Page last updated: 2024-08-07 15:26:25
Tyrosine-protein kinase JAK2
A tyrosine-protein kinase JAK2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O60674]
Synonyms
EC 2.7.10.2;
Janus kinase 2;
JAK-2
Research
Bioassay Publications (161)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 24 (14.91) | 29.6817 |
| 2010's | 103 (63.98) | 24.3611 |
| 2020's | 34 (21.12) | 2.80 |
Compounds (172)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| 4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| whi p154 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| niclosamide | Homo sapiens (human) | IC50 | 55.0000 | 2 | 2 |
| ag 1879 | Homo sapiens (human) | IC50 | 50,000.0000 | 1 | 1 |
| sb 202190 | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| vorinostat | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| staurosporine | Homo sapiens (human) | IC50 | 0.0016 | 9 | 9 |
| lestaurtinib | Homo sapiens (human) | IC50 | 0.0009 | 1 | 1 |
| birb 796 | Homo sapiens (human) | IC50 | 30.0000 | 1 | 1 |
| erlotinib | Homo sapiens (human) | IC50 | 12.0000 | 2 | 2 |
| sulfuretin | Homo sapiens (human) | IC50 | 9.3200 | 1 | 1 |
| ag-490 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| jnj-7706621 | Homo sapiens (human) | IC50 | 4.6703 | 3 | 3 |
| 2-tert-butyl-9-fluoro-3,6-dihydro-7h-benz(h)imidazo(4,5-f)isoquinoline-7-one | Homo sapiens (human) | IC50 | 0.1463 | 7 | 10 |
| 2-((aminocarbonyl)amino)-5-(4-fluorophenyl)-3-thiophenecarboxamide | Homo sapiens (human) | Ki | 0.0050 | 1 | 1 |
| tofacitinib | Homo sapiens (human) | GI50 | 1.1570 | 1 | 1 |
| tofacitinib | Homo sapiens (human) | IC50 | 0.2065 | 79 | 92 |
| tofacitinib | Homo sapiens (human) | Ki | 0.0008 | 5 | 5 |
| sotrastaurin | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| l 783277 | Homo sapiens (human) | IC50 | 10.0000 | 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) | IC50 | 0.0060 | 1 | 1 |
| nvp-aew541 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| 3-[1-(2,6-dichloro-3-fluorophenyl)ethoxy]-5-[1-(piperidin-4-yl)pyrazol-4-yl]pyridin-2-amine | Homo sapiens (human) | IC50 | 0.0920 | 1 | 1 |
| gw 2580 | Homo sapiens (human) | IC50 | 13.0000 | 1 | 1 |
| crizotinib | Homo sapiens (human) | IC50 | 0.0270 | 1 | 1 |
| 4-[2-(2-chloro-4-fluoroanilino)-5-methyl-4-pyrimidinyl]-N-[(1S)-1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide | Homo sapiens (human) | Ki | 4.0000 | 1 | 1 |
| N-(2,4-dimethoxyphenyl)-N-[2-[4-(4-methyl-1-piperazinyl)anilino]-4-pyrimidinyl]carbamic acid (2,6-dimethylphenyl) ester | Homo sapiens (human) | IC50 | 0.4870 | 1 | 4 |
| nvp-tae684 | Homo sapiens (human) | IC50 | 1.5050 | 1 | 1 |
| mf63 compound | Homo sapiens (human) | IC50 | 0.1000 | 1 | 1 |
| azd 1480 | Homo sapiens (human) | IC50 | 0.0305 | 2 | 2 |
| tg101209 | Homo sapiens (human) | IC50 | 0.0060 | 4 | 4 |
| fedratinib | Homo sapiens (human) | IC50 | 0.0035 | 8 | 8 |
| 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) | IC50 | 0.0972 | 4 | 4 |
| 3-cyclopentyl-3-[4-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1-pyrazolyl]propanenitrile | Homo sapiens (human) | IC50 | 0.0009 | 1 | 1 |
| amg 458 | Homo sapiens (human) | IC50 | 25.0000 | 1 | 1 |
| bms 777607 | Homo sapiens (human) | IC50 | 2.0000 | 1 | 1 |
| pci 32765 | Homo sapiens (human) | GI50 | 5.0345 | 2 | 2 |
| pci 32765 | Homo sapiens (human) | IC50 | 5.5000 | 2 | 2 |
| ponatinib | Homo sapiens (human) | IC50 | 0.1690 | 1 | 1 |
| n-(cyanomethyl)-4-(2-((4-(4-morpholinyl)phenyl)amino)-4-pyrimidinyl)benzamide | Homo sapiens (human) | IC50 | 0.0206 | 5 | 5 |
| az 960 | Homo sapiens (human) | GI50 | 0.0240 | 1 | 1 |
| az 960 | Homo sapiens (human) | IC50 | 0.0030 | 1 | 1 |
| az 960 | Homo sapiens (human) | Ki | 0.0004 | 1 | 1 |
| defactinib | Homo sapiens (human) | IC50 | 0.0282 | 1 | 1 |
| incb-018424 | Homo sapiens (human) | IC50 | 0.0573 | 37 | 39 |
| incb-018424 | Homo sapiens (human) | Ki | 0.0001 | 3 | 3 |
| entrectinib | Homo sapiens (human) | IC50 | 0.0400 | 1 | 1 |
| mk 2461 | Homo sapiens (human) | IC50 | 0.2300 | 1 | 1 |
| baricitinib | Homo sapiens (human) | IC50 | 0.1233 | 21 | 23 |
| p505-15 | Homo sapiens (human) | IC50 | 1.7500 | 1 | 1 |
| 4-(cyclopropylamino)-2-((4-(4-(ethylsulfonyl)piperazin-1-yl)phenyl)amino)pyrimidine-5-carboxamide | Homo sapiens (human) | IC50 | 0.0060 | 2 | 2 |
| oclacitinib | Homo sapiens (human) | IC50 | 0.0180 | 1 | 1 |
| pha 793887 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| abt-348 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| ly2784544 | Homo sapiens (human) | IC50 | 0.0030 | 1 | 1 |
| sb 1518 | Homo sapiens (human) | IC50 | 0.0176 | 5 | 5 |
| nvp-bsk805 | Homo sapiens (human) | IC50 | 0.0073 | 1 | 1 |
| gsk143 | Homo sapiens (human) | IC50 | 1.5849 | 1 | 1 |
| glpg0634 | Homo sapiens (human) | GI50 | 10.0000 | 1 | 1 |
| glpg0634 | Homo sapiens (human) | IC50 | 3.6122 | 21 | 22 |
| nms-p118 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| delgocitinib | Homo sapiens (human) | IC50 | 0.0745 | 6 | 6 |
| bms-911543 | Homo sapiens (human) | IC50 | 0.3604 | 3 | 3 |
| pf 956980 | Homo sapiens (human) | IC50 | 0.0526 | 3 | 3 |
| incb039110 | Homo sapiens (human) | IC50 | 0.1000 | 1 | 0 |
| lfm a13 | Homo sapiens (human) | IC50 | 500.0000 | 1 | 1 |
| cep 33779 | Homo sapiens (human) | IC50 | 0.0314 | 2 | 2 |
| ceritinib | Homo sapiens (human) | IC50 | 1.3850 | 2 | 2 |
| HG-10-102-01 | Homo sapiens (human) | Ki | 3.2000 | 1 | 1 |
| cc-292 | Homo sapiens (human) | IC50 | 0.5337 | 1 | 1 |
| vx-509 | Homo sapiens (human) | IC50 | 2.9721 | 5 | 7 |
| vx-509 | Homo sapiens (human) | Ki | 0.0060 | 2 | 3 |
| vx-970 | Homo sapiens (human) | Ki | 0.1500 | 1 | 1 |
| vx-787 | Homo sapiens (human) | Ki | 4.0000 | 1 | 1 |
| pf-06463922 | Homo sapiens (human) | Ki | 0.5290 | 1 | 0 |
| at 9283 | Homo sapiens (human) | IC50 | 0.0014 | 4 | 4 |
| nms-e973 | Homo sapiens (human) | IC50 | 0.0100 | 1 | 1 |
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| sb 202190 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| imatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| staurosporine | Homo sapiens (human) | Kd | 0.0106 | 3 | 3 |
| gefitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| lestaurtinib | Homo sapiens (human) | Kd | 0.0037 | 2 | 2 |
| vatalanib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| ruboxistaurin | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| 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 | 10.0000 | 1 | 1 |
| erlotinib | Homo sapiens (human) | Kd | 6.8500 | 2 | 2 |
| lapatinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| sorafenib | Homo sapiens (human) | Kd | 10.0000 | 3 | 3 |
| pd 173955 | Homo sapiens (human) | Kd | 0.1000 | 1 | 1 |
| s 1033 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| bms 387032 | Homo sapiens (human) | Kd | 20.0000 | 3 | 4 |
| tandutinib | Homo sapiens (human) | Kd | 10.0000 | 3 | 3 |
| vx-745 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| dasatinib | Homo sapiens (human) | Kd | 1.0000 | 2 | 2 |
| ha 1100 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| zd 6474 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| 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 |
| sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| alvocidib | Homo sapiens (human) | Kd | 15.1667 | 3 | 3 |
| bosutinib | Homo sapiens (human) | Kd | 1.1000 | 1 | 1 |
| su 11248 | Homo sapiens (human) | Kd | 6.4340 | 5 | 5 |
| jnj-7706621 | Homo sapiens (human) | Kd | 0.3798 | 13 | 13 |
| vx680 | Homo sapiens (human) | Kd | 0.1900 | 3 | 3 |
| ekb 569 | Homo sapiens (human) | Kd | 6.0000 | 2 | 2 |
| axitinib | Homo sapiens (human) | Kd | 16.6500 | 2 | 2 |
| temsirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pd 184352 | Homo sapiens (human) | Kd | 10.0000 | 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 | 0.0940 | 3 | 3 |
| ki 20227 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| cp 724714 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| pi103 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| 2-((aminocarbonyl)amino)-5-(4-fluorophenyl)-3-thiophenecarboxamide | Homo sapiens (human) | Kd | 0.0220 | 1 | 1 |
| hki 272 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| tofacitinib | Homo sapiens (human) | EC50 | 0.1266 | 5 | 5 |
| tofacitinib | Homo sapiens (human) | Kd | 0.0031 | 4 | 4 |
| 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 | 10.0000 | 1 | 1 |
| masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| pazopanib | Homo sapiens (human) | Kd | 5.8500 | 2 | 2 |
| azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| su 14813 | Homo sapiens (human) | Kd | 1.6000 | 2 | 2 |
| bibw 2992 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| saracatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| crenolanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tg100-115 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| pha 665752 | Homo sapiens (human) | Kd | 0.4300 | 1 | 1 |
| azd 7762 | Homo sapiens (human) | Kd | 3.6780 | 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) | EC50 | 0.0130 | 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 | 15.0018 | 2 | 2 |
| brivanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| at 7519 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| 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 | 0.9100 | 2 | 2 |
| kw 2449 | Homo sapiens (human) | Kd | 20.0253 | 2 | 3 |
| danusertib | Homo sapiens (human) | Kd | 0.1530 | 1 | 1 |
| abt 869 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| ridaforolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| crizotinib | Homo sapiens (human) | Kd | 10.1003 | 3 | 3 |
| osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir-265 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| motesanib | Homo sapiens (human) | Kd | 10.0000 | 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 | 16.6667 | 3 | 3 |
| GDC-0879 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| ly2603618 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tg100801 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 461364 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| azd 1152-hqpa | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| nvp-tae684 | Homo sapiens (human) | Kd | 0.0160 | 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 |
| ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| fedratinib | Homo sapiens (human) | Kd | 0.0011 | 1 | 1 |
| gsk690693 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| gdc 0941 | Homo sapiens (human) | Kd | 10.0000 | 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 | 0.0250 | 1 | 1 |
| cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sgx 523 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| amg 900 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk-1775 | Homo sapiens (human) | Kd | 0.1100 | 1 | 1 |
| AMG-208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| quizartinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| tak 733 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sns 314 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bi d1870 | Homo sapiens (human) | Kd | 1.3100 | 2 | 2 |
| 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 | 4.4570 | 1 | 1 |
| cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| incb-018424 | Homo sapiens (human) | EC50 | 1.2747 | 3 | 3 |
| incb-018424 | Homo sapiens (human) | Kd | 0.0111 | 3 | 3 |
| gsk 1838705a | Homo sapiens (human) | Kd | 5.3000 | 1 | 1 |
| azd2014 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| plx4032 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 1363089 | Homo sapiens (human) | Kd | 1.5000 | 1 | 1 |
| as 703026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| dabrafenib | Homo sapiens (human) | Kd | 3.2230 | 1 | 1 |
| mk-8033 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| nvp-bsk805 | Homo sapiens (human) | Kd | 42.0000 | 1 | 1 |
| gsk 1070916 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| glpg0634 | Homo sapiens (human) | Kd | 0.0320 | 1 | 0 |
| encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms-911543 | Homo sapiens (human) | Kd | 15.0002 | 2 | 2 |
| cep-32496 | Homo sapiens (human) | Kd | 4.7000 | 1 | 1 |
| gs-9973 | Homo sapiens (human) | EC50 | 0.4530 | 1 | 1 |
| at 9283 | Homo sapiens (human) | Kd | 0.0110 | 1 | 1 |
| chir 258 | Homo sapiens (human) | Kd | 12.3767 | 3 | 3 |
| nintedanib | Homo sapiens (human) | Kd | 0.0595 | 2 | 2 |
| pp242 | Homo sapiens (human) | Kd | 0.0110 | 1 | 1 |
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| tofacitinib | Homo sapiens (human) | fIC50 | 0.0538 | 6 | 6 |
| tofacitinib | Homo sapiens (human) | INH | 0.5620 | 2 | 2 |
| baricitinib | Homo sapiens (human) | INH | 0.1580 | 2 | 2 |
| sb 1518 | Homo sapiens (human) | IC5 | 0.0230 | 1 | 1 |
Synthesis and structure-activity relationships of 4-fluorophenyl-imidazole p38α MAPK, CK1δ and JAK2 kinase inhibitors.Bioorganic & medicinal chemistry letters, , Aug-01, Volume: 24, Issue:15, 2014
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
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
Synthesis and biological evaluation of new [1,2,4]triazolo[4,3-a]pyridine derivatives as potential c-Met inhibitors.Bioorganic & medicinal chemistry, , 08-15, Volume: 24, Issue:16, 2016
Design, Synthesis, and Antitumor Evaluation of 4-Amino-(1ACS medicinal chemistry letters, , Oct-13, Volume: 7, Issue:10, 2016
Design, synthesis and preliminary biological evaluation of 4-aminopyrazole derivatives as novel and potent JAKs inhibitors.Bioorganic & medicinal chemistry, , 06-15, Volume: 24, Issue:12, 2016
Design, synthesis and biological evaluation of pyrazol-furan carboxamide analogues as novel Akt kinase inhibitors.European journal of medicinal chemistry, , Jul-19, Volume: 117, 2016
Synthesis and biological evaluation of 3-([1,2,4]triazolo[4,3-a]pyridin-3-yl)-4-(indol-3-yl)-maleimides as potent, selective GSK-3β inhibitors and neuroprotective agents.Bioorganic & medicinal chemistry, , Mar-01, Volume: 23, Issue:5, 2015
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
Synthesis, activity, and pharmacophore development for isatin-beta-thiosemicarbazones with selective activity toward multidrug-resistant cells.Journal of medicinal chemistry, , May-28, Volume: 52, Issue:10, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, 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
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
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
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD).Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 21, Issue:23, 2011
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
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
Erlotinib effectively inhibits JAK2V617F activity and polycythemia vera cell growth.The Journal of biological chemistry, , Feb-09, Volume: 282, Issue:6, 2007
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
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
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 small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Conversion of a False Virtual Screen Hit into Selective JAK2 JH2 Domain Binders Using Convergent Design Strategies.ACS medicinal chemistry letters, , May-12, Volume: 13, Issue:5, 2022
Insights on JAK2 Modulation by Potent, Selective, and Cell-Permeable Pseudokinase-Domain Ligands.Journal of medicinal chemistry, , 06-23, Volume: 65, Issue:12, 2022
Selective Janus Kinase 2 (JAK2) Pseudokinase Ligands with a Diaminotriazole Core.Journal of medicinal chemistry, , 05-28, Volume: 63, Issue:10, 2020
JAK2 JH2 Fluorescence Polarization Assay and Crystal Structures for Complexes with Three Small Molecules.ACS medicinal chemistry letters, , Jun-08, Volume: 8, Issue:6, 2017
Identification and Characterization of JAK2 Pseudokinase Domain Small Molecule Binders.ACS medicinal chemistry letters, , Jun-08, Volume: 8, Issue:6, 2017
Diamino-1,2,4-triazole derivatives are selective inhibitors of TYK2 and JAK1 over JAK2 and JAK3.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 20, Issue:24, 2010
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Pyridones in drug discovery: Recent advances.Bioorganic & medicinal chemistry letters, , 04-15, Volume: 38, 2021
Benzimidazole Derivatives as Potent JAK1-Selective Inhibitors.Journal of medicinal chemistry, , Sep-24, Volume: 58, Issue:18, 2015
Jak1 has a dominant role over Jak3 in signal transduction through γc-containing cytokine receptors.Chemistry & biology, , Mar-25, Volume: 18, Issue:3, 2011
Virtual screening to successfully identify novel janus kinase 3 inhibitors: a sequential focused screening approach.Journal of medicinal chemistry, , Nov-13, Volume: 51, Issue:21, 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
Photochemical preparation of a pyridone containing tetracycle: a Jak protein kinase inhibitor.Bioorganic & medicinal chemistry letters, , Apr-22, Volume: 12, Issue:8, 2002
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery and development of aurora kinase inhibitors as anticancer agents.Journal of medicinal chemistry, , May-14, Volume: 52, Issue:9, 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
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
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Synthesis and evaluation of hydrazinyl-containing pyrrolo[2,3-d]pyrimidine series as potent, selective and oral JAK1 inhibitors for the treatment of rheumatoid arthritis.Bioorganic & medicinal chemistry letters, , 10-15, Volume: 74, 2022
[no title available]Journal of medicinal chemistry, , 08-11, Volume: 65, Issue:15, 2022
[no title available]Journal of medicinal chemistry, , 09-22, Volume: 65, Issue:18, 2022
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.Journal of medicinal chemistry, , 02-25, Volume: 64, Issue:4, 2021
Discovery and Biological Evaluation of Journal of medicinal chemistry, , 01-28, Volume: 64, Issue:2, 2021
Design and synthesis of boron-containing diphenylpyrimidines as potent BTK and JAK3 dual inhibitors.Bioorganic & medicinal chemistry, , 01-15, Volume: 28, Issue:2, 2020
Design, synthesis, and pharmacological evaluation of 4- or 6-phenyl-pyrimidine derivatives as novel and selective Janus kinase 3 inhibitors.European journal of medicinal chemistry, , Apr-01, Volume: 191, 2020
Discovery of a Janus Kinase Inhibitor Bearing a Highly Three-Dimensional Spiro Scaffold: JTE-052 (Delgocitinib) as a New Dermatological Agent to Treat Inflammatory Skin Disorders.Journal of medicinal chemistry, , 07-09, Volume: 63, Issue:13, 2020
Fragment-Based Discovery of Pyrazolopyridones as JAK1 Inhibitors with Excellent Subtype Selectivity.Journal of medicinal chemistry, , 07-09, Volume: 63, Issue:13, 2020
Discovery of a Gut-Restricted JAK Inhibitor for the Treatment of Inflammatory Bowel Disease.Journal of medicinal chemistry, , 03-26, Volume: 63, Issue:6, 2020
Structure-based design and synthesis of pyrimidine-4,6-diamine derivatives as Janus kinase 3 inhibitors.Bioorganic & medicinal chemistry, , 04-15, Volume: 27, Issue:8, 2019
Discovery of a class of highly potent Janus Kinase 1/2 (JAK1/2) inhibitors demonstrating effective cell-based blockade of IL-13 signaling.Bioorganic & medicinal chemistry letters, , 06-15, Volume: 29, Issue:12, 2019
Discovery of novel selective Janus kinase 2 (JAK2) inhibitors bearing a 1H-pyrazolo[3,4-d]pyrimidin-4-amino scaffold.Bioorganic & medicinal chemistry, , 04-15, Volume: 27, Issue:8, 2019
Discovery of potent anti-inflammatory 4-(4,5,6,7-tetrahydrofuro[3,2-c]pyridin-2-yl) pyrimidin-2-amines for use as Janus kinase inhibitors.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Identification of N-{cis-3-[Methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl}propane-1-sulfonamide (PF-04965842): A Selective JAK1 Clinical Candidate for the Treatment of Autoimmune Diseases.Journal of medicinal chemistry, , 02-08, Volume: 61, Issue:3, 2018
Development of selective inhibitors for the treatment of rheumatoid arthritis: (R)-3-(3-(Methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino)pyrrolidin-1-yl)-3-oxopropanenitrile as a JAK1-selective inhibitor.Bioorganic & medicinal chemistry, , 05-01, Volume: 26, Issue:8, 2018
Development, Optimization, and Structure-Activity Relationships of Covalent-Reversible JAK3 Inhibitors Based on a Tricyclic Imidazo[5,4- d]pyrrolo[2,3- b]pyridine Scaffold.Journal of medicinal chemistry, , 06-28, Volume: 61, Issue:12, 2018
Application of Sequential Palladium Catalysis for the Discovery of Janus Kinase Inhibitors in the Benzo[ c]pyrrolo[2,3- h][1,6]naphthyridin-5-one (BPN) Series.Journal of medicinal chemistry, , 12-13, Volume: 61, Issue:23, 2018
Dual Inhibition of TYK2 and JAK1 for the Treatment of Autoimmune Diseases: Discovery of (( S)-2,2-Difluorocyclopropyl)((1 R,5 S)-3-(2-((1-methyl-1 H-pyrazol-4-yl)amino)pyrimidin-4-yl)-3,8-diazabicyclo[3.2.1]octan-8-yl)methanone (PF-06700841).Journal of medicinal chemistry, , 10-11, Volume: 61, Issue:19, 2018
Structure-based design and synthesis of 1H-pyrazolo[3,4-d]pyrimidin-4-amino derivatives as Janus kinase 3 inhibitors.Bioorganic & medicinal chemistry, , 09-15, Volume: 26, Issue:17, 2018
Kinase Inhibitors for the Treatment of Immunological Disorders: Recent Advances.Journal of medicinal chemistry, , 10-25, Volume: 61, Issue:20, 2018
Identification of 4-(2-furanyl)pyrimidin-2-amines as Janus kinase 2 inhibitors.Bioorganic & medicinal chemistry, , 01-01, Volume: 25, Issue:1, 2017
The Discovery of 3-((4-Chloro-3-methoxyphenyl)amino)-1-((3R,4S)-4-cyanotetrahydro-2H-pyran-3-yl)-1H-pyrazole-4-carboxamide, a Highly Ligand Efficient and Efficacious Janus Kinase 1 Selective Inhibitor with Favorable Pharmacokinetic Properties.Journal of medicinal chemistry, , 12-14, Volume: 60, Issue:23, 2017
Discovery of a JAK3-Selective Inhibitor: Functional Differentiation of JAK3-Selective Inhibition over pan-JAK or JAK1-Selective Inhibition.ACS chemical biology, , 12-16, Volume: 11, Issue:12, 2016
The discovery of 2,5-isomers of triazole-pyrrolopyrimidine as selective Janus kinase 2 (JAK2) inhibitors versus JAK1 and JAK3.Bioorganic & medicinal chemistry, , 11-01, Volume: 24, Issue:21, 2016
Structure-based design and development of (benz)imidazole pyridones as JAK1-selective kinase inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 26, Issue:7, 2016
Design, synthesis and preliminary biological evaluation of 4-aminopyrazole derivatives as novel and potent JAKs inhibitors.Bioorganic & medicinal chemistry, , 06-15, Volume: 24, Issue:12, 2016
Design, synthesis and evaluation of pyrrolo[2,3-d]pyrimidine-phenylamide hybrids as potent Janus kinase 2 inhibitors.Bioorganic & medicinal chemistry letters, , 06-15, Volume: 26, Issue:12, 2016
Selective JAK3 Inhibitors with a Covalent Reversible Binding Mode Targeting a New Induced Fit Binding Pocket.Cell chemical biology, , Nov-17, Volume: 23, Issue:11, 2016
Structure activity optimization of 6H-pyrrolo[2,3-e][1,2,4]triazolo[4,3-a]pyrazines as Jak1 kinase inhibitors.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 25, Issue:20, 2015
Discovery of 3,6-dihydroimidazo[4,5-d]pyrrolo[2,3-b]pyridin-2(1H)-one derivatives as novel JAK inhibitors.Bioorganic & medicinal chemistry, , Aug-01, Volume: 23, Issue:15, 2015
Anilino-monoindolylmaleimides as potent and selective JAK3 inhibitors.Bioorganic & medicinal chemistry letters, , Feb-15, Volume: 24, Issue:4, 2014
Triazolopyridines as selective JAK1 inhibitors: from hit identification to GLPG0634.Journal of medicinal chemistry, , Nov-26, Volume: 57, Issue:22, 2014
Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases.Journal of medicinal chemistry, , Jun-26, Volume: 57, Issue:12, 2014
Scaffold hopping towards potent and selective JAK3 inhibitors: discovery of novel C-5 substituted pyrrolopyrazines.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 24, Issue:21, 2014
Linear propargylic alcohol functionality attached to the indazole-7-carboxamide as a JAK1-specific linear probe group.Bioorganic & medicinal chemistry, , Feb-01, Volume: 22, Issue:3, 2014
Identification of C-2 hydroxyethyl imidazopyrrolopyridines as potent JAK1 inhibitors with favorable physicochemical properties and high selectivity over JAK2.Journal of medicinal chemistry, , Jun-13, Volume: 56, Issue:11, 2013
Lead optimization of a 4-aminopyridine benzamide scaffold to identify potent, selective, and orally bioavailable TYK2 inhibitors.Journal of medicinal chemistry, , Jun-13, Volume: 56, Issue:11, 2013
Discovery of a series of novel 5H-pyrrolo[2,3-b]pyrazine-2-phenyl ethers, as potent JAK3 kinase inhibitors.Bioorganic & medicinal chemistry letters, , May-01, Volume: 23, Issue:9, 2013
Strategic use of conformational bias and structure based design to identify potent JAK3 inhibitors with improved selectivity against the JAK family and the kinome.Bioorganic & medicinal chemistry letters, , May-01, Volume: 23, Issue:9, 2013
3-Amido pyrrolopyrazine JAK kinase inhibitors: development of a JAK3 vs JAK1 selective inhibitor and evaluation in cellular and in vivo models.Journal of medicinal chemistry, , Jan-10, Volume: 56, Issue:1, 2013
Discovery and optimization of C-2 methyl imidazopyrrolopyridines as potent and orally bioavailable JAK1 inhibitors with selectivity over JAK2.Journal of medicinal chemistry, , Jul-12, Volume: 55, Issue:13, 2012
Identification of imidazo-pyrrolopyridines as novel and potent JAK1 inhibitors.Journal of medicinal chemistry, , Jun-28, Volume: 55, Issue:12, 2012
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery of potent and highly selective thienopyridine Janus kinase 2 inhibitors.Journal of medicinal chemistry, , Dec-22, Volume: 54, Issue:24, 2011
Identification of a potent Janus kinase 3 inhibitor with high selectivity within the Janus kinase family.Journal of medicinal chemistry, , Jan-13, Volume: 54, Issue:1, 2011
Discovery of CP-690,550: a potent and selective Janus kinase (JAK) inhibitor for the treatment of autoimmune diseases and organ transplant rejection.Journal of medicinal chemistry, , Dec-23, Volume: 53, Issue:24, 2010
Diamino-1,2,4-triazole derivatives are selective inhibitors of TYK2 and JAK1 over JAK2 and JAK3.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 20, Issue:24, 2010
Phenylaminopyrimidines as inhibitors of Janus kinases (JAKs).Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 19, Issue:20, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Examining the chirality, conformation and selective kinase inhibition of 3-((3R,4R)-4-methyl-3-(methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino)piperidin-1-yl)-3-oxopropanenitrile (CP-690,550).Journal of medicinal chemistry, , Dec-25, Volume: 51, Issue:24, 2008
Development of new pyrrolopyrimidine-based inhibitors of Janus kinase 3 (JAK3).Bioorganic & medicinal chemistry letters, , Mar-01, Volume: 17, Issue:5, 2007
Development of pyrimidine-based inhibitors of Janus tyrosine kinase 3.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 16, Issue:21, 2006
Prevention of organ allograft rejection by a specific Janus kinase 3 inhibitor.Science (New York, N.Y.), , Oct-31, Volume: 302, Issue:5646, 2003
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
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
Discovery of GS-9973, a selective and orally efficacious inhibitor of spleen tyrosine kinase.Journal of medicinal chemistry, , May-08, Volume: 57, Issue:9, 2014
Syk inhibitors with high potency in presence of blood.Bioorganic & medicinal chemistry letters, , May-15, Volume: 24, Issue:10, 2014
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
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Inhibition of colony-stimulating-factor-1 signaling in vivo with the orally bioavailable cFMS kinase inhibitor GW2580.Proceedings of the National Academy of Sciences of the United States of America, , Nov-01, Volume: 102, Issue:44, 2005
Design, synthesis and structure-activity relationship study of aminopyridine derivatives as novel inhibitors of Janus kinase 2.Bioorganic & medicinal chemistry letters, , 06-15, Volume: 29, Issue:12, 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
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
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Identification of NVP-TAE684, a potent, selective, and efficacious inhibitor of NPM-ALK.Proceedings of the National Academy of Sciences of the United States of America, , Jan-02, Volume: 104, Issue:1, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of 5-chloro-N2-[(1S)-1-(5-fluoropyrimidin-2-yl)ethyl]-N4-(5-methyl-1H-pyrazol-3-yl)pyrimidine-2,4-diamine (AZD1480) as a novel inhibitor of the Jak/Stat pathway.Journal of medicinal chemistry, , Jan-13, Volume: 54, Issue:1, 2011
Rational Design and Evaluation of 6-(Pyrimidin-2-ylamino)-3,4-dihydroquinoxalin-2(1Journal of medicinal chemistry, , 09-10, Volume: 63, Issue:17, 2020
Drug Discovery Targeting Bromodomain-Containing Protein 4.Journal of medicinal chemistry, , 06-08, Volume: 60, Issue:11, 2017
Non-kinase targets of protein kinase inhibitors.Nature reviews. Drug discovery, , Volume: 16, Issue:6, 2017
Evaluation of the anti-malarial activity and cytotoxicity of 2,4-diamino-pyrimidine-based kinase inhibitors.European journal of medicinal chemistry, , Nov-29, Volume: 124, 2016
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Development and Therapeutic Potential of NUAKs Inhibitors.Journal of medicinal chemistry, , 01-14, Volume: 64, Issue:1, 2021
Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.Journal of medicinal chemistry, , 02-25, Volume: 64, Issue:4, 2021
Kinase Inhibitors for the Treatment of Immunological Disorders: Recent Advances.Journal of medicinal chemistry, , 10-25, Volume: 61, Issue:20, 2018
Non-kinase targets of protein kinase inhibitors.Nature reviews. Drug discovery, , Volume: 16, Issue:6, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Diamino-1,2,4-triazole derivatives are selective inhibitors of TYK2 and JAK1 over JAK2 and JAK3.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 20, Issue:24, 2010
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Cyclin Dependent Kinase 9 Inhibitors for Cancer Therapy.Journal of medicinal chemistry, , 10-13, Volume: 59, Issue:19, 2016
Macrocyclic compounds as anti-cancer agents: design and synthesis of multi-acting inhibitors against HDAC, FLT3 and JAK2.European journal of medicinal chemistry, , May-05, Volume: 95, 2015
Discovery of kinase spectrum selective macrocycle (16E)-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 (SB1317/TG02), a potent inhibitor of cyclin dependent kinases (CDKs), Janus kJournal of medicinal chemistry, , Jan-12, Volume: 55, Issue:1, 2012
Design and synthesis of boron-containing diphenylpyrimidines as potent BTK and JAK3 dual inhibitors.Bioorganic & medicinal chemistry, , 01-15, Volume: 28, Issue:2, 2020
[no title available]European journal of medicinal chemistry, , Feb-10, Volume: 145, 2018
[no title available]European journal of medicinal chemistry, , Sep-08, Volume: 137, 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
Optimisation of momelotinib with improved potency and efficacy as pan-JAK inhibitor.Bioorganic & medicinal chemistry letters, , 06-15, Volume: 66, 2022
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Discovery of Janus Kinase 2 (JAK2) and Histone Deacetylase (HDAC) Dual Inhibitors as a Novel Strategy for the Combinational Treatment of Leukemia and Invasive Fungal Infections.Journal of medicinal chemistry, , Jul-26, Volume: 61, Issue:14, 2018
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Phenylaminopyrimidines as inhibitors of Janus kinases (JAKs).Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 19, Issue:20, 2009
Discovery and antiparasitic activity of AZ960 as a Trypanosoma brucei ERK8 inhibitor.Bioorganic & medicinal chemistry, , 10-01, Volume: 24, Issue:19, 2016
In vitro and in vivo evaluation of 6-aminopyrazolyl-pyridine-3-carbonitriles as JAK2 kinase inhibitors.Bioorganic & medicinal chemistry letters, , May-15, Volume: 21, Issue:10, 2011
Insights on JAK2 Modulation by Potent, Selective, and Cell-Permeable Pseudokinase-Domain Ligands.Journal of medicinal chemistry, , 06-23, Volume: 65, Issue:12, 2022
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Pyrazole-containing pharmaceuticals: target, pharmacological activity, and their SAR studies.RSC medicinal chemistry, , Nov-16, Volume: 13, Issue:11, 2022
[no title available]Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Discovery of novel JAK2 and EGFR inhibitors from a series of thiazole-based chalcone derivatives.RSC medicinal chemistry, , Mar-01, Volume: 12, Issue:3, 2021
Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.Journal of medicinal chemistry, , 02-25, Volume: 64, Issue:4, 2021
Design, synthesis, and pharmacological evaluation of 4- or 6-phenyl-pyrimidine derivatives as novel and selective Janus kinase 3 inhibitors.European journal of medicinal chemistry, , Apr-01, Volume: 191, 2020
Discovery of (2Journal of medicinal chemistry, , 05-14, Volume: 63, Issue:9, 2020
The Exploration of Chirality for Improved Druggability within the Human Kinome.Journal of medicinal chemistry, , 01-23, Volume: 63, Issue:2, 2020
The impact of binding site waters on the activity/selectivity trade-off of Janus kinase 2 (JAK2) inhibitors.Bioorganic & medicinal chemistry, , 04-15, Volume: 27, Issue:8, 2019
Emerging and Re-Emerging Warheads for Targeted Covalent Inhibitors: Applications in Medicinal Chemistry and Chemical Biology.Journal of medicinal chemistry, , 06-27, Volume: 62, Issue:12, 2019
Design, synthesis and structure-activity relationship study of aminopyridine derivatives as novel inhibitors of Janus kinase 2.Bioorganic & medicinal chemistry letters, , 06-15, Volume: 29, Issue:12, 2019
Discovery and Optimization of a Novel Series of Highly Selective JAK1 Kinase Inhibitors.Journal of medicinal chemistry, , 06-28, Volume: 61, Issue:12, 2018
Identification of N-{cis-3-[Methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl}propane-1-sulfonamide (PF-04965842): A Selective JAK1 Clinical Candidate for the Treatment of Autoimmune Diseases.Journal of medicinal chemistry, , 02-08, Volume: 61, Issue:3, 2018
Merging of ruxolitinib and vorinostat leads to highly potent inhibitors of JAK2 and histone deacetylase 6 (HDAC6).Bioorganic & medicinal chemistry letters, , 08-15, Volume: 28, Issue:15, 2018
Design and synthesis of triple inhibitors of janus kinase (JAK), histone deacetylase (HDAC) and Heat Shock Protein 90 (HSP90).Bioorganic & medicinal chemistry letters, , 05-01, Volume: 28, Issue:8, 2018
Design and Synthesis of Ligand Efficient Dual Inhibitors of Janus Kinase (JAK) and Histone Deacetylase (HDAC) Based on Ruxolitinib and Vorinostat.Journal of medicinal chemistry, , 10-26, Volume: 60, Issue:20, 2017
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
The discovery of 2,5-isomers of triazole-pyrrolopyrimidine as selective Janus kinase 2 (JAK2) inhibitors versus JAK1 and JAK3.Bioorganic & medicinal chemistry, , 11-01, Volume: 24, Issue:21, 2016
Structure-based design and development of (benz)imidazole pyridones as JAK1-selective kinase inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 26, Issue:7, 2016
Design, synthesis and preliminary biological evaluation of 4-aminopyrazole derivatives as novel and potent JAKs inhibitors.Bioorganic & medicinal chemistry, , 06-15, Volume: 24, Issue:12, 2016
Anilino-monoindolylmaleimides as potent and selective JAK3 inhibitors.Bioorganic & medicinal chemistry letters, , Feb-15, Volume: 24, Issue:4, 2014
Triazolopyridines as selective JAK1 inhibitors: from hit identification to GLPG0634.Journal of medicinal chemistry, , Nov-26, Volume: 57, Issue:22, 2014
Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases.Journal of medicinal chemistry, , Jun-26, Volume: 57, Issue:12, 2014
Lead optimization of a 4-aminopyridine benzamide scaffold to identify potent, selective, and orally bioavailable TYK2 inhibitors.Journal of medicinal chemistry, , Jun-13, Volume: 56, Issue:11, 2013
Strategic use of conformational bias and structure based design to identify potent JAK3 inhibitors with improved selectivity against the JAK family and the kinome.Bioorganic & medicinal chemistry letters, , May-01, Volume: 23, Issue:9, 2013
Discovery and optimization of C-2 methyl imidazopyrrolopyridines as potent and orally bioavailable JAK1 inhibitors with selectivity over JAK2.Journal of medicinal chemistry, , Jul-12, Volume: 55, Issue:13, 2012
Discovery of potent and selective pyrazolopyrimidine janus kinase 2 inhibitors.Journal of medicinal chemistry, , Nov-26, Volume: 55, Issue:22, 2012
Identification of imidazo-pyrrolopyridines as novel and potent JAK1 inhibitors.Journal of medicinal chemistry, , Jun-28, Volume: 55, Issue:12, 2012
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Diamino-1,2,4-triazole derivatives are selective inhibitors of TYK2 and JAK1 over JAK2 and JAK3.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 20, Issue:24, 2010
Bicyclic Heterocyclic Replacement of an Aryl Amide Leading to Potent and Kinase-Selective Adaptor Protein 2-Associated Kinase 1 Inhibitors.Journal of medicinal chemistry, , 03-10, Volume: 65, Issue:5, 2022
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Pyrazole-containing pharmaceuticals: target, pharmacological activity, and their SAR studies.RSC medicinal chemistry, , Nov-16, Volume: 13, Issue:11, 2022
Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.Journal of medicinal chemistry, , 02-25, Volume: 64, Issue:4, 2021
[no title available]European journal of medicinal chemistry, , Jun-05, Volume: 218, 2021
Discovery, Structure-Activity Relationships, and In Vivo Evaluation of Novel Aryl Amides as Brain Penetrant Adaptor Protein 2-Associated Kinase 1 (AAK1) Inhibitors for the Treatment of Neuropathic Pain.Journal of medicinal chemistry, , 08-12, Volume: 64, Issue:15, 2021
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Discovery of potent anti-inflammatory 4-(4,5,6,7-tetrahydrofuro[3,2-c]pyridin-2-yl) pyrimidin-2-amines for use as Janus kinase inhibitors.Bioorganic & medicinal chemistry, , 06-15, Volume: 27, Issue:12, 2019
Identification of N-{cis-3-[Methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl}propane-1-sulfonamide (PF-04965842): A Selective JAK1 Clinical Candidate for the Treatment of Autoimmune Diseases.Journal of medicinal chemistry, , 02-08, Volume: 61, Issue:3, 2018
Design, synthesis and preliminary biological evaluation of 4-aminopyrazole derivatives as novel and potent JAKs inhibitors.Bioorganic & medicinal chemistry, , 06-15, Volume: 24, Issue:12, 2016
Structure-Based Design and Synthesis of 3-Amino-1,5-dihydro-4H-pyrazolopyridin-4-one Derivatives as Tyrosine Kinase 2 Inhibitors.Journal of medicinal chemistry, , Jan-28, Volume: 59, Issue:2, 2016
Structure activity optimization of 6H-pyrrolo[2,3-e][1,2,4]triazolo[4,3-a]pyrazines as Jak1 kinase inhibitors.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 25, Issue:20, 2015
Benzimidazole Derivatives as Potent JAK1-Selective Inhibitors.Journal of medicinal chemistry, , Sep-24, Volume: 58, Issue:18, 2015
Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases.Journal of medicinal chemistry, , Jun-26, Volume: 57, Issue:12, 2014
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Fibrogenic Disorders in Human Diseases: From Inflammation to Organ Dysfunction.Journal of medicinal chemistry, , 11-21, Volume: 61, Issue:22, 2018
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
FLT3 Inhibitors in Acute Myeloid Leukemia: Challenges and Recent Developments in Overcoming Resistance.Journal of medicinal chemistry, , 03-25, Volume: 64, Issue:6, 2021
Dual FLT3 inhibitors: Against the drug resistance of acute myeloid leukemia in recent decade.European journal of medicinal chemistry, , Sep-15, Volume: 178, 2019
Design and Synthesis of Janus Kinase 2 (JAK2) and Histone Deacetlyase (HDAC) Bispecific Inhibitors Based on Pacritinib and Evidence of Dual Pathway Inhibition in Hematological Cell Lines.Journal of medicinal chemistry, , Sep-22, Volume: 59, Issue:18, 2016
Discovery of the macrocycle 11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[19.3.1.1(2,6).1(8,12)]heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene (SB1518), a potent Janus kinase 2/fms-like tyrosine kinase-3 (JAK2/FLT3) inhibitor Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
JAK2 JH2 Fluorescence Polarization Assay and Crystal Structures for Complexes with Three Small Molecules.ACS medicinal chemistry letters, , Jun-08, Volume: 8, Issue:6, 2017
Discovery and SAR of potent, orally available 2,8-diaryl-quinoxalines as a new class of JAK2 inhibitors.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 20, Issue:8, 2010
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Identification of TUL01101: A Novel Potent and Selective JAK1 Inhibitor for the Treatment of Rheumatoid Arthritis.Journal of medicinal chemistry, , 12-22, Volume: 65, Issue:24, 2022
Small molecule approaches to treat autoimmune and inflammatory diseases (Part I): Kinase inhibitors.Bioorganic & medicinal chemistry letters, , 04-15, Volume: 38, 2021
Discovery and Biological Evaluation of Journal of medicinal chemistry, , 01-28, Volume: 64, Issue:2, 2021
Discovery of triazolo [1,5-a] pyridine derivatives as novel JAK1/2 inhibitors.Bioorganic & medicinal chemistry letters, , 07-15, Volume: 30, Issue:14, 2020
Design, synthesis and evaluation of (MedChemComm, , Mar-01, Volume: 9, Issue:3, 2018
Benzimidazole Derivatives as Potent JAK1-Selective Inhibitors.Journal of medicinal chemistry, , Sep-24, Volume: 58, Issue:18, 2015
Triazolopyridines as selective JAK1 inhibitors: from hit identification to GLPG0634.Journal of medicinal chemistry, , Nov-26, Volume: 57, Issue:22, 2014
Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases.Journal of medicinal chemistry, , Jun-26, Volume: 57, Issue:12, 2014
[no title available],
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Discovery of a Janus Kinase Inhibitor Bearing a Highly Three-Dimensional Spiro Scaffold: JTE-052 (Delgocitinib) as a New Dermatological Agent to Treat Inflammatory Skin Disorders.Journal of medicinal chemistry, , 07-09, Volume: 63, Issue:13, 2020
Discovery of a class of highly potent Janus Kinase 1/2 (JAK1/2) inhibitors demonstrating effective cell-based blockade of IL-13 signaling.Bioorganic & medicinal chemistry letters, , 06-15, Volume: 29, Issue:12, 2019
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of a Highly Selective JAK2 Inhibitor, BMS-911543, for the Treatment of Myeloproliferative Neoplasms.ACS medicinal chemistry letters, , Aug-13, Volume: 6, Issue:8, 2015
Monomeric Targeted Protein Degraders.Journal of medicinal chemistry, , 10-22, Volume: 63, Issue:20, 2020
Design and Synthesis of a Pan-Janus Kinase Inhibitor Clinical Candidate (PF-06263276) Suitable for Inhaled and Topical Delivery for the Treatment of Inflammatory Diseases of the Lungs and Skin.Journal of medicinal chemistry, , 01-26, Volume: 60, Issue:2, 2017
Benzimidazole Derivatives as Potent JAK1-Selective Inhibitors.Journal of medicinal chemistry, , Sep-24, Volume: 58, Issue:18, 2015
Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases.Journal of medicinal chemistry, , Jun-26, Volume: 57, Issue:12, 2014
Recent Developments in the Use of Kinase Inhibitors for Management of Viral Infections.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Design, synthesis, biological activity evaluation of 3-(4-phenyl-1H-imidazol-2-yl)-1H-pyrazole derivatives as potent JAK 2/3 and aurora A/B kinases multi-targeted inhibitors.European journal of medicinal chemistry, , Jan-01, Volume: 209, 2021
Identification and Characterization of JAK2 Pseudokinase Domain Small Molecule Binders.ACS medicinal chemistry letters, , Jun-08, Volume: 8, Issue:6, 2017
Fragment-based discovery of the pyrazol-4-yl urea (AT9283), a multitargeted kinase inhibitor with potent aurora kinase activity.Journal of medicinal chemistry, , Jan-22, Volume: 52, Issue:2, 2009
Discovery and development of aurora kinase inhibitors as anticancer agents.Journal of medicinal chemistry, , May-14, Volume: 52, Issue:9, 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
Enables
This protein enables 20 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 tyrosine kinase activity | molecular function | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. [RHEA:10596] |
| non-membrane spanning protein tyrosine kinase activity | molecular function | Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein. [EC:2.7.10.2] |
| 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] |
| growth hormone receptor binding | molecular function | Binding to a growth hormone receptor. [GOC:ai] |
| interleukin-12 receptor binding | molecular function | Binding to an interleukin-12 receptor. [GOC:ai] |
| 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 binding | molecular function | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. [GOC:jl] |
| heme binding | molecular function | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. [GOC:ai] |
| type 1 angiotensin receptor binding | molecular function | Binding to a type 1 angiotensin receptor. [GOC:mah, GOC:nln] |
| acetylcholine receptor binding | molecular function | Binding to an acetylcholine receptor. [GOC:mah] |
| histone H3Y41 kinase activity | molecular function | Catalysis of the reaction: histone H3-tyrosine (position 41) + ATP = histone H3-phosphotyrosine (position 41) + ADP. This reaction is the addition of a phosphate group to the tyrosine residue at position 41 of histone H3. [GOC:bf] |
| SH2 domain binding | molecular function | Binding to a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class. [GOC:go_curators, Pfam:PF00017] |
| histone binding | molecular function | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. [GOC:jl, PMID:16209651, PMID:30212449, PMID:9305837] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| phosphatidylinositol 3-kinase binding | molecular function | Binding to a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring. [PMID:10209156, PMID:9255069] |
| insulin receptor substrate binding | molecular function | Binding to an insulin receptor substrate (IRS) protein, an adaptor protein that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex. [PMID:12829233] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| peptide hormone receptor binding | molecular function | Binding to a receptor for a peptide hormone. [GOC:ai] |
Located In
This protein is located in 12 target(s):
| Target | Category | Definition |
|---|
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| 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] |
| cytoskeleton | cellular component | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. [GOC:mah, PMID:16959967, PMID:27419875] |
| 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] |
| caveola | cellular component | A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis. Caveolae may be pinched off to form free vesicles within the cytoplasm. [GOC:mah, ISBN:0721662544, PMID:16645198] |
| focal adhesion | cellular component | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002] |
| endosome lumen | cellular component | The volume enclosed by the membrane of an endosome. [GOC:mah] |
| membrane raft | cellular component | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. [PMID:16645198, PMID:20044567] |
| postsynapse | cellular component | The part of a synapse that is part of the post-synaptic cell. [GOC:dos] |
| glutamatergic synapse | cellular component | A synapse that uses glutamate as a neurotransmitter. [GOC:dos] |
Active In
This protein is active in 3 target(s):
| Target | Category | Definition |
|---|
| extrinsic component of plasma membrane | cellular component | The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. [GOC:curators, GOC:dos] |
| extrinsic component of cytoplasmic side of plasma membrane | cellular component | The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region. [GOC:mah] |
| 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 4 target(s):
| Target | Category | Definition |
|---|
| granulocyte macrophage colony-stimulating factor receptor complex | cellular component | The heterodimeric receptor for granulocyte macrophage colony-stimulating factor. [GOC:mah] |
| interleukin-12 receptor complex | cellular component | A protein complex that binds interleukin-12 and that consists of, at a minimum, a dimeric interleukin and its two receptor subunits as well as optional additional kinase subunits. [GOC:ebc, GOC:mah, PMID:10971505] |
| interleukin-23 receptor complex | cellular component | A protein complex that binds interleukin-23 and that consists of, at a minimum, a dimeric interleukin and its two receptor subunits as well as optional additional kinase subunits. [GOC:BHF, GOC:mah, PMID:12023369] |
| euchromatin | cellular component | A dispersed and relatively uncompacted form of chromatin that is in a transcription-competent conformation. [PMID:32017156] |
Involved In
This protein is involved in 93 target(s):
| Target | Category | Definition |
|---|
| microglial cell activation | biological process | The change in morphology and behavior of a microglial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. [GOC:mgi_curators, PMID:10626665, PMID:10695728, PMID:12580336, PMID:9893949] |
| adaptive immune response | biological process | An immune response mediated by cells expressing specific receptors for antigens produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). [GO_REF:0000022, GOC:add, ISBN:0781735149] |
| chromatin remodeling | biological process | A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. [GOC:jid, GOC:vw, PMID:12042764, PMID:12697820] |
| transcription by RNA polymerase II | biological process | The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs). [GOC:jl, GOC:txnOH, ISBN:0321000382] |
| protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
| apoptotic process | biological process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. [GOC:cjm, GOC:dhl, GOC:ecd, GOC:go_curators, GOC:mtg_apoptosis, GOC:tb, ISBN:0198506732, PMID:18846107, PMID:21494263] |
| activation of cysteine-type endopeptidase activity involved in apoptotic process | biological process | Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process. [GOC:al, GOC:dph, GOC:jl, GOC:mtg_apoptosis, GOC:tb, PMID:14744432, PMID:18328827, Wikipedia:Caspase] |
| immune response | biological process | Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat. [GO_REF:0000022, GOC:add] |
| signal transduction | biological process | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11] |
| enzyme-linked receptor protein signaling pathway | biological process | The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell, where the receptor possesses catalytic activity or is closely associated with an enzyme such as a protein kinase, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling, ISBN:0815316194] |
| G protein-coupled receptor signaling pathway | biological process | The series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane. [GOC:bf, GOC:mah, PMID:16902576, PMID:24568158, Wikipedia:G_protein-coupled_receptor] |
| positive regulation of cytosolic calcium ion concentration | biological process | Any process that increases the concentration of calcium ions in the cytosol. [GOC:ai] |
| cell surface receptor signaling pathway via JAK-STAT | biological process | A cell surface receptor signaling pathway in which ligand binding causes the receptor to dimerize, bringing the receptor-associated JAKs into close proximity. The JAKs then phosphorylate and activate each other on tyrosine residues.This leads to the activation of associated STAT protein, causing the STATs to dissociate from the receptor, translocate to the nucleus. The pathway ends with regulation of target gene expression by STAT proteins. [PMID:12039028] |
| tyrosine phosphorylation of STAT protein | biological process | The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein. [GOC:jl, PMID:10918594] |
| mesoderm development | biological process | The process whose specific outcome is the progression of the mesoderm over time, from its formation to the mature structure. The mesoderm is the middle germ layer that develops into muscle, bone, cartilage, blood and connective tissue. [GOC:dph, GOC:tb] |
| negative regulation of cell population proliferation | biological process | Any process that stops, prevents or reduces the rate or extent of cell proliferation. [GOC:go_curators] |
| intrinsic apoptotic signaling pathway in response to oxidative stress | biological process | The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, and ends when the execution phase of apoptosis is triggered. [GOC:ai, GOC:mtg_apoptosis] |
| negative regulation of cardiac muscle cell apoptotic process | biological process | Any process that decreases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death. [GOC:BHF, GOC:dph, GOC:mtg_apoptosis, GOC:rl, GOC:tb] |
| positive regulation of cell-substrate adhesion | biological process | Any process that increases the frequency, rate or extent of cell-substrate adhesion. Cell-substrate adhesion is the attachment of a cell to the underlying substrate via adhesion molecules. [GOC:dph, GOC:pf, GOC:tb] |
| response to amine | 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 amine stimulus. An amine is a compound formally derived from ammonia by replacing one, two or three hydrogen atoms by hydrocarbyl groups. [GOC:ef] |
| peptidyl-tyrosine phosphorylation | biological process | The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. [RESID:AA0039] |
| cytokine-mediated signaling pathway | biological process | The series of molecular signals initiated by the binding of a cytokine to a receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling, PMID:19295629] |
| negative regulation of cell-cell adhesion | biological process | Any process that stops, prevents or reduces the rate or extent of cell adhesion to another cell. [GOC:isa_complete] |
| actin filament polymerization | biological process | Assembly of actin filaments by the addition of actin monomers to a filament. [GOC:mah] |
| 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] |
| erythrocyte differentiation | biological process | The process in which a myeloid precursor cell acquires specializes features of an erythrocyte. [GOC:mah] |
| positive regulation of cell migration | biological process | Any process that activates or increases the frequency, rate or extent of cell migration. [GOC:go_curators] |
| axon regeneration | biological process | The regrowth of axons following their loss or damage. [GOC:dgh, GOC:dph, GOC:tb] |
| intracellular mineralocorticoid receptor signaling pathway | biological process | The series of molecular signals initiated by mineralocorticoid binding to its nuclear receptor inside the cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, PMID:11027914, PMID:12606724] |
| positive regulation of insulin secretion | biological process | Any process that activates or increases the frequency, rate or extent of the regulated release of insulin. [GOC:mah] |
| response to lipopolysaccharide | biological process | Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. [GOC:add, ISBN:0721601464] |
| positive regulation of type II interferon production | biological process | Any process that activates or increases the frequency, rate, or extent of interferon-gamma production. Interferon-gamma is also known as type II interferon. [GOC:add, GOC:mah, PMID:15546383] |
| positive regulation of interleukin-1 beta production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production. [GOC:mah] |
| positive regulation of interleukin-17 production | biological process | Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines. [GOC:add, GOC:mah, PMID:16482511] |
| positive regulation of tumor necrosis factor production | biological process | Any process that activates or increases the frequency, rate or extent of tumor necrosis factor production. [GO_REF:0000058, GOC:TermGenie, PMID:10891884, PMID:15560120] |
| positive regulation of natural killer cell proliferation | biological process | Any process that activates or increases the frequency, rate or extent of natural killer cell proliferation. [GOC:mah] |
| response to hydroperoxide | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydroperoxide stimulus. Hydroperoxides are monosubstitution products of hydrogen peroxide, HOOH. [GOC:mah] |
| tumor necrosis factor-mediated signaling pathway | biological process | The series of molecular signals initiated by tumor necrosis factor binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling] |
| symbiont-induced defense-related programmed cell death | biological process | Cell death resulting from activation of endogenous cellular processes after interaction with a symbiont (defined as the smaller of two, or more, organisms engaged in symbiosis, a close interaction encompassing mutualism through parasitism). This can be triggered by direct interaction with the organism, for example, contact with penetrating hyphae of a fungus; or an indirect interaction such as symbiont-secreted molecules. [GOC:pamgo_curators] |
| response to tumor necrosis factor | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus. [GOC:mah] |
| post-embryonic hemopoiesis | biological process | The stages of blood cell formation that take place after completion of embryonic development. [GOC:bf] |
| intracellular signal transduction | biological process | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. [GOC:bf, GOC:jl, GOC:signaling, ISBN:3527303782] |
| interleukin-12-mediated signaling pathway | biological process | The series of molecular signals initiated by interleukin-12 binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:BHF, GOC:signaling] |
| 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] |
| interleukin-5-mediated signaling pathway | biological process | The series of molecular signals initiated by interleukin-5 binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling] |
| collagen-activated signaling pathway | biological process | The series of molecular signals initiated by collagen binding to a cell surface receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:bf, GOC:uh, PMID:21568710] |
| interleukin-3-mediated signaling pathway | biological process | The series of molecular signals initiated by interleukin-3 binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling] |
| granulocyte-macrophage colony-stimulating factor signaling pathway | biological process | The series of molecular signals initiated by the binding of the cytokine granulocyte macrophage colony-stimulating factor (GM-CSF) to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. GM-CSF binds to a heterodimer receptor (CSF2R) consisting of an alpha ligand-binding subunit, and a common beta subunit that is shared with other cytokine receptors. [GOC:nhn, GOC:signaling, PMID:17027509] |
| positive regulation of T cell proliferation | biological process | Any process that activates or increases the rate or extent of T cell proliferation. [GOC:ai] |
| positive regulation of protein import into nucleus | biological process | Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus. [GOC:jl] |
| positive regulation of tyrosine phosphorylation of STAT protein | biological process | Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein. [GOC:jl, PMID:11426647] |
| activation of Janus kinase activity | biological process | The process of introducing a phosphate group to a tyrosine residue of a JAK (Janus Activated Kinase) protein, thereby activating it. [GOC:jl, PMID:12479803] |
| negative regulation of DNA binding | biological process | Any process that stops or reduces the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid). [GOC:dph, GOC:jl, GOC:tb] |
| positive regulation of MAPK cascade | biological process | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. [GOC:go_curators] |
| 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] |
| post-translational protein modification | biological process | The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome. [GOC:jsg] |
| positive regulation of MHC class II biosynthetic process | biological process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of MHC class II. [GOC:go_curators] |
| regulation of nitric oxide biosynthetic process | biological process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nitric oxide. [GOC:go_curators] |
| positive regulation of nitric oxide biosynthetic process | biological process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nitric oxide. [GOC:go_curators] |
| positive regulation of cell differentiation | biological process | Any process that activates or increases the frequency, rate or extent of cell differentiation. [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] |
| regulation of receptor signaling pathway via JAK-STAT | biological process | Any process that modulates the frequency, rate or extent of receptor signaling via JAK-STAT. [GOC:bf] |
| positive regulation of receptor signaling pathway via JAK-STAT | biological process | Any process that activates or increases the frequency, rate or extent of the JAK-STAT signaling pathway activity. [GOC:bf] |
| protein autophosphorylation | biological process | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). [ISBN:0198506732] |
| platelet-derived growth factor receptor signaling pathway | biological process | The series of molecular signals initiated by a ligand binding to a platelet-derived growth factor receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:ceb] |
| regulation of inflammatory response | biological process | Any process that modulates the frequency, rate or extent of the inflammatory response, the immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. [GOC:ai] |
| modulation of chemical synaptic transmission | biological process | Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission. [GOC:ai] |
| positive regulation of NK T cell proliferation | biological process | Any process that activates or increases the frequency, rate or extent of natural killer T cell proliferation. [ISBN:0781735149, PMID:12154375, PMID:9133426] |
| positive regulation of nitric-oxide synthase biosynthetic process | biological process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of a nitric oxide synthase enzyme. [GOC:ai] |
| positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | biological process | Any process that activates or increases the frequency, rate or extent of phosphatidylinositol 3-kinase/protein kinase B signal transduction. [GOC:ai] |
| type II interferon-mediated signaling pathway | biological process | The series of molecular signals initiated by interferon-gamma binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. Interferon gamma is the only member of the type II interferon found so far. [GOC:add, GOC:dph, GOC:signaling, PMID:28901902] |
| growth hormone receptor signaling pathway | biological process | The series of molecular signals generated as a consequence of growth hormone receptor binding to its physiological ligand. [GOC:BHF, GOC:dph, PMID:11445442] |
| growth hormone receptor signaling pathway via JAK-STAT | biological process | The process in which STAT proteins (Signal Transducers and Activators of Transcription) are activated by members of the JAK (janus activated kinase) family of tyrosine kinases, following the binding of physiological ligands to the growth hormone receptor. Once activated, STATs dimerize and translocate to the nucleus and modulate the expression of target genes. [GOC:BHF, GOC:dph, PMID:11445442] |
| positive regulation of growth hormone receptor signaling pathway | biological process | Any process that increases the rate, frequency or extent of the growth hormone receptor signaling pathway. The growth hormone receptor signaling pathway is the series of molecular signals generated as a consequence of growth hormone receptor binding to its physiological ligand. [GOC:BHF, GOC:dph] |
| mammary gland epithelium development | biological process | The process whose specific outcome is the progression of the mammary gland epithelium over time, from its formation to the mature structure. The mammary gland is a large compound sebaceous gland that in female mammals is modified to secrete milk. [GOC:dph, GOC:yaf] |
| interleukin-6-mediated signaling pathway | biological process | The series of molecular signals initiated by interleukin-6 binding to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:add, GOC:BHF, GOC:mah, GOC:signaling] |
| positive regulation of leukocyte proliferation | biological process | Any process that activates or increases the frequency, rate or extent of leukocyte proliferation. [GOC:add, GOC:mah] |
| response to interleukin-12 | 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-12 stimulus. [GOC:mah] |
| interleukin-35-mediated signaling pathway | biological process | The series of molecular signals initiated by interleukin-35 binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:add, GOC:mah, GOC:signaling] |
| cellular response to lipopolysaccharide | 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 lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. [GOC:mah] |
| cellular response to dexamethasone 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 dexamethasone stimulus. [GOC:mah, GOC:yaf] |
| 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] |
| activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway | biological process | Any process that initiates the activity of an inactive cysteine-type endopeptidase involved in the apoptotic signaling pathway. [GOC:mtg_apoptosis] |
| cellular response to virus | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a virus. [GOC:dos] |
| positive regulation of cold-induced thermogenesis | biological process | Any process that activates or increases the frequency, rate or extent of cold-induced thermogenesis. [PMID:27876809] |
| positive regulation of growth factor dependent skeletal muscle satellite cell proliferation | biological process | Any process that activates or increases the frequency, rate or extent of satellite cell proliferation; dependent on specific growth factor activity such as fibroblast growth factors and transforming growth factor beta. [GO_REF:0000058, GOC:TermGenie, PMID:23212449] |
| positive regulation of epithelial cell apoptotic process | biological process | Any process that activates or increases the frequency, rate or extent of epithelial cell apoptotic process. [GO_REF:0000058, GOC:TermGenie, PMID:19137015] |
| positive regulation of vascular associated smooth muscle cell proliferation | biological process | Any process that activates or increases the frequency, rate or extent of vascular smooth muscle cell proliferation. [GO_REF:0000058, GOC:TermGenie, PMID:23246467] |
| regulation of postsynapse to nucleus signaling pathway | biological process | Any process that modulates the frequency, rate or extent of postsynapse to nucleus signaling pathway. [GO_REF:0000058, GOC:TermGenie, ISBN:9780071120005] |
| positive regulation of signaling receptor activity | biological process | Any process that activates or increases the frequency, rate or extent of signaling receptor activity. [GOC:obol] |
| positive regulation of T-helper 17 type immune response | biological process | Any process that activates or increases the frequency, rate or extent of T-helper 17 type immune response. [GOC:BHF, GOC:mah] |
| positive regulation of apoptotic signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of apoptotic signaling pathway. [GOC:mtg_apoptosis] |
| regulation of apoptotic process | biological process | Any process that modulates the occurrence or rate of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |