:16899232] |
Active In
This protein is active in 4 target(s):
Target | Category | Definition |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
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] |
axon | cellular component | The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter. [GOC:nln, 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] |
Part Of
This protein is part of 1 target(s):
Target | Category | Definition |
beta-catenin destruction complex | cellular component | A cytoplasmic protein complex containing glycogen synthase kinase-3-beta (GSK-3-beta), the adenomatous polyposis coli protein (APC), and the scaffolding protein axin, among others; phosphorylates beta-catenin, targets it for degradation by the proteasome. [PMID:14600025] |
Involved In
This protein is involved in 49 target(s):
Target | Category | Definition |
regulation of systemic arterial blood pressure | biological process | The process that modulates the force with which blood travels through the systemic arterial circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure. [GOC:mtg_cardio] |
cardiac left ventricle morphogenesis | biological process | The process in which the left cardiac ventricle is generated and organized. [GOC:mtg_heart] |
glycogen metabolic process | biological process | The chemical reactions and pathways involving glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues in alpha-(1->4) glycosidic linkage, joined together by alpha-(1->6) glycosidic linkages. [ISBN:0198506732] |
protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
dopamine receptor signaling pathway | biological process | The series of molecular signals generated as a consequence of a dopamine receptor binding to one of its physiological ligands. [GOC:mah, PMID:21711983] |
nervous system development | biological process | The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state. [GOC:dgh] |
insulin receptor signaling pathway | biological process | The series of molecular signals generated as a consequence of the insulin receptor binding to insulin. [GOC:ceb] |
positive regulation of autophagy | biological process | Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. [GOC:dph, GOC:tb] |
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 peptidyl-threonine phosphorylation | biological process | Any process that increases the frequency, rate or extent of peptidyl-threonine phosphorylation. Peptidyl-threonine phosphorylation is the phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [GOC:dph, GOC:tb] |
negative regulation of UDP-glucose catabolic process | biological process | Any process that decreases the rate, frequency or extent of UDP-glucose catabolism. UDP-glucose catabolic processes are the chemical reactions and pathways resulting in the breakdown of UDP-glucose, uridinediphosphoglucose, a substance composed of glucose in glycosidic linkage with uridine diphosphate. [GOC:BHF, GOC:tb] |
Wnt signaling pathway | biological process | The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of a target cell and ending with a change in cell state. [PMID:11532397] |
cell migration | biological process | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. [GOC:cjm, GOC:dph, GOC:ems, GOC:pf, Wikipedia:Cell_migration] |
peptidyl-threonine phosphorylation | biological process | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038] |
viral protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. [GOC:bf, GOC:jl, ISBN:0781702534] |
positive regulation of protein ubiquitination | biological process | Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein. [GOC:mah] |
negative regulation of TOR signaling | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of TOR signaling. [GOC:mah] |
positive regulation of proteasomal ubiquitin-dependent protein catabolic process | biological process | Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. [GOC:mah] |
cellular response to insulin 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 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] |
positive regulation of peptidyl-serine phosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-serine. [GOC:mah] |
cellular response to interleukin-3 | 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 an interleukin-3 stimulus. [GOC:yaf] |
proteasome-mediated ubiquitin-dependent protein catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. [GOC:go_curators] |
negative regulation of glycogen biosynthetic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen. [GOC:go_curators] |
positive regulation of protein catabolic process | biological process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. [GOC:go_curators] |
positive regulation of heart contraction | biological process | Any process that activates or increases the frequency, rate or extent of heart contraction. [GOC:go_curators] |
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] |
negative regulation of glucose import | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. [GOC:ai] |
negative regulation of insulin receptor signaling pathway | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling. [GOC:bf] |
excitatory postsynaptic potential | biological process | A process that leads to a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential. [GOC:dph, GOC:ef] |
negative regulation of cell growth involved in cardiac muscle cell development | biological process | Any process that decreases the rate, frequency, or extent of the growth of a cardiac muscle cell, where growth contributes to the progression of the cell over time from its initial formation to its mature state. [GOC:dph] |
cellular response to lithium ion | 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 lithium (Li+) ion stimulus. [GOC:mah] |
cellular response to glucocorticoid 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 glucocorticoid stimulus. Glucocorticoids are hormonal C21 corticosteroids synthesized from cholesterol with the ability to bind with the cortisol receptor and trigger similar effects. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects. [GOC:mah] |
positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of the adenylate cyclase-activating adrenergic receptor protein signaling pathway. An adrenergic receptor signaling pathway is the series of molecular signals generated as a consequence of an adrenergic receptor binding to one of its physiological ligands. [GOC:BHF, 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] |
extrinsic apoptotic signaling pathway | biological process | The series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with either a ligand binding to a cell surface receptor, or a ligand being withdrawn from a cell surface receptor (e.g. in the case of signaling by dependence receptors), and ends when the execution phase of apoptosis is triggered. [GOC:mtg_apoptosis, GOC:yaf, PMID:17340152] |
extrinsic apoptotic signaling pathway in absence of ligand | biological process | The series of molecular signals in which a signal is conveyed from the cell surface to trigger the apoptotic death of a cell. The pathway starts with withdrawal of a ligand from a cell surface receptor, and ends when the execution phase of apoptosis is triggered. [GOC:mtg_apoptosis, PMID:15044679, PMID:20816705] |
positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of an adenylate cyclase-activating G protein-coupled receptor signaling pathway. [GOC:hjd, PMID:19246489] |
autosome genomic imprinting | biological process | The establishment of epigenetic modifications (imprints) in autosomal (non-sexual) chromosomes during gametogenesis, and propagation of these imprints during the organism's life. Genomic imprinting leads to an asymmetry between the maternal and paternal alleles and differential expression of the corresponding alleles. This can happen through heterochromatin formation or differential chromatin loop formation. [PMID:31782494] |
positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway. [GOC:BHF, GOC:mtg_apoptosis, GOC:TermGenie] |
regulation of mitophagy | biological process | Any process that modulates the frequency, rate or extent of macromitophagy. [GOC:TermGenie] |
positive regulation of amyloid-beta formation | biological process | Any process that activates or increases the frequency, rate or extent of amyloid-beta formation. [GOC:dph, GOC:TermGenie, PMID:17098871] |
positive regulation of protein targeting to mitochondrion | biological process | Any process that activates or increases the frequency, rate or extent of protein targeting to mitochondrion. [GO_REF:0000058, GOC:pad, GOC:PARL, GOC:TermGenie, PMID:24270810] |
negative regulation of glycogen synthase activity, transferring glucose-1-phosphate | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of glycogen synthase activity, transferring glucose-1-phosphate. [GO_REF:0000059, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:17569761] |
negative regulation of type B pancreatic cell development | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of pancreatic B cell development. [GOC:obol, GOC:yaf] |
negative regulation of glycogen (starch) synthase activity | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of glycogen (starch) synthase activity. [GOC:obol] |
positive regulation of glycogen (starch) synthase activity | biological process | Any process that activates or increases the frequency, rate or extent of glycogen (starch) synthase activity. [GOC:obol] |
cell differentiation | biological process | The cellular developmental process in which a relatively unspecialized cell, e.g. embryonic or regenerative cell, acquires specialized structural and/or functional features that characterize a specific cell. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. [ISBN:0198506732] |
regulation of microtubule cytoskeleton organization | biological process | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins. [GOC:mah] |
regulation of neuron projection development | biological process | Any process that modulates the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites). [GOC:dph, GOC:tb] |