Page last updated: 2024-08-07 16:41:03
Tyrosine-protein kinase SYK
A tyrosine-protein kinase SYK that is encoded in the genome of human. [PRO:CNA, UniProtKB:P43405]
Synonyms
EC 2.7.10.2;
Spleen tyrosine kinase;
p72-Syk
Research
Bioassay Publications (59)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 17 (28.81) | 29.6817 |
| 2010's | 36 (61.02) | 24.3611 |
| 2020's | 6 (10.17) | 2.80 |
Compounds (265)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| imatinib | Homo sapiens (human) | IC50 | 7.5000 | 2 | 2 |
| imatinib | Homo sapiens (human) | Ki | 5.0000 | 2 | 2 |
| 1,3-diphenylurea | Homo sapiens (human) | IC50 | 660.0000 | 1 | 1 |
| 1,4-diaminoanthraquinone | Homo sapiens (human) | IC50 | 40.0000 | 1 | 1 |
| staurosporine | Homo sapiens (human) | IC50 | 0.0057 | 13 | 13 |
| rivastigmine | Homo sapiens (human) | IC50 | 0.1600 | 1 | 1 |
| birb 796 | Homo sapiens (human) | IC50 | 25.0000 | 2 | 2 |
| tv3326 | Homo sapiens (human) | IC50 | 0.4800 | 1 | 1 |
| ag-213 | Homo sapiens (human) | IC50 | 38.0000 | 1 | 1 |
| 3,3',4,5'-tetrahydroxystilbene | Homo sapiens (human) | IC50 | 24.0000 | 2 | 2 |
| vx-745 | Homo sapiens (human) | IC50 | 5.0000 | 1 | 1 |
| dasatinib | Homo sapiens (human) | IC50 | 4.8200 | 1 | 0 |
| quercetin | Homo sapiens (human) | IC50 | 20.0000 | 1 | 1 |
| apigenin | Homo sapiens (human) | IC50 | 4.2000 | 1 | 1 |
| luteolin | Homo sapiens (human) | IC50 | 12.0000 | 1 | 1 |
| genistein | Homo sapiens (human) | IC50 | 39.0000 | 1 | 1 |
| sulfuretin | Homo sapiens (human) | IC50 | 4.6300 | 1 | 1 |
| fisetin | Homo sapiens (human) | IC50 | 15.0000 | 1 | 1 |
| morin | Homo sapiens (human) | IC50 | 28.0000 | 1 | 1 |
| myricetin | Homo sapiens (human) | IC50 | 6.4000 | 1 | 1 |
| bosutinib | Homo sapiens (human) | IC50 | 0.0520 | 1 | 1 |
| a 770041 | Homo sapiens (human) | IC50 | 25.0000 | 1 | 1 |
| c 1368 | Homo sapiens (human) | IC50 | 0.8870 | 1 | 1 |
| bay 61-3606 | Homo sapiens (human) | Ki | 0.0075 | 1 | 1 |
| sotrastaurin | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| ucn 1028 c | Homo sapiens (human) | IC50 | 1.1000 | 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 | 0.1670 | 6 | 7 |
| 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) | Ki | 0.0300 | 1 | 1 |
| N-[5-[[5-[(4-acetyl-1-piperazinyl)-oxomethyl]-4-methoxy-2-methylphenyl]thio]-2-thiazolyl]-4-[(3,3-dimethylbutan-2-ylamino)methyl]benzamide | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
| nvp-aew541 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| gw 2580 | Homo sapiens (human) | IC50 | 16.0000 | 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 |
| fostamatinib | Homo sapiens (human) | IC50 | 16.7613 | 3 | 3 |
| 4-methyl-3-(2-(2-morpholinoethylamino)quinazolin-6-yl)-n-(3-(trifluoromethyl)phenyl)benzamide | Homo sapiens (human) | IC50 | 0.2920 | 1 | 1 |
| pci 32765 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| entrectinib | Homo sapiens (human) | IC50 | 1.0000 | 1 | 1 |
| gdc 0980 | Homo sapiens (human) | IC50 | 0.1340 | 1 | 1 |
| p505-15 | Homo sapiens (human) | IC50 | 2.1453 | 12 | 13 |
| gsk 2334470 | Homo sapiens (human) | IC50 | 25.1180 | 1 | 1 |
| gsk143 | Homo sapiens (human) | IC50 | 0.0316 | 1 | 1 |
| nms p937 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| nms-p118 | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| urmc-099 | Homo sapiens (human) | IC50 | 0.7310 | 1 | 1 |
| ceritinib | Homo sapiens (human) | IC50 | 3.0500 | 1 | 1 |
| vx-970 | Homo sapiens (human) | Ki | 0.1900 | 1 | 1 |
| gs-9973 | Homo sapiens (human) | IC50 | 2.3270 | 8 | 9 |
| nms-e973 | Homo sapiens (human) | IC50 | 0.0100 | 1 | 1 |
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| fasudil | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sb 202190 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| imatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| staurosporine | Homo sapiens (human) | Kd | 0.0117 | 3 | 3 |
| picropodophyllin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gefitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| lestaurtinib | Homo sapiens (human) | Kd | 0.0947 | 3 | 3 |
| perifosine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vatalanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| ruboxistaurin | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| canertinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| birb 796 | Homo sapiens (human) | 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 | 20.0000 | 2 | 2 |
| erlotinib | Homo sapiens (human) | Kd | 20.0000 | 3 | 4 |
| lapatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| sorafenib | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
| pd 173955 | Homo sapiens (human) | Kd | 0.4100 | 1 | 1 |
| s 1033 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| 3,3',4,5'-tetrahydroxystilbene | Homo sapiens (human) | EC50 | 15.0000 | 2 | 2 |
| xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 387032 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| sf 2370 | Homo sapiens (human) | Kd | 0.5450 | 1 | 1 |
| tandutinib | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
| vx-745 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| dasatinib | Homo sapiens (human) | Kd | 2.7517 | 3 | 3 |
| ha 1100 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| 7-epi-hydroxystaurosporine | Homo sapiens (human) | Kd | 0.2170 | 1 | 1 |
| zd 6474 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1h-imidazol-2-yl)benzamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| imd 0354 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| quercetin | Homo sapiens (human) | EC50 | 35.0000 | 1 | 1 |
| apigenin | Homo sapiens (human) | EC50 | 3.0000 | 1 | 1 |
| luteolin | Homo sapiens (human) | EC50 | 4.5000 | 1 | 1 |
| fisetin | Homo sapiens (human) | EC50 | 19.0000 | 1 | 1 |
| morin | Homo sapiens (human) | EC50 | 300.0000 | 1 | 1 |
| myricetin | Homo sapiens (human) | EC50 | 54.0000 | 1 | 1 |
| sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| alvocidib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| bosutinib | Homo sapiens (human) | Kd | 15.1450 | 2 | 2 |
| orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| su 11248 | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
| palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| jnj-7706621 | Homo sapiens (human) | Kd | 1.3000 | 1 | 1 |
| vx680 | Homo sapiens (human) | Kd | 11.2000 | 3 | 3 |
| cyc 116 | Homo sapiens (human) | Kd | 5.0680 | 1 | 1 |
| everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ekb 569 | Homo sapiens (human) | Kd | 12.8000 | 3 | 3 |
| axitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| temsirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pd 184352 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| on 01910 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| av 412 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| telatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| y-39983 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cp 547632 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms345541 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| lenvatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pd 0325901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| midostaurin | Homo sapiens (human) | Kd | 2.3725 | 4 | 4 |
| px-866 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ripasudil | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| osi 930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ki 20227 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| scio-469 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cp 724714 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| pi103 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| hmn-214 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tivozanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| hki 272 | Homo sapiens (human) | Kd | 17.5500 | 2 | 2 |
| tofacitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| cediranib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pazopanib | Homo sapiens (human) | Kd | 14.9000 | 3 | 3 |
| azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| su 14813 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| bibw 2992 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bay 61-3606 | Homo sapiens (human) | EC50 | 0.0483 | 3 | 3 |
| binimetinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sotrastaurin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| aee 788 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| saracatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vx 702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| crenolanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tg100-115 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| cc 401 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 599626 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| exel-7647 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 665752 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| azd 7762 | Homo sapiens (human) | Kd | 1.4840 | 1 | 1 |
| regorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-one | Homo sapiens (human) | EC50 | 0.0832 | 12 | 12 |
| 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 | 0.7190 | 2 | 2 |
| brivanib | Homo sapiens (human) | Kd | 23.3333 | 2 | 3 |
| mp470 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| rgb 286638 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| at 7519 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bms-690514 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bi 2536 | Homo sapiens (human) | Kd | 17.3500 | 2 | 2 |
| inno-406 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| nvp-ast487 | Homo sapiens (human) | Kd | 0.6000 | 2 | 2 |
| kw 2449 | Homo sapiens (human) | Kd | 15.3350 | 2 | 2 |
| danusertib | Homo sapiens (human) | Kd | 5.2050 | 1 | 1 |
| abt 869 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| azd 8931 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| arq 197 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd 1152 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pf 00299804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ridaforolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ch 4987655 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cc-930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
| tak 285 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| idelalisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| crizotinib | Homo sapiens (human) | Kd | 16.2500 | 2 | 2 |
| osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir-265 | Homo sapiens (human) | Kd | 14.8000 | 3 | 3 |
| motesanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| fostamatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| trametinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mln8054 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| pf-562,271 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| GDC-0879 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| jnj-26483327 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ly2603618 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tg100801 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| dactolisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bgt226 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 461364 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| azd 1152-hqpa | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| nvp-tae684 | Homo sapiens (human) | Kd | 1.3000 | 1 | 1 |
| enmd 2076 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| e 7050 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 2-amino-8-ethyl-4-methyl-6-(1H-pyrazol-5-yl)-7-pyrido[2,3-d]pyrimidinone | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tak-901 | Homo sapiens (human) | Kd | 4.6620 | 1 | 1 |
| gdc-0973 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| buparlisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd 1480 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd8330 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 848125 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| fedratinib | Homo sapiens (human) | Kd | 16.3500 | 2 | 2 |
| gsk690693 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| 14-methyl-20-oxa-5,7,14,26-tetraazatetracyclo(19.3.1.1(2,6).1(8,12))heptacosa-1(25),2(26),3,5,8(27),9,11,16,21,23-decaene | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd5438 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pf 04217903 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gdc 0941 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| icotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ph 797804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| kx-01 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| plx 4720 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| mk 5108 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cx 4945 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| arry-614 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tak 593 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mln 8237 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sgx 523 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bms 754807 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| bms 777607 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sgi 1776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pci 32765 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ponatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| amg 900 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk-1775 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| AMG-208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| quizartinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| at13148 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| tak 733 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk 2206 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sns 314 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| lucitanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pf-04691502 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| n-(cyanomethyl)-4-(2-((4-(4-morpholinyl)phenyl)amino)-4-pyrimidinyl)benzamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| dcc-2036 | Homo sapiens (human) | Kd | 1.8280 | 1 | 1 |
| cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| defactinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ly2584702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| incb-018424 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| poziotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| asp3026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| entrectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pexidartinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| TAK-580 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 2126458 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| emd1214063 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 1838705a | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| pf 3758309 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| gdc 0980 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd2014 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| (5-(2,4-bis((3s)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| plx4032 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 1363089 | Homo sapiens (human) | Kd | 15.1400 | 2 | 2 |
| arry-334543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| kin-193 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk 2461 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bay 869766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| as 703026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| baricitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| dabrafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pki 587 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| n-(3-fluoro-4-((1-methyl-6-(1h-pyrazol-4-yl)-1h-indazol-5 yl)oxy)phenyl)-1-(4-fluorophenyl)-6-methyl-2-oxo-1,2-dihydropyridine-3-carboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ribociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk-8033 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 793887 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sb 1518 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| abemaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| mk-8776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| afuresertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 1070916 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| jnj38877605 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| dinaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| gilteritinib | Homo sapiens (human) | Kd | 4.0430 | 1 | 1 |
| alectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| glpg0634 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms-911543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk2141795 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd8186 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| byl719 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cep-32496 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| rociletinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ceritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd1208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vx-509 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gs-9973 | Homo sapiens (human) | EC50 | 0.0485 | 4 | 4 |
| debio 1347 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| volitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| osimertinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| at 9283 | Homo sapiens (human) | Kd | 0.1160 | 1 | 1 |
| otssp167 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir 258 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| nintedanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pp242 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
Drug-target interactions that involve the replacement or displacement of magnesium ions.Bioorganic & medicinal chemistry letters, , 12-15, Volume: 27, Issue:24, 2017
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery and development of spleen tyrosine kinase (SYK) inhibitors.Journal of medicinal chemistry, , Apr-26, Volume: 55, Issue:8, 2012
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Pharmacophore modeling study based on known spleen tyrosine kinase inhibitors together with virtual screening for identifying novel inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 19, Issue:7, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Rational design of inhibitors that bind to inactive kinase conformations.Nature chemical biology, , Volume: 2, Issue:7, 2006
Isoxazole derivatives as anticancer agent: A review on synthetic strategies, mechanism of action and SAR studies.European journal of medicinal chemistry, , Oct-05, Volume: 221, 2021
Discovery of a potent, selective, and covalent ZAP-70 kinase inhibitor.European journal of medicinal chemistry, , Jul-05, Volume: 219, 2021
ASR352, A potent anticancer agent: Synthesis, preliminary SAR, and biological activities against colorectal cancer bulk, 5-fluorouracil/oxaliplatin resistant and stem cells.European journal of medicinal chemistry, , Jan-01, Volume: 161, 2019
Novel quinazoline derivatives bearing various 6-benzamide moieties as highly selective and potent EGFR inhibitors.Bioorganic & medicinal chemistry, , 05-01, Volume: 26, Issue:8, 2018
Novel LCK/FMS inhibitors based on phenoxypyrimidine scaffold as potential treatment for inflammatory disorders.European journal of medicinal chemistry, , Dec-01, Volume: 141, 2017
Novel pyrrolopyrimidines as Mps1/TTK kinase inhibitors for breast cancer.Bioorganic & medicinal chemistry, , 04-01, Volume: 25, Issue:7, 2017
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
Discovery of 4-arylamido 3-methyl isoxazole derivatives as novel FMS kinase inhibitors.European journal of medicinal chemistry, , Sep-18, Volume: 102, 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
Syntheses of phenylpyrazolodiazepin-7-ones as conformationally rigid analogs of aminopyrazole amide scaffold and their antiproliferative effects on cancer cells.Bioorganic & medicinal chemistry, , Nov-15, Volume: 19, Issue:22, 2011
Pharmacophore modeling study based on known spleen tyrosine kinase inhibitors together with virtual screening for identifying novel inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 19, Issue:7, 2009
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
Structure-activity relationship studies of imidazo[1,2-c]pyrimidine derivatives as potent and orally effective Syk family kinases inhibitors.Bioorganic & medicinal chemistry, , Oct-15, Volume: 16, Issue:20, 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
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
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
Pyrazole urea-based inhibitors of p38 MAP kinase: from lead compound to clinical candidate.Journal of medicinal chemistry, , Jul-04, Volume: 45, Issue:14, 2002
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery and development of spleen tyrosine kinase (SYK) inhibitors.Journal of medicinal chemistry, , Apr-26, Volume: 55, Issue:8, 2012
Pharmacophore modeling study based on known spleen tyrosine kinase inhibitors together with virtual screening for identifying novel inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 19, Issue:7, 2009
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.Proceedings of the National Academy of Sciences of the United States of America, , Dec-18, Volume: 104, Issue:51, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
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
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The Discovery of VX-745: A Novel and Selective p38α Kinase Inhibitor.ACS medicinal chemistry letters, , Oct-13, Volume: 2, Issue:10, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
[no title available],
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells.Leukemia, , Volume: 23, Issue:3, 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
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
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
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes.Journal of medicinal chemistry, , Oct-22, Volume: 52, Issue:20, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
LEADOPT: an automatic tool for structure-based lead optimization, and its application in structural optimizations of VEGFR2 and SYK inhibitors.European journal of medicinal chemistry, , Mar-26, Volume: 93, 2015
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
Discovery and development of spleen tyrosine kinase (SYK) inhibitors.Journal of medicinal chemistry, , Apr-26, Volume: 55, Issue:8, 2012
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Pharmacophore modeling study based on known spleen tyrosine kinase inhibitors together with virtual screening for identifying novel inhibitors.Bioorganic & medicinal chemistry letters, , Apr-01, Volume: 19, Issue:7, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
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
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Inhibition of colony-stimulating-factor-1 signaling in vivo with the orally bioavailable cFMS kinase inhibitor GW2580.Proceedings of the National Academy of Sciences of the United States of America, , Nov-01, Volume: 102, Issue:44, 2005
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Pyrrolopyrazines as selective spleen tyrosine kinase inhibitors.Journal of medicinal chemistry, , Feb-28, Volume: 56, Issue:4, 2013
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
[no title available]European journal of medicinal chemistry, , Feb-10, Volume: 145, 2018
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of Entrectinib: A New 3-Aminoindazole As a Potent Anaplastic Lymphoma Kinase (ALK), c-ros Oncogene 1 Kinase (ROS1), and Pan-Tropomyosin Receptor Kinases (Pan-TRKs) inhibitor.Journal of medicinal chemistry, , Apr-14, Volume: 59, Issue:7, 2016
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of a potent, selective, and orally available class I phosphatidylinositol 3-kinase (PI3K)/mammalian target of rapamycin (mTOR) kinase inhibitor (GDC-0980) for the treatment of cancer.Journal of medicinal chemistry, , Nov-10, Volume: 54, Issue:21, 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
3-aminopyrazolopyrazine derivatives as spleen tyrosine kinase inhibitors.Chemical biology & drug design, , Volume: 88, Issue:5, 2016
Discovery and profiling of a selective and efficacious Syk inhibitor.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 2015
Orally bioavailable Syk inhibitors with activity in a rat PK/PD model.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 25, Issue:20, 2015
Syk inhibitors with high potency in presence of blood.Bioorganic & medicinal chemistry letters, , May-15, Volume: 24, Issue:10, 2014
Pyrrolopyrazines as selective spleen tyrosine kinase inhibitors.Journal of medicinal chemistry, , Feb-28, Volume: 56, Issue:4, 2013
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Synthesis, structure-activity relationships, and in vivo efficacy of the novel potent and selective anaplastic lymphoma kinase (ALK) inhibitor 5-chloro-N2-(2-isopropoxy-5-methyl-4-(piperidin-4-yl)phenyl)-N4-(2-(isopropylsulfonyl)phenyl)pyrimidine-2,4-diamJournal of medicinal chemistry, , Jul-25, Volume: 56, Issue:14, 2013
Structural modification aimed for improving solubility of lead compounds in early phase drug discovery.Bioorganic & medicinal chemistry, , 02-15, Volume: 56, 2022
Scaffold hopping of the SYK inhibitor entospletinib leads to broader targeting of the BCR signalosome.European journal of medicinal chemistry, , Oct-15, Volume: 204, 2020
Discovery of Lanraplenib (GS-9876): A Once-Daily Spleen Tyrosine Kinase Inhibitor for Autoimmune Diseases.ACS medicinal chemistry letters, , Apr-09, Volume: 11, Issue:4, 2020
Discovery and profiling of a selective and efficacious Syk inhibitor.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 2015
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
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 17 target(s):
| Target | Category | Definition |
|---|
| phosphotyrosine residue binding | molecular function | Binding to a phosphorylated tyrosine residue within a protein. [PMID:14636584] |
| protein kinase activity | molecular function | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. [PMID:25399640] |
| protein serine/threonine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925] |
| 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] |
| integrin binding | molecular function | Binding to an integrin. [GOC:ceb] |
| 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] |
| interleukin-15 receptor binding | molecular function | Binding to an interleukin-15 receptor. [GOC:ai] |
| kinase activity | molecular function | Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. [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] |
| phosphatase binding | molecular function | Binding to a phosphatase. [GOC:jl] |
| Toll-like receptor binding | molecular function | Binding to a Toll-like protein, a pattern recognition receptor that binds pattern motifs from a variety of microbial sources to initiate an innate immune response. [PMID:19076341] |
| 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] |
| phospholipase binding | molecular function | Binding to a phospholipase. [GOC:jl] |
| scaffold protein binding | molecular function | Binding to a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes. [GOC:BHF, GOC:sjp, PMID:10433269, Wikipedia:Scaffold_protein] |
Located In
This protein is located in 5 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] |
| 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] |
| 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] |
| early phagosome | cellular component | A membrane-bounded intracellular vesicle as initially formed upon the ingestion of particulate material by phagocytosis. [GOC:mah, PMID:12388753] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| 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] |
Part Of
This protein is part of 3 target(s):
| Target | Category | Definition |
|---|
| B cell receptor complex | cellular component | An immunoglobulin complex that is present in the plasma membrane of B cells and that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains and a signaling subunit, a heterodimer of the Ig-alpha and Ig-beta proteins. [GOC:add, ISBN:0781735149] |
| protein-containing complex | cellular component | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah] |
| T cell receptor complex | cellular component | A protein complex that contains a disulfide-linked heterodimer of T cell receptor (TCR) chains, which are members of the immunoglobulin superfamily, and mediates antigen recognition, ultimately resulting in T cell activation. The TCR heterodimer is associated with the CD3 complex, which consists of the nonpolymorphic polypeptides gamma, delta, epsilon, zeta, and, in some cases, eta (an RNA splice variant of zeta) or Fc epsilon chains. [GOC:mah, ISBN:0781735149] |
Involved In
This protein is involved in 75 target(s):
| Target | Category | Definition |
|---|
| angiogenesis | biological process | Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels. [ISBN:0878932453] |
| cell activation | biological process | A multicellular organismal process by which exposure to an activating factor such as a cellular or soluble ligand results in a change in the morphology or behavior of a cell. [GOC:mgi_curators] |
| lymph vessel development | biological process | The process whose specific outcome is the progression of a lymph vessel over time, from its formation to the mature structure. [GOC:dph, UBERON:0001473] |
| positive regulation of receptor internalization | biological process | Any process that activates or increases the frequency, rate or extent of receptor internalization. [GOC:hjd] |
| stimulatory C-type lectin receptor signaling pathway | biological process | The series of molecular signals initiated by the binding of C-type lectin to its receptor on the surface of a target cell, and resulting in cellular activation. [GO_REF:0000022, GOC:add, ISBN:0781735149] |
| 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] |
| macrophage activation involved in immune response | biological process | A change in morphology and behavior of a macrophage resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. [GOC:add, ISBN:0781735149] |
| neutrophil activation involved in immune response | biological process | The change in morphology and behavior of a neutrophil resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. [GOC:add, ISBN:0781735149] |
| leukocyte activation involved in immune response | biological process | A change in morphology and behavior of a leukocyte resulting from exposure to a specific antigen, mitogen, cytokine, cellular ligand, or soluble factor, leading to the initiation or perpetuation of an immune response. [GOC:add, ISBN:0781735149] |
| serotonin secretion by platelet | biological process | The regulated release of serotonin by a platelet or group of platelets. [GOC:add, ISBN:0781735149] |
| negative regulation of inflammatory response to antigenic stimulus | biological process | Any process that stops, prevents, or reduces the frequency, rate, or extent of an inflammatory response to an antigenic stimulus. [GOC:add] |
| protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
| leukocyte cell-cell adhesion | biological process | The attachment of a leukocyte to another cell via adhesion molecules. [GOC:go_curators] |
| integrin-mediated signaling pathway | biological process | The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling] |
| animal organ morphogenesis | biological process | Morphogenesis of an animal organ. An organ is defined as a tissue or set of tissues that work together to perform a specific function or functions. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions. [GOC:dgh, GOC:go_curators, ISBN:0471245208, ISBN:0721662544] |
| regulation of platelet activation | biological process | Any process that modulates the rate or frequency of platelet activation. Platelet activation is a series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. [GOC:BHF, GOC:dph, GOC:tb] |
| regulation of tumor necrosis factor-mediated signaling pathway | biological process | Any process that modulates the rate or extent of the tumor necrosis factor-mediated signaling pathway. The tumor necrosis factor-mediated signaling pathway is the series of molecular signals generated as a consequence of tumor necrosis factor binding to a cell surface receptor. [GOC:dph, GOC:tb] |
| peptidyl-tyrosine phosphorylation | biological process | The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. [RESID:AA0039] |
| leukotriene biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of leukotriene, a pharmacologically active substance derived from a polyunsaturated fatty acid, such as arachidonic acid. [GOC:go_curators] |
| calcium-mediated signaling | biological process | Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions. [GOC:signaling] |
| platelet activation | biological process | A series of progressive, overlapping events triggered by exposure of the platelets to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug. [http://www.graylab.ac.uk/omd/] |
| B cell differentiation | biological process | The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity. [GO_REF:0000022, GOC:mah] |
| neutrophil chemotaxis | biological process | The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. [GOC:jl, ISBN:0198506732] |
| positive regulation of protein-containing complex assembly | biological process | Any process that activates or increases the frequency, rate or extent of protein complex assembly. [GOC:mah] |
| receptor internalization | biological process | A receptor-mediated endocytosis process that results in the movement of receptors from the plasma membrane to the inside of the cell. The process begins when cell surface receptors are monoubiquitinated following ligand-induced activation. Receptors are subsequently taken up into endocytic vesicles from where they are either targeted to the lysosome or vacuole for degradation or recycled back to the plasma membrane. [GOC:bf, GOC:mah, GOC:signaling, PMID:15006537, PMID:19643732] |
| positive regulation of type I interferon production | biological process | Any process that activates or increases the frequency, rate, or extent of type I interferon production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families. [GOC:add, GOC:mah] |
| positive regulation of granulocyte macrophage colony-stimulating factor production | biological process | Any process that activates or increases the frequency, rate, or extent of granulocyte macrophage colony-stimulating factor production. [GOC:mah] |
| positive regulation of interleukin-10 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-10 production. [GOC:mah] |
| positive regulation of interleukin-12 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-12 production. [GOC:mah] |
| positive regulation of interleukin-3 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-3 production. [GOC:mah] |
| positive regulation of interleukin-4 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-4 production. [GOC:mah] |
| positive regulation of interleukin-6 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-6 production. [GOC:mah] |
| positive regulation of interleukin-8 production | biological process | Any process that activates or increases the frequency, rate, or extent of interleukin-8 production. [GOC:mah] |
| 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 mast cell cytokine production | biological process | Any process that activates or increases the frequency, rate, or extent of mast cell cytokine production. [GOC:mah] |
| regulation of superoxide anion generation | biological process | Any process that modulates the frequency, rate or extent of enzymatic generation of superoxide by a cell. [GOC:mah] |
| positive regulation of superoxide anion generation | biological process | Any process that activates or increases the frequency, rate or extent of enzymatic generation of superoxide by a cell. [GOC:mah] |
| positive regulation of cell adhesion mediated by integrin | biological process | Any process that activates or increases the frequency, rate, or extent of cell adhesion mediated by integrin. [GOC:add] |
| 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] |
| collagen-activated tyrosine kinase receptor signaling pathway | biological process | The series of molecular signals initiated by collagen binding to its receptor on the surface of a target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:bf, GOC:uh, PMID:15888913, PMID:16626936] |
| Fc-epsilon receptor signaling pathway | biological process | The series of molecular signals initiated by the binding of the Fc portion of immunoglobulin E (IgE) to an Fc-epsilon receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region. [GOC:phg, PMID:12413516, PMID:15048725] |
| Fc-gamma receptor signaling pathway involved in phagocytosis | biological process | An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes. [GOC:phg, PMID:12488490, PMID:15466916] |
| 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] |
| gamma-delta T cell differentiation | biological process | The process in which a relatively unspecialized hemopoietic cell acquires specialized features of a gamma-delta T cell. A gamma-delta T cell is a T cell that expresses a gamma-delta T cell receptor complex. [CL:0000798, GOC:jl] |
| defense response to bacterium | biological process | Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. [GOC:jl] |
| positive regulation of cysteine-type endopeptidase activity involved in apoptotic process | biological process | Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process. [GOC:jl, GOC:mtg_apoptosis] |
| mast cell degranulation | biological process | The regulated exocytosis of secretory granules containing preformed mediators such as histamine, serotonin, and neutral proteases by a mast cell. [ISBN:0781735149] |
| positive regulation of mast cell degranulation | biological process | Any process that activates or increases the frequency, rate or extent of mast cell degranulation. [ISBN:0781735149] |
| regulation of neutrophil degranulation | biological process | Any process that modulates the frequency, rate, or extent of neutrophil degranulation. [ISBN:0781735149] |
| beta selection | biological process | The process in which successful recombination of a T cell receptor beta chain into a translatable protein coding sequence leads to rescue from apoptosis and subsequent proliferation of an immature T cell. [ISBN:0781735149, PMID:12220932] |
| 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] |
| innate immune response | biological process | Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. [GO_REF:0000022, GOC:add, GOC:ebc, GOC:mtg_sensu] |
| positive regulation of B cell differentiation | biological process | Any process that activates or increases the frequency, rate or extent of B cell differentiation. [GOC:go_curators] |
| positive regulation of gamma-delta T cell differentiation | biological process | Any process that activates or increases the frequency, rate or extent of gamma-delta T cell differentiation. [GOC:go_curators] |
| positive regulation of bone resorption | biological process | Any process that activates or increases the frequency, rate or extent of bone resorption. [GOC:go_curators] |
| positive regulation of alpha-beta T cell differentiation | biological process | Any process that activates or increases the frequency, rate or extent of alpha-beta T cell differentiation. [GOC:ai] |
| positive regulation of alpha-beta T cell proliferation | biological process | Any process that activates or increases the frequency, rate or extent of alpha-beta T cell proliferation. [GOC:ai] |
| blood vessel morphogenesis | biological process | The process in which the anatomical structures of blood vessels are generated and organized. The blood vessel is the vasculature carrying blood. [GOC:jid] |
| positive regulation of peptidyl-tyrosine phosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine. [GOC:ai] |
| regulation of phagocytosis | biological process | Any process that modulates the frequency, rate or extent of phagocytosis, the process in which phagocytes engulf external particulate material. [GOC:ai] |
| positive regulation of calcium-mediated signaling | biological process | Any process that activates or increases the frequency, rate or extent of calcium-mediated signaling. [GOC:ai] |
| B cell receptor signaling pathway | biological process | The series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell. [GOC:add] |
| positive regulation of killing of cells of another organism | biological process | Any process that activates or increases the frequency, rate or extent of the killing by an organism of cells in another organism. [GOC:ai] |
| regulation of ERK1 and ERK2 cascade | biological process | Any process that modulates the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986] |
| cellular response to molecule of fungal origin | 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 by molecules of fungal origin such as chito-octamer oligosaccharide. [GOC:mah] |
| cellular response to lipid | 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 lipid stimulus. [GOC:mah] |
| cellular response to low-density lipoprotein particle 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 low-density lipoprotein particle stimulus. [GOC:mah] |
| positive regulation of monocyte chemotactic protein-1 production | biological process | Any process that activates or increases the frequency, rate, or extent of production of monocyte chemotactic protein-1. [GOC:mah] |
| regulation of arachidonic acid secretion | biological process | Any process that modulates the rate, frequency, or extent of arachidonic acid secretion, the controlled release of arachidonic acid from a cell or a tissue. [GOC:dph, GOC:tb] |
| regulation of platelet aggregation | biological process | Any process that modulates the rate, frequency or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules. [GOC:dph, GOC:tb] |
| 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 TORC1 signaling | biological process | Any process that activates or increases the frequency, rate or extent of TORC1 signaling. [GO_REF:0000058, GOC:TermGenie, PMID:25366275] |
| cellular response to lectin | 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 lectin stimulus. A lectin is a carbohydrate-binding protein, highly specific for binding sugar moieties. [PMID:25996210, PMID:26306444] |
| cell surface receptor protein tyrosine kinase signaling pathway | biological process | The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:ceb, GOC:signaling] |
| 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] |