Janus kinase 3 | Janus kinase (JakA) family | IUPHAR Guide to IMMUNOPHARMACOLOGY

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Janus kinase 3

Target id: 2049

Nomenclature: Janus kinase 3

Abbreviated Name: JAK3

Family: Janus kinase (JakA) family

Annotation status:  image of an orange circle Annotated and awaiting review. Please contact us if you can help with reviewing.  » Email us

   GtoImmuPdb view: ON :     Janus kinase 3 has curated data in GtoImmuPdb

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 1124 19p13-p12 JAK3 Janus kinase 3
Mouse - 1100 8 B3.3 Jak3 Janus kinase 3
Rat - 1100 16 p14 Jak3 Janus kinase 3
Previous and Unofficial Names
JAKL | leukocyte Janus kinase | LJAK
Database Links
DrugBank Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
RefSeq Nucleotide
RefSeq Protein
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  JAK3 kinase domain in complex with 2-Cyclopropyl-5H-pyrrolo[2,3-b]pyrazine-7-carboxylic acid ((S)-1,2,2-trimethyl-propyl)-amide
Resolution:  1.85Å
Species:  Human
References:  32
Enzyme Reaction
EC Number:

Download all structure-activity data for this target as a CSV file

Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
AC0010 Hs Inhibition 10.1 pIC50 42
pIC50 10.1 (IC50 9x10-11 M) [42]
Description: In a biochemical assay.
PF-06651600 Hs Inhibition 9.5 pIC50
pIC50 9.5 (IC50 3x10-10 M)
Description: At 4 μM ATP (Km).
AT-9283 Hs Inhibition 9.0 pIC50 21
pIC50 9.0 (IC50 1.1x10-9 M) [21]
JAK inhibitor I Hs Inhibition 8.3 pIC50 35
pIC50 8.3 (IC50 5x10-9 M) [35]
delgocitinib Hs Inhibition 8.3 pIC50 34
pIC50 8.3 (IC50 5.5x10-9 M) [34]
Description: In an assay using the kinase domain of the recombinant human enzyme, a biotinylated peptide substrate, and [33P]ATP.
compound 2 [PMID: 15546730] Hs Inhibition 8.2 pIC50 11
pIC50 8.2 (IC50 6x10-9 M) [11]
cerdulatinib Hs Inhibition 8.1 pIC50 13
pIC50 8.1 (IC50 8x10-9 M) [13]
decernotinib Hs Inhibition 7.1 – 8.9 pIC50 12
pIC50 8.9 (IC50 1.2x10-9 M) [12]
pIC50 7.1 (IC50 7.44x10-8 M) [12]
tofacitinib Hs Inhibition 6.7 – 9.0 pIC50 9,12,16,28
pIC50 8.2 (IC50 6x10-9 M) [28]
pIC50 6.7 – 9.0 (IC50 2.1x10-7 – 1x10-9 M) [9,16]
pIC50 7.3 (IC50 5.5x10-8 M) [12]
Description: In a biochemical enzyme assay.
compound 1d [PMID: 21493067] Hs Inhibition 7.8 pIC50 38
pIC50 7.8 (IC50 1.5x10-8 M) [38]
PRN694 Hs Inhibition 7.5 pIC50 43
pIC50 7.5 (IC50 3x10-8 M) [43]
ibrutinib Hs Inhibition 7.5 pIC50 7
pIC50 7.5 (IC50 3.2x10-8 M) [7]
ilginatinib Hs Inhibition 7.4 pIC50 27
pIC50 7.4 (IC50 3.9x10-8 M) [27]
ruxolitinib Hs Inhibition 6.3 – 8.5 pIC50 12,20
pIC50 8.5 (IC50 3.22x10-9 M) [20]
pIC50 6.3 (IC50 4.87x10-7 M) [12]
gandotinib Hs Inhibition 7.3 pIC50 25
pIC50 7.3 (IC50 4.8x10-8 M) [25]
poseltinib Hs Inhibition >7.3 pIC50 8
pIC50 >7.3 (IC50 <5x10-8 M) [8]
Description: Biochemical assay result. Binned IC50 value provided in patent.
PF-06263276 Hs Inhibition 7.2 pIC50 23
pIC50 7.2 (IC50 5.99x10-8 M) [23]
BMS-911543 Hs Inhibition 7.1 pIC50 31
pIC50 7.1 (IC50 7.3x10-8 M) [31]
JAK3 inhibitor IV Hs Inhibition 7.1 pIC50 6
pIC50 7.1 (IC50 7.9x10-8 M) [6]
oclacitinib Hs Inhibition 7.0 pIC50 4
pIC50 7.0 (IC50 9.51x10-8 M) [4]
TAK-659 Hs Inhibition 6.9 pIC50 24
pIC50 6.9 (IC50 1.15x10-7 M) [24]
CEP-33779 Hs Inhibition 6.8 pIC50 15
pIC50 6.8 (IC50 1.5x10-7 M) [15]
momelotinib Hs Inhibition 6.8 pIC50 29
pIC50 6.8 (IC50 1.55x10-7 M) [29]
XL019 Hs Inhibition 6.7 pIC50 17
pIC50 6.7 (IC50 2.142x10-7 M) [17]
compound 19a [PMID: 24359159] Hs Inhibition 6.7 pIC50 33
pIC50 6.7 (IC50 2.2x10-7 M) [33]
filgotinib Hs Inhibition 6.5 pIC50 36
pIC50 6.5 (IC50 8.1x10-7 M) [36]
solcitinib Hs Inhibition 6.4 pIC50 5
pIC50 6.4 (IC50 4.08x10-7 M) [5]
pacritinib Hs Inhibition 6.3 pIC50 39
pIC50 6.3 (IC50 5.2x10-7 M) [39]
baricitinib Hs Inhibition 6.1 pIC50 12
pIC50 6.1 (IC50 7.87x10-7 M) [12]
fedratinib Hs Inhibition 6.0 pIC50 26
pIC50 6.0 (IC50 1x10-6 M) [26]
acalabrutinib Hs Inhibition <6.0 pIC50 7
pIC50 <6.0 (IC50 >1x10-6 M) [7]
SAR-20347 Hs Inhibition 5.8 pIC50 41
pIC50 5.8 (IC50 1.437x10-6 M) [41]
Description: In a TR-FRET assay.
JAK3 inhibitor II Hs Inhibition 5.7 pIC50 10
pIC50 5.7 (IC50 1.8x10-6 M) [10]
upadacitinib Hs Inhibition 5.6 pIC50 37
pIC50 5.6 (IC50 2.3x10-6 M) [37]
AZD1480 Hs Inhibition 5.4 pIC50 19
pIC50 5.4 (IC50 3.63x10-6 M) [19]
peficitinib Hs Inhibition >- pIC50 22
pIC50 [22]
Inhibitor Comments
The IC50 for filgotinib vs. JAK3 is >10 μM [12].
DiscoveRx KINOMEscan® screen
A screen of 72 inhibitors against 456 human kinases. Quantitative data were derived using DiscoveRx KINOMEscan® platform.
Reference: 14,40

Key to terms and symbols Click column headers to sort
Target used in screen: JAK3(JH1domain-catalytic)
Ligand Sp. Type Action Affinity Units
tofacitinib Hs Inhibitor Inhibition 9.8 pKd
ruxolitinib Hs Inhibitor Inhibition 8.7 pKd
lestaurtinib Hs Inhibitor Inhibition 8.6 pKd
midostaurin Hs Inhibitor Inhibition 7.9 pKd
staurosporine Hs Inhibitor Inhibition 7.9 pKd
NVP-TAE684 Hs Inhibitor Inhibition 7.8 pKd
JNJ-28312141 Hs Inhibitor Inhibition 7.7 pKd
tamatinib Hs Inhibitor Inhibition 7.4 pKd
KW-2449 Hs Inhibitor Inhibition 7.4 pKd
fedratinib Hs Inhibitor Inhibition 7.1 pKd
Displaying the top 10 most potent ligands  View all ligands in screen »
EMD Millipore KinaseProfilerTM screen/Reaction Biology Kinase HotspotSM screen
A screen profiling 158 kinase inhibitors (Calbiochem Protein Kinase Inhibitor Library I and II, catalogue numbers 539744 and 539745) for their inhibitory activity at 1µM and 10µM against 234 human recombinant kinases using the EMD Millipore KinaseProfilerTM service.

A screen profiling the inhibitory activity of 178 commercially available kinase inhibitors at 0.5µM against a panel of 300 recombinant protein kinases using the Reaction Biology Corporation Kinase HotspotSM platform.


Reference: 2,18

Key to terms and symbols Click column headers to sort
Target used in screen: JAK3/JAK3
Ligand Sp. Type Action % Activity remaining at 0.5µM % Activity remaining at 1µM % Activity remaining at 10µM
EGFR/ErbB-2/ErbB-4 inhibitor Hs Inhibitor Inhibition -0.2 51.0 59.0
JAK inhibitor I Hs Inhibitor Inhibition 0.4 1.0 1.0
K-252a Hs Inhibitor Inhibition 0.5 0.0 0.0
staurosporine Hs Inhibitor Inhibition 0.7 0.0 0.5
midostaurin Hs Inhibitor Inhibition 0.8 1.0 1.0
SB 218078 Hs Inhibitor Inhibition 1.9 8.0 9.0
tofacitinib Hs Inhibitor Inhibition 1.9
Gö 6976 Hs Inhibitor Inhibition 2.4 1.0 2.0
JAK3 inhibitor VI Hs Inhibitor Inhibition 4.8 6.0 1.0
Cdk1/2 inhibitor III Hs Inhibitor Inhibition 5.2 0.0 2.0
Displaying the top 10 most potent ligands  View all ligands in screen »
Clinically-Relevant Mutations and Pathophysiology
Disease:  Combined immunodeficiency
Description: Combined immunodeficiency evolving into predominant CD4+ lymphopenia
Disease:  Severe combined immunodeficiency, autosomal recessive, T cell-negative, B cell-positive, NK cell-negative
Synonyms: T-B+ severe combined immunodeficiency due to JAK3 deficiency [Orphanet: ORPHA35078]
Disease Ontology: DOID:0060008
OMIM: 600802
Orphanet: ORPHA35078
Biologically Significant Variants
Type:  Missense mutation
Species:  Human
Description:  This mutation causes combined immunodeficiency evolving into predominant CD4+ lymphopenia.
Amino acid change:  Cys1066Arg
Nucleotide change:  T3196C
References:  3
Type:  Naturally occurring SNP
Species:  Human
Description:  An inherited non-coding homozygous mutation creating a dominant splice site and reduced wild-type protein expression causes SCID/CID.
Nucleotide change:  c.2652C>T
References:  30


Show »

1. Alves de Medeiros AK, Speeckaert R, Desmet E, Van Gele M, De Schepper S, Lambert J. (2016) JAK3 as an Emerging Target for Topical Treatment of Inflammatory Skin Diseases. PLoS ONE, 11 (10): e0164080. [PMID:27711196]

2. Anastassiadis T, Deacon SW, Devarajan K, Ma H, Peterson JR. (2011) Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat. Biotechnol., 29 (11): 1039-45. [PMID:22037377]

3. Ban SA, Salzer E, Eibl MM, Linder A, Geier CB, Santos-Valente E, Garncarz W, Lion T, Ott R, Seelbach C et al.. (2014) Combined immunodeficiency evolving into predominant CD4+ lymphopenia caused by somatic chimerism in JAK3. J. Clin. Immunol., 34 (8): 941-53. [PMID:25205547]

4. Berlinski PJ, Birchmeier MJ, Bowman JW, Gonzales AJ, Kamerling SG, Mann DW, Mitton-Fry MJ. (2010) Pyrrolo[2,3-d]pyrimidine compounds. Patent number: WO2010020905. Assignee: Pfizer Inc.. Priority date: 20/08/2008. Publication date: 25/02/2010.

5. Blanc J. (2010) Novel compound useful for the treatment of degenerative and inflammatory diseases. Patent number: WO2010149771. Assignee: Galapagos Nv, Menet, Christel Jeanne Marie. Priority date: 26/06/2009. Publication date: 29/12/2010.

6. Brown GR, Bamford AM, Bowyer J, James DS, Rankine N, Tang E, Torr V, Culbert EJ. (2000) Naphthyl ketones: a new class of Janus kinase 3 inhibitors. Bioorg. Med. Chem. Lett., 10 (6): 575-9. [PMID:10741557]

7. Byrd JC, Harrington B, O'Brien S, Jones JA, Schuh A, Devereux S, Chaves J, Wierda WG, Awan FT, Brown JR et al.. (2016) Acalabrutinib (ACP-196) in Relapsed Chronic Lymphocytic Leukemia. N. Engl. J. Med., 374 (4): 323-32. [PMID:26641137]

8. Cha MY, Kang SJ, Kim MR, Lee JY, Jeon JY, Jo MG, Kwak EJ, Lee KO, Ha TH, Suh KH, Kim MS. (2011) Novel fused pyrimidine derivatives for inhd3ition of tyrosine kinase activity. Patent number: WO2011162515A2. Assignee: Hanmi Holdings Co. , Ltd.. Priority date: 23/06/2010. Publication date: 29/12/2011.

9. Changelian PS, Flanagan ME, Ball DJ, Kent CR, Magnuson KS, Martin WH, Rizzuti BJ, Sawyer PS, Perry BD, Brissette WH et al.. (2003) Prevention of organ allograft rejection by a specific Janus kinase 3 inhibitor. Science, 302 (5646): 875-8. [PMID:14593182]

10. Changelian PS, Moshinsky D, Kuhn CF, Flanagan ME, Munchhof MJ, Harris TM, Whipple DA, Doty JL, Sun J, Kent CR et al.. (2008) The specificity of JAK3 kinase inhibitors. Blood, 111 (4): 2155-7. [PMID:18094329]

11. Chen P, Norris D, Das J, Spergel SH, Wityak J, Leith L, Zhao R, Chen BC, Pitt S, Pang S et al.. (2004) Discovery of novel 2-(aminoheteroaryl)-thiazole-5-carboxamides as potent and orally active Src-family kinase p56(Lck) inhibitors. Bioorg. Med. Chem. Lett., 14 (24): 6061-6. [PMID:15546730]

12. Clark JD, Flanagan ME, Telliez JB. (2014) Discovery and development of Janus kinase (JAK) inhibitors for inflammatory diseases. J. Med. Chem., 57 (12): 5023-38. [PMID:24417533]

13. Coffey G, Betz A, DeGuzman F, Pak Y, Inagaki M, Baker DC, Hollenbach SJ, Pandey A, Sinha U. (2014) The novel kinase inhibitor PRT062070 (Cerdulatinib) demonstrates efficacy in models of autoimmunity and B-cell cancer. J. Pharmacol. Exp. Ther., 351 (3): 538-48. [PMID:25253883]

14. Davis MI, Hunt JP, Herrgard S, Ciceri P, Wodicka LM, Pallares G, Hocker M, Treiber DK, Zarrinkar PP. (2011) Comprehensive analysis of kinase inhibitor selectivity. Nat. Biotechnol., 29 (11): 1046-51. [PMID:22037378]

15. Dugan BJ, Gingrich DE, Mesaros EF, Milkiewicz KL, Curry MA, Zulli AL, Dobrzanski P, Serdikoff C, Jan M, Angeles TS et al.. (2012) A selective, orally bioavailable 1,2,4-triazolo[1,5-a]pyridine-based inhibitor of Janus kinase 2 for use in anticancer therapy: discovery of CEP-33779. J. Med. Chem., 55 (11): 5243-54. [PMID:22594690]

16. Flanagan ME, Blumenkopf TA, Brissette WH, Brown MF, Casavant JM, Shang-Poa C, Doty JL, Elliott EA, Fisher MB, Hines M et al.. (2010) Discovery of CP-690,550: a potent and selective Janus kinase (JAK) inhibitor for the treatment of autoimmune diseases and organ transplant rejection. J. Med. Chem., 53 (24): 8468-84. [PMID:21105711]

17. Forsyth T, Kearney PC, Kim BG, Johnson HW, Aay N, Arcalas A, Brown DS, Chan V, Chen J, Du H et al.. (2012) SAR and in vivo evaluation of 4-aryl-2-aminoalkylpyrimidines as potent and selective Janus kinase 2 (JAK2) inhibitors. Bioorg. Med. Chem. Lett., 22 (24): 7653-8. [PMID:23127890]

18. Gao Y, Davies SP, Augustin M, Woodward A, Patel UA, Kovelman R, Harvey KJ. (2013) A broad activity screen in support of a chemogenomic map for kinase signalling research and drug discovery. Biochem. J., 451 (2): 313-28. [PMID:23398362]

19. Gozgit JM, Bebernitz G, Patil P, Ye M, Parmentier J, Wu J, Su N, Wang T, Ioannidis S, Davies A et al.. (2008) Effects of the JAK2 inhibitor, AZ960, on Pim/BAD/BCL-xL survival signaling in the human JAK2 V617F cell line SET-2. J. Biol. Chem., 283 (47): 32334-43. [PMID:18775810]

20. Hanan EJ, van Abbema A, Barrett K, Blair WS, Blaney J, Chang C, Eigenbrot C, Flynn S, Gibbons P, Hurley CA et al.. (2012) Discovery of potent and selective pyrazolopyrimidine janus kinase 2 inhibitors. J. Med. Chem., 55 (22): 10090-107. [PMID:23061660]

21. Howard S, Berdini V, Boulstridge JA, Carr MG, Cross DM, Curry J, Devine LA, Early TR, Fazal L, Gill AL et al.. (2009) Fragment-based discovery of the pyrazol-4-yl urea (AT9283), a multitargeted kinase inhibitor with potent aurora kinase activity. J. Med. Chem., 52 (2): 379-88. [PMID:19143567]

22. Ito M, Yamazaki S, Yamagami K, Kuno M, Morita Y, Okuma K, Nakamura K, Chida N, Inami M, Inoue T et al.. (2017) A novel JAK inhibitor, peficitinib, demonstrates potent efficacy in a rat adjuvant-induced arthritis model. J. Pharmacol. Sci., 133 (1): 25-33. [PMID:28117214]

23. Jones P, Storer RI, Sabnis YA, Wakenhut FM, Whitlock GA, England KS, Mukaiyama T, Dehnhardt CM, Coe JW, Kortum SW et al.. (2017) 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. J. Med. Chem., 60 (2): 767-786. [PMID:27983835]

24. Lam B, Arikawa Y, Cramlett J, Dong Q, de Jong R, Feher V, Grimshaw CE, Farrell PJ, Hoffman ID, Jennings A et al.. (2016) Discovery of TAK-659 an orally available investigational inhibitor of Spleen Tyrosine Kinase (SYK). Bioorg. Med. Chem. Lett., 26 (24): 5947-5950. [PMID:27839918]

25. Ma L, Clayton JR, Walgren RA, Zhao B, Evans RJ, Smith MC, Heinz-Taheny KM, Kreklau EL, Bloem L, Pitou C et al.. (2013) Discovery and characterization of LY2784544, a small-molecule tyrosine kinase inhibitor of JAK2V617F. Blood Cancer J, 3: e109. [PMID:23584399]

26. Malerich JP, Lam JS, Hart B, Fine RM, Klebansky B, Tanga MJ, D'Andrea A. (2010) Diamino-1,2,4-triazole derivatives are selective inhibitors of TYK2 and JAK1 over JAK2 and JAK3. Bioorg. Med. Chem. Lett., 20 (24): 7454-7. [PMID:21106455]

27. Nakaya Y, Shide K, Niwa T, Homan J, Sugahara S, Horio T, Kuramoto K, Kotera T, Shibayama H, Hori K et al.. (2011) Efficacy of NS-018, a potent and selective JAK2/Src inhibitor, in primary cells and mouse models of myeloproliferative neoplasms. Blood Cancer J, 1 (7): e29. [PMID:22829185]

28. Ostrovskyi D, Rumpf T, Eib J, Lumbroso A, Slynko I, Klaeger S, Heinzlmeir S, Forster M, Gehringer M, Pfaffenrot E et al.. (2016) Tofacitinib and analogs as inhibitors of the histone kinase PRK1 (PKN1). Future Med Chem, 8 (13): 1537-51. [PMID:27572962]

29. Pardanani A, Lasho T, Smith G, Burns CJ, Fantino E, Tefferi A. (2009) CYT387, a selective JAK1/JAK2 inhibitor: in vitro assessment of kinase selectivity and preclinical studies using cell lines and primary cells from polycythemia vera patients. Leukemia, 23 (8): 1441-5. [PMID:19295546]

30. Platt CD, Massaad MJ, Cangemi B, Schmidt B, Aldhekri H, Geha RS. (2017) Janus kinase 3 deficiency caused by a homozygous synonymous exonic mutation that creates a dominant splice site. J. Allergy Clin. Immunol., 140 (1): 268-271.e6. [PMID:27956217]

31. Purandare AV, McDevitt TM, Wan H, You D, Penhallow B, Han X, Vuppugalla R, Zhang Y, Ruepp SU, Trainor GL et al.. (2012) Characterization of BMS-911543, a functionally selective small-molecule inhibitor of JAK2. Leukemia., 26 (2): 280-8. [PMID:22015772]

32. Soth M, Hermann JC, Yee C, Alam M, Barnett JW, Berry P, Browner MF, Frank K, Frauchiger S, Harris S et al.. (2013) 3-Amido pyrrolopyrazine JAK kinase inhibitors: development of a JAK3 vs JAK1 selective inhibitor and evaluation in cellular and in vivo models. J. Med. Chem., 56 (1): 345-56. [PMID:23214979]

33. Su Q, Ioannidis S, Chuaqui C, Almeida L, Alimzhanov M, Bebernitz G, Bell K, Block M, Howard T, Huang S et al.. (2014) Discovery of 1-methyl-1H-imidazole derivatives as potent Jak2 inhibitors. J. Med. Chem., 57 (1): 144-58. [PMID:24359159]

34. Tanimoto A, Ogawa Y, Oki C, Kimoto Y, Nozawa K, Amano W, Noji S, Shiozaki M, Matsuo A, Shinozaki Y et al.. (2015) Pharmacological properties of JTE-052: a novel potent JAK inhibitor that suppresses various inflammatory responses in vitro and in vivo. Inflamm. Res., 64 (1): 41-51. [PMID:25387665]

35. Thompson JE, Cubbon RM, Cummings RT, Wicker LS, Frankshun R, Cunningham BR, Cameron PM, Meinke PT, Liverton N, Weng Y et al.. (2002) Photochemical preparation of a pyridone containing tetracycle: a Jak protein kinase inhibitor. Bioorg. Med. Chem. Lett., 12 (8): 1219-23. [PMID:11934592]

36. Van Rompaey L, Galien R, van der Aar EM, Clement-Lacroix P, Nelles L, Smets B, Lepescheux L, Christophe T, Conrath K, Vandeghinste N et al.. (2013) Preclinical characterization of GLPG0634, a selective inhibitor of JAK1, for the treatment of inflammatory diseases. J. Immunol., 191 (7): 3568-77. [PMID:24006460]

37. Voss JW, Camp HS, Padley RJ. (2015) Jak1 selective inhibitor and uses thereof. Patent number: WO2015061665. Assignee: Abbvie Inc.. Priority date: 24/10/2013. Publication date: 30/04/2015.

38. Wang T, Ioannidis S, Almeida L, Block MH, Davies AM, Lamb ML, Scott DA, Su M, Zhang HJ, Alimzhanov M et al.. (2011) In vitro and in vivo evaluation of 6-aminopyrazolyl-pyridine-3-carbonitriles as JAK2 kinase inhibitors. Bioorg. Med. Chem. Lett., 21 (10): 2958-61. [PMID:21493067]

39. William AD, Lee AC, Blanchard S, Poulsen A, Teo EL, Nagaraj H, Tan E, Chen D, Williams M, Sun ET et al.. (2011) Discovery of the macrocycle 11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[,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 for the treatment of myelofibrosis and lymphoma. J. Med. Chem., 54 (13): 4638-58. [PMID:21604762]

40. Wodicka LM, Ciceri P, Davis MI, Hunt JP, Floyd M, Salerno S, Hua XH, Ford JM, Armstrong RC, Zarrinkar PP et al.. (2010) Activation state-dependent binding of small molecule kinase inhibitors: structural insights from biochemistry. Chem. Biol., 17 (11): 1241-9. [PMID:21095574]

41. Works MG, Yin F, Yin CC, Yiu Y, Shew K, Tran TT, Dunlap N, Lam J, Mitchell T, Reader J et al.. (2014) Inhibition of TYK2 and JAK1 ameliorates imiquimod-induced psoriasis-like dermatitis by inhibiting IL-22 and the IL-23/IL-17 axis. J. Immunol., 193 (7): 3278-87. [PMID:25156366]

42. Xu X, Mao L, Xu W, Tang W, Zhang X, Xi B, Xu R, Fang X, Liu J, Fang C et al.. (2016) AC0010, an Irreversible EGFR Inhibitor Selectively Targeting Mutated EGFR and Overcoming T790M-Induced Resistance in Animal Models and Lung Cancer Patients. Mol. Cancer Ther., 15 (11): 2586-2597. [PMID:27573423]

43. Zhong Y, Dong S, Strattan E, Ren L, Butchar JP, Thornton K, Mishra A, Porcu P, Bradshaw JM, Bisconte A et al.. (2015) Targeting interleukin-2-inducible T-cell kinase (ITK) and resting lymphocyte kinase (RLK) using a novel covalent inhibitor PRN694. J. Biol. Chem., 290 (10): 5960-78. [PMID:25593320]

How to cite this page

Janus kinase (JakA) family: Janus kinase 3. Last modified on 08/08/2018. Accessed on 20/01/2019. IUPHAR/BPS Guide to PHARMACOLOGY, http://guidetoimmunopharmacology.org/GRAC/ObjectDisplayForward?objectId=2049.