Page last updated: 2024-08-07 16:38:23
Protein kinase C iota type
A protein kinase C iota type that is encoded in the genome of human. [PRO:DNx, UniProtKB:P41743]
Synonyms
EC 2.7.11.13;
Atypical protein kinase C-lambda/iota;
PRKC-lambda/iota;
aPKC-lambda/iota;
nPKC-iota
Research
Bioassay Publications (42)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 7 (16.67) | 18.2507 |
2000's | 23 (54.76) | 29.6817 |
2010's | 12 (28.57) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (267)
Drugs with Inhibition Measurements
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 |
imatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
tetradecanoylphorbol acetate | Homo sapiens (human) | EC50 | 0.0095 | 1 | 1 |
triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
staurosporine | Homo sapiens (human) | Kd | 0.0260 | 1 | 1 |
picropodophyllin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gefitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
lestaurtinib | Homo sapiens (human) | Kd | 15.9000 | 2 | 2 |
perifosine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vatalanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
ruboxistaurin | Homo sapiens (human) | Kd | 15.7000 | 2 | 2 |
canertinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
birb 796 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
cyc 202 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
enzastaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
erlotinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
lapatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
sorafenib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
pd 173955 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
12-deoxyphorbol 13-acetate | Homo sapiens (human) | EC50 | 0.9100 | 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 | 20.0000 | 2 | 2 |
sf 2370 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tandutinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
vx-745 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
dasatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
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 | 20.0000 | 2 | 2 |
imd 0354 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alvocidib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bosutinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
su 11248 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vx680 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
cyc 116 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ekb 569 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
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 |
pep005 | Homo sapiens (human) | EC50 | 0.0725 | 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 | 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 | 30.0000 | 1 | 1 |
pd 0325901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
midostaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
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 | 30.0000 | 1 | 1 |
pi103 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
hmn-214 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
tivozanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
hki 272 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
tofacitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
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 | 20.0000 | 2 | 2 |
azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
su 14813 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bibw 2992 | Homo sapiens (human) | Kd | 20.0000 | 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 | 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 | 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 | 2 |
np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
at 7519 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bms-690514 | Homo sapiens (human) | Kd | 2.4220 | 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 | 10.0000 | 1 | 1 |
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 | 20.0000 | 2 | 2 |
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 | 1 | 1 |
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 | 20.0000 | 2 | 2 |
motesanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
fostamatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
trametinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mln8054 | Homo sapiens (human) | Kd | 23.3333 | 2 | 3 |
pf-562,271 | Homo sapiens (human) | Kd | 30.0000 | 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 | 30.0000 | 1 | 1 |
gsk 461364 | Homo sapiens (human) | Kd | 17.9000 | 2 | 2 |
azd 1152-hqpa | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
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 | 30.0000 | 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 | 1.1160 | 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 | 30.0000 | 1 | 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 | 1 |
arry-614 | Homo sapiens (human) | Kd | 30.0000 | 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 | 1 |
ponatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
amg 900 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
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 | 20.0000 | 2 | 2 |
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 | 2 |
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 | 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 | 27.3880 | 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 | 1 |
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 | 2 |
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 | 2 |
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 | 2 |
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 | 51.0180 | 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 | 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 | 1 |
gsk2141795 | Homo sapiens (human) | Kd | 1.2300 | 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 | 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 | 23.3333 | 2 | 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 |
Drugs with Other Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
edelfosine | Homo sapiens (human) | ID50 | 12.0000 | 1 | 1 |
phenidone | Homo sapiens (human) | Activity | 300.0000 | 1 | 1 |
Methyl 3-(3-(4-(2,4,4-Trimethylpentan-2-yl)phenoxy)-propanamido)benzoate as a Novel and Dual Malate Dehydrogenase (MDH) 1/2 Inhibitor Targeting Cancer Metabolism.Journal of medicinal chemistry, , 10-26, Volume: 60, Issue:20, 2017
Kinase inhibitors: not just for kinases anymore.Journal of medicinal chemistry, , Apr-10, Volume: 46, Issue:8, 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
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
Syntheses, neural protective activities, and inhibition of glycogen synthase kinase-3β of substituted quinolines.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 24, Issue:15, 2014
Structure-based design, synthesis and biological evaluation of diphenylmethylamine derivatives as novel Akt1 inhibitors.European journal of medicinal chemistry, , Feb-12, Volume: 73, 2014
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Protein kinase C epsilon regulates gamma-aminobutyrate type A receptor sensitivity to ethanol and benzodiazepines through phosphorylation of gamma2 subunits.The Journal of biological chemistry, , Nov-09, Volume: 282, Issue:45, 2007
Synthesis and biological evaluation of 1-aryl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one inhibitors of cyclin-dependent kinases.Journal of medicinal chemistry, , Nov-18, Volume: 47, Issue:24, 2004
Aryl[a]pyrrolo[3,4-c]carbazoles as selective cyclin D1-CDK4 inhibitors.Bioorganic & medicinal chemistry letters, , Nov-03, Volume: 13, Issue:21, 2003
Identification of orally active, potent, and selective 4-piperazinylquinazolines as antagonists of the platelet-derived growth factor receptor tyrosine kinase family.Journal of medicinal chemistry, , Aug-15, Volume: 45, Issue:17, 2002
New dermatological agents for the treatment of psoriasis.Journal of medicinal chemistry, , Feb-01, Volume: 44, Issue:3, 2001
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
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
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
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
Synthesis and kinase inhibitory activity of 3'-(S)-epi-K-252a.Bioorganic & medicinal chemistry letters, , Oct-21, Volume: 12, Issue:20, 2002
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 review on flavones targeting serine/threonine protein kinases for potential anticancer drugs.Bioorganic & medicinal chemistry, , 03-01, Volume: 27, Issue:5, 2019
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 aminothiazole inhibitors of cyclin-dependent kinase 2: synthesis, X-ray crystallographic analysis, and biological activities.Journal of medicinal chemistry, , Aug-29, Volume: 45, Issue:18, 2002
Structure-activity relationship studies of flavopiridol analogues.Bioorganic & medicinal chemistry letters, , May-15, Volume: 10, Issue:10, 2000
Aryl[a]pyrrolo[3,4-c]carbazoles as selective cyclin D1-CDK4 inhibitors.Bioorganic & medicinal chemistry letters, , Nov-03, Volume: 13, Issue:21, 2003
Dianilinophthalimides: potent and selective, ATP-competitive inhibitors of the EGF-receptor protein tyrosine kinase.Journal of medicinal chemistry, , Apr-01, Volume: 37, Issue:7, 1994
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
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
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
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
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 3,4,6-Trisubstituted Piperidine Derivatives as Orally Active, Low hERG Blocking Akt Inhibitors via Conformational Restriction and Structure-Based Design.Journal of medicinal chemistry, , 08-08, Volume: 62, Issue:15, 2019
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
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 kinase activity | molecular function | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. [PMID:25399640] |
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] |
diacylglycerol-dependent serine/threonine kinase activity | molecular function | Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires diacylglycerol. [EC:2.7.11.13] |
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] |
phospholipid binding | molecular function | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester. [ISBN:0198506732] |
metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
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 17 target(s):
Target | Category | Definition |
Golgi membrane | cellular component | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. [GOC:mah] |
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] |
endosome | cellular component | A vacuole to which materials ingested by endocytosis are delivered. [ISBN:0198506732, PMID:19696797] |
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] |
plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
brush border | cellular component | The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell. [GOC:sl, ISBN:0815316194] |
bicellular tight junction | cellular component | An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes. [GOC:mah, ISBN:0815332181] |
microtubule cytoskeleton | cellular component | The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins. [GOC:jl, ISBN:0395825172] |
apical plasma membrane | cellular component | The region of the plasma membrane located at the apical end of the cell. [GOC:curators] |
cell leading edge | cellular component | The area of a motile cell closest to the direction of movement. [GOC:pg] |
Schmidt-Lanterman incisure | cellular component | Regions within compact myelin in which the cytoplasmic faces of the enveloping myelin sheath are not tightly juxtaposed, and include cytoplasm from the cell responsible for making the myelin. Schmidt-Lanterman incisures occur in the compact myelin internode, while lateral loops are analogous structures found in the paranodal region adjacent to the nodes of Ranvier. [GOC:dgh] |
intercellular bridge | cellular component | A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised. [PMID:9635420] |
extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
tight junction | cellular component | A cell-cell junction that seals cells together in an epithelium in a way that prevents even small molecules from leaking from one side of the sheet to the other. [ISBN:0815332181] |
Schaffer collateral - CA1 synapse | cellular component | A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell. [PMID:16399689] |
glutamatergic synapse | cellular component | A synapse that uses glutamate as a neurotransmitter. [GOC:dos] |
Part Of
This protein is part of 1 target(s):
Target | Category | Definition |
PAR polarity complex | cellular component | A protein kinase complex that is required for the establishment of a cell polarity axis during the cell division cycle. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. In S. cerevisiae components are: BEM1, CDC24 and CLA4; from worms to vertebrates it contains a PAR6 protein, PAR3 protein and an atypical PKC. [GOC:lnp, PMID:11113154, PMID:18005931, PMID:22500799, PMID:28682236] |
Involved In
This protein is involved in 29 target(s):
Target | Category | Definition |
protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
protein targeting to membrane | biological process | The process of directing proteins towards a membrane, usually using signals contained within the protein. [GOC:curators] |
cytoskeleton organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures. [GOC:dph, GOC:jl, GOC:mah] |
actin filament organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. [GOC:mah] |
positive regulation of neuron projection development | biological process | Any process that increases 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] |
vesicle-mediated transport | biological process | A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane. [GOC:ai, GOC:mah, ISBN:08789310662000] |
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] |
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] |
negative regulation of glial cell apoptotic process | biological process | Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process. [GOC:mah, GOC:mtg_apoptosis] |
establishment of apical/basal cell polarity | biological process | The specification and formation of the polarity of a cell along its apical/basal axis. [GOC:bf] |
eye photoreceptor cell development | biological process | Development of a photoreceptor, a sensory cell in the eye that reacts to the presence of light. They usually contain a pigment that undergoes a chemical change when light is absorbed, thus stimulating a nerve. [GOC:jl, ISBN:0192800981] |
negative regulation of apoptotic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
negative regulation of neuron apoptotic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process in neurons. [GOC:go_curators, GOC:mtg_apoptosis] |
establishment or maintenance of epithelial cell apical/basal polarity | biological process | Any cellular process that results in the specification, formation or maintenance of the apicobasal polarity of an epithelial cell. [GOC:bf, GOC:mah] |
cell-cell junction organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a cell-cell junction. A cell-cell junction is a specialized region of connection between two cells. [GOC:ai, GOC:dph, GOC:jl, GOC:mah] |
positive regulation of Notch signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of the Notch signaling pathway. [GOC:go_curators] |
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] |
secretion | biological process | The controlled release of a substance by a cell or a tissue. [GOC:ai] |
Golgi vesicle budding | biological process | The evagination of the Golgi membrane, resulting in formation of a vesicle. [GOC:jid, ISBN:0716731363, PMID:10219233] |
positive regulation of NF-kappaB transcription factor activity | biological process | Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB. [GOC:dph, GOC:tb, PMID:15087454, PMID:15170030] |
positive regulation of glial cell proliferation | biological process | Any process that activates or increases the rate or extent of glial cell proliferation. [GOC:dph, GOC:sl, GOC:tb] |
membrane organization | biological process | A process which results in the assembly, arrangement of constituent parts, or disassembly of a membrane. A membrane is a double layer of lipid molecules that encloses all cells, and, in eukaryotes, many organelles; may be a single or double lipid bilayer; also includes associated proteins. [GOC:dph, GOC:tb] |
cellular response to chemical stress | 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 chemical stimulus indicating the organism is under stress. [PMID:26653712] |
response to interleukin-1 | 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 interleukin-1 stimulus. [GOC:BHF, GOC:mah] |
regulation of postsynaptic membrane neurotransmitter receptor levels | biological process | Any process that regulates the the local concentration of neurotransmitter receptor at the postsynaptic membrane. [GOC:dos] |
positive regulation of protein localization to plasma membrane | biological process | Any process that activates or increases the frequency, rate or extent of protein localization to plasma membrane. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:11602640] |
positive regulation of endothelial cell apoptotic process | biological process | Any process that activates or increases the frequency, rate or extent of endothelial cell apoptotic process. [GOC:BHF, GOC:mah, GOC:mtg_apoptosis] |
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] |
peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |