mitogen-activated protein kinase 14 | p38 subfamily | IUPHAR Guide to IMMUNOPHARMACOLOGY

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mitogen-activated protein kinase 14

  Target has curated data in GtoImmuPdb

Target id: 1499

Nomenclature: mitogen-activated protein kinase 14

Abbreviated Name: p38α

Family: p38 subfamily

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

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 360 6p21.3-p21.2 MAPK14 mitogen-activated protein kinase 14
Mouse - 360 17 Mapk14 mitogen-activated protein kinase 14
Rat - 360 20p12 Mapk14 mitogen activated protein kinase 14
Previous and Unofficial Names
CRK1 | Csaids binding protein | CSBP | CSBP1 | CSBP2 | CSPB1 | Cytokine suppressive anti-inflammatory drug binding protein | Exip | Hog | MAPK 14 | MAP kinase 14 | MAP kinase 2 | MAP kinase Mxi2 | MAP kinase p38 alpha | MAX-interacting protein 2 | mitogen-activated protein kinase 14A | mitogen-activated protein kinase p38 alpha | Mxi2 | p38αMAPK | p38 MAPK | p38 MAP kinase alpha | p38 mitogen activated protein kinase | PRKM14 | PRKM15 | Sapk2A | stress-activated protein kinase 2A
Database Links
ChEMBL 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:  Crystal structure of human p38alpha complexed with PH-797804
Ligand:  PH-797804
Resolution:  1.95Å
Species:  Human
References:  36
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of p38 MAPKα in complex with BMS-582949
Ligand:  BMS-582949
Resolution:  2.8Å
Species:  Human
References:  24
Image of receptor 3D structure from RCSB PDB
Description:  P38 kinase crystal structure in complex with pamapimod.
Ligand:  pamapimod
Resolution:  2.1Å
Species:  Human
References:  18
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of p38 alpha MAP kinase in complex with a novel isoform selective drug candidate
PDB Id:  4R3C
Ligand:  MW150
Resolution:  2.06Å
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 Value Parameter Reference
PF-03715455 Hs Binding 12.0 pKd 26
pKd 12.0 (Kd 1x10-12 M) [26]
doramapimod Hs Inhibition 9.4 pKd 12
pKd 9.4 (Kd 4.5x10-10 M) [12]
pamapimod Hs Inhibition 8.9 pKd 18
pKd 8.9 (Kd 1.3x10-9 M) [18]
Description: In a biochemical assay.
VX-702 Hs Inhibition 8.4 pKd 17
pKd 8.4 (Kd 3.7x10-9 M) [17]
PH-797804 Hs Inhibition 8.5 pKi
pKi 8.5 (Ki 2.9x10-9 M)
losmapimod Hs Inhibition 8.1 pKi 7
pKi 8.1 (Ki 7.94x10-9 M) [7]
SB203580 Hs Inhibition 8.0 pKi 13
pKi 8.0 (Ki 1x10-8 M) [13]
MW150 Hs Inhibition 7.0 pKi 6,32
pKi 7.0 (Ki 1.01x10-7 M) [6,32]
Description: Ki determined from a TR-FRET based (LanthaScreen®) kinase binding assay, which analysed competitive binding to the non-activated form of p38α MAPK.
compound 12 [PMID: 22521646] Hs Inhibition 9.2 pIC50 3
pIC50 9.2 (IC50 6.4x10-10 M) [3]
PF-03715455 Hs Inhibition 9.1 pIC50 26
pIC50 9.1 (IC50 8.8x10-10 M) [26]
ralimetinib Hs Inhibition 8.1 pIC50 25
pIC50 8.1 (IC50 7x10-9 M) [25]
TAK-715 Hs Inhibition 8.1 pIC50 27
pIC50 8.1 (IC50 7.1x10-9 M) [27]
talmapimod Hs Inhibition 8.1 pIC50 33
pIC50 8.1 (IC50 9x10-9 M) [33]
neflamapimod Hs Inhibition 8.0 pIC50 21
pIC50 8.0 (IC50 1x10-8 M) [21]
BMS-582949 Hs Inhibition 7.9 pIC50 24
pIC50 7.9 (IC50 1.3x10-8 M) [24]
AZD6703 Hs Inhibition 7.8 pIC50 11
pIC50 7.8 (IC50 1.558x10-8 M) [11]
SB220025 Hs Inhibition 7.7 pIC50 1
pIC50 7.7 (IC50 1.9x10-8 M) [1]
doramapimod Hs Inhibition 7.7 pIC50 28
pIC50 7.7 (IC50 2x10-8 M) [28]
SB202190 Hs Inhibition 7.5 pIC50 16
pIC50 7.5 (IC50 3x10-8 M) [16]
pexmetinib Hs Inhibition 7.5 pIC50 8
pIC50 7.5 (IC50 3.5x10-8 M) [8]
7-hydroxystaurosporine Hs Inhibition 7.0 pIC50 31
pIC50 7.0 (IC50 9.5x10-8 M) [31]
SKF-86002 Hs Inhibition 7.0 pIC50 22
pIC50 7.0 (IC50 1.1x10-7 M) [22]
Description: Measured using a classic homogeneous time-resolved fluorescence (HTRF) kinase assay
PF-670462 Hs Inhibition 6.7 pIC50 9
pIC50 6.7 (IC50 1.9x10-7 M) [9]
Description: In a biochemical kinase assay.
CBS-3595 Hs Inhibition 6.3 pIC50 4
pIC50 6.3 (IC50 5x10-7 M) [4]
Description: In vitro determination.
PP1 Hs Inhibition 6.2 pIC50 10
pIC50 6.2 (IC50 6.4x10-7 M) [10]
acumapimod Hs Inhibition >6.0 pIC50 14
pIC50 >6.0 (IC50 <1x10-6 M) [14]
dilmapimod Hs Inhibition >5.0 pIC50 2
pIC50 >5.0 (IC50 <1x10-5 M) [2]
DiscoveRx KINOMEscan® screen
A screen of 72 inhibitors against 456 human kinases. Quantitative data were derived using DiscoveRx KINOMEscan® platform.
Reference: 12,35

Key to terms and symbols Click column headers to sort
Target used in screen: p38-alpha
Ligand Sp. Type Action Value Parameter
doramapimod Hs Inhibitor Inhibition 9.4 pKd
neflamapimod Hs Inhibitor Inhibition 8.6 pKd
SB203580 Hs Inhibitor Inhibition 7.9 pKd
dasatinib Hs Inhibitor Inhibition 7.6 pKd
PD-173955 Hs Inhibitor Inhibition 7.2 pKd
AST-487 Hs Inhibitor Inhibition 7.1 pKd
foretinib Hs Inhibitor Inhibition 6.5 pKd
sorafenib Hs Inhibitor Inhibition 6.4 pKd
nilotinib Hs Inhibitor Inhibition 6.3 pKd
afatinib Hs Inhibitor Inhibition 5.9 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: 5,15

Key to terms and symbols Click column headers to sort
Target used in screen: SAPK2a/P38a(MAPK14)
Ligand Sp. Type Action % Activity remaining at 0.5µM % Activity remaining at 1µM % Activity remaining at 10µM
VX-702 Hs Inhibitor Inhibition 5.2
SB202190 Hs Inhibitor Inhibition 7.4 1.0 1.0
p38 MAP kinase inhibitor III Hs Inhibitor Inhibition 7.6 -1.0 0.0
PD 169316 Hs Inhibitor Inhibition 7.8 1.0 2.0
p38 MAP kinase inhibitor Hs Inhibitor Inhibition 11.2 3.0 0.0
SB220025 Hs Inhibitor Inhibition 13.1 2.0 1.0
SB203580 Hs Inhibitor Inhibition 22.8 5.0 2.0
nilotinib Hs Inhibitor Inhibition 23.3
dasatinib Hs Inhibitor Inhibition 36.5
sorafenib Hs Inhibitor Inhibition 40.2
Displaying the top 10 most potent ligands  View all ligands in screen »
Immunopharmacology Comments
p38 MAP kinases are ubiquitous, highly conserved enzymes which regulate the production of proinflammatory mediators (such as TNFα and IL-1) in response to inflammatory cytokines or environmental stress [19-20,23,29-30,34]. They are essential for normal immune and inflammatory responses, but are also involved in many other cellular processes such as regulating the cell cycle and cytoskeletal remodelling.

Pharmacological inhibition of p38 MAP kinases reduces inflammatory cytokine synthesis, making these enzymes validated and extensively pursued drug targets for autoimmune and inflammatory diseases, including arthritis and other joint diseases, septic shock, myocardial injury and neuroinflammation. A number of pan-p38 MAP kinase inhibitors and isoform selective inhibitors have been evaluated in clinical trials, although none have yet reached the clinic.
Immuno Process Associations
Immuno Process:  Inflammation
GO Annotations:  Associated to 3 GO processes
GO:0043312 neutrophil degranulation TAS
GO:1900015 regulation of cytokine production involved in inflammatory response IDA
click arrow to show/hide IEA associations
GO:0010759 positive regulation of macrophage chemotaxis IEA
Immuno Process:  Immune regulation
GO Annotations:  Associated to 4 GO processes
GO:0045648 positive regulation of erythrocyte differentiation IMP
GO:1900015 regulation of cytokine production involved in inflammatory response IDA
click arrow to show/hide IEA associations
GO:0002741 positive regulation of cytokine secretion involved in immune response IEA
GO:0010759 positive regulation of macrophage chemotaxis IEA
Immuno Process:  Immune system development
GO Annotations:  Associated to 2 GO processes
GO:0030316 osteoclast differentiation ISS
GO:0045648 positive regulation of erythrocyte differentiation IMP
Immuno Process:  Cytokine production & signalling
GO Annotations:  Associated to 4 GO processes
GO:1900015 regulation of cytokine production involved in inflammatory response IDA
GO:2001184 positive regulation of interleukin-12 secretion IMP
click arrow to show/hide IEA associations
GO:0002741 positive regulation of cytokine secretion involved in immune response IEA
GO:0071356 cellular response to tumor necrosis factor IEA
Immuno Process:  Cellular signalling
GO Annotations:  Associated to 1 GO processes
GO:0043312 neutrophil degranulation TAS
Immuno Process:  Chemotaxis & migration
GO Annotations:  Associated to 1 GO processes, IEA only
click arrow to show/hide IEA associations
GO:0010759 positive regulation of macrophage chemotaxis IEA
Immuno Process:  Tissue repair
GO Annotations:  Associated to 1 GO processes
GO:0014835 myoblast differentiation involved in skeletal muscle regeneration IMP


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1. Adams JL, Boehm JC, Gallagher TF, Kassis S, Webb EF, Hall R, Sorenson M, Garigipati R, Griswold DE, Lee JC. (2001) Pyrimidinylimidazole inhibitors of p38: cyclic N-1 imidazole substituents enhance p38 kinase inhibition and oral activity. Bioorg. Med. Chem. Lett., 11 (21): 2867-70. [PMID:11597418]

2. Adams JL, Boehm JC, Hall R, Jin Q, Kasparec J, Silva DJ, Taggart JJ. Novel trisubstituted-8H-pyrido[2,3-d]pyrimidin-7-one compound for the treatment of CSBP/p38 kinase mediated diseases. Patent number: EP1333833. Assignee: GlaxoSmithKline LLC. Priority date: 23/10/2000. Publication date: 23/10/2001.

3. Aiguadé J, Balagué C, Carranco I, Caturla F, Domínguez M, Eastwood P, Esteve C, González J, Lumeras W, Orellana A et al.. (2012) Novel triazolopyridylbenzamides as potent and selective p38α inhibitors. Bioorg. Med. Chem. Lett., 22 (10): 3431-6. [PMID:22521646]

4. Albrecht W, Unger A, Bauer SM, Laufer SA. (2017) Discovery of N-{4-[5-(4-Fluorophenyl)-3-methyl-2-methylsulfanyl-3H-imidazol-4-yl]-pyridin-2-yl}-acetamide (CBS-3595), a Dual p38α MAPK/PDE-4 Inhibitor with Activity against TNFα-Related Diseases. J. Med. Chem., 60 (13): 5290-5305. [PMID:28613871]

5. 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]

6. Arancio O, Watterson DM, Pelletier JC, Roy SM. (2014) Map kinase modulators and uses thereof. Patent number: WO2014145485A2. Assignee: The Trustees Of Columbia University In The City Of New York. Priority date: 15/03/2013. Publication date: 18/09/2014.

7. Aston NM, Bamborough P, Buckton JB, Edwards CD, Holmes DS, Jones KL, Patel VK, Smee PA, Somers DO, Vitulli G et al.. (2009) p38alpha mitogen-activated protein kinase inhibitors: optimization of a series of biphenylamides to give a molecule suitable for clinical progression. J. Med. Chem., 52 (20): 6257-69. [PMID:19772287]

8. Bachegowda L, Morrone K, Winski SL, Mantzaris I, Bartenstein M, Ramachandra N, Giricz O, Sukrithan V, Nwankwo G, Shahnaz S et al.. (2016) Pexmetinib: A Novel Dual Inhibitor of Tie2 and p38 MAPK with Efficacy in Preclinical Models of Myelodysplastic Syndromes and Acute Myeloid Leukemia. Cancer Res., 76 (16): 4841-4849. [PMID:27287719]

9. Badura L, Swanson T, Adamowicz W, Adams J, Cianfrogna J, Fisher K, Holland J, Kleiman R, Nelson F, Reynolds L et al.. (2007) An inhibitor of casein kinase I epsilon induces phase delays in circadian rhythms under free-running and entrained conditions. J. Pharmacol. Exp. Ther., 322 (2): 730-8. [PMID:17502429]

10. Bain J, McLauchlan H, Elliott M, Cohen P. (2003) The specificities of protein kinase inhibitors: an update. Biochem. J., 371 (Pt 1): 199-204. [PMID:12534346]

11. Brown DS, Cumming JG, Bethel P, Finlayson J, Gerhardt S, Nash I, Pauptit RA, Pike KG, Reid A, Snelson W et al.. (2012) The discovery of N-cyclopropyl-4-methyl-3-[6-(4-methylpiperazin-1-yl)-4-oxoquinazolin-3(4H)-yl]benzamide (AZD6703), a clinical p38α MAP kinase inhibitor for the treatment of inflammatory diseases. Bioorg. Med. Chem. Lett., 22 (12): 3879-83. [PMID:22608965]

12. 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]

13. Eyers PA, Craxton M, Morrice N, Cohen P, Goedert M. (1998) Conversion of SB 203580-insensitive MAP kinase family members to drug-sensitive forms by a single amino-acid substitution. Chem. Biol., 5 (6): 321-8. [PMID:9653550]

14. Fryszman OM, Lang H, Lan J, Chang E, Fang Y. (2005) 5-membered heterocycle-based p38 kinase inhibitors. Patent number: WO2005009973. Assignee: Novartis Ag. Priority date: 26/06/2003. Publication date: 03/02/2005.

15. 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]

16. Goldstein DM, Alfredson T, Bertrand J, Browner MF, Clifford K, Dalrymple SA, Dunn J, Freire-Moar J, Harris S, Labadie SS et al.. (2006) Discovery of S-[5-amino-1-(4-fluorophenyl)-1H-pyrazol-4-yl]-[3-(2,3-dihydroxypropoxy)phenyl]methanone (RO3201195), an orally bioavailable and highly selective inhibitor of p38 MAP kinase. J. Med. Chem., 49 (5): 1562-75. [PMID:16509574]

17. Goldstein DM, Kuglstatter A, Lou Y, Soth MJ. (2010) Selective p38alpha inhibitors clinically evaluated for the treatment of chronic inflammatory disorders. J. Med. Chem., 53 (6): 2345-53. [PMID:19950901]

18. Goldstein DM, Soth M, Gabriel T, Dewdney N, Kuglstatter A, Arzeno H, Chen J, Bingenheimer W, Dalrymple SA, Dunn J et al.. (2011) Discovery of 6-(2,4-difluorophenoxy)-2-[3-hydroxy-1-(2-hydroxyethyl)propylamino]-8-methyl-8H-pyrido[2,3-d]pyrimidin-7-one (pamapimod) and 6-(2,4-difluorophenoxy)-8-methyl-2-(tetrahydro-2H-pyran-4-ylamino)pyrido[2,3-d]pyrimidin-7(8H)-one (R1487) as orally bioavailable and highly selective inhibitors of p38α mitogen-activated protein kinase. J. Med. Chem., 54 (7): 2255-65. [PMID:21375264]

19. Han J, Jiang Y, Li Z, Kravchenko VV, Ulevitch RJ. (1997) Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature, 386 (6622): 296-9. [PMID:9069290]

20. Han J, Lee JD, Bibbs L, Ulevitch RJ. (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science, 265 (5173): 808-11. [PMID:7914033]

21. Karaman MW, Herrgard S, Treiber DK, Gallant P, Atteridge CE, Campbell BT, Chan KW, Ciceri P, Davis MI, Edeen PT et al.. (2008) A quantitative analysis of kinase inhibitor selectivity. Nat. Biotechnol., 26 (1): 127-32. [PMID:18183025]

22. Klüter S, Grütter C, Naqvi T, Rabiller M, Simard JR, Pawar V, Getlik M, Rauh D. (2010) Displacement assay for the detection of stabilizers of inactive kinase conformations. J. Med. Chem., 53 (1): 357-67. [PMID:19928858]

23. Lee JC, Kumar S, Griswold DE, Underwood DC, Votta BJ, Adams JL. (2000) Inhibition of p38 MAP kinase as a therapeutic strategy. Immunopharmacology, 47 (2-3): 185-201. [PMID:10878289]

24. Liu C, Lin J, Wrobleski ST, Lin S, Hynes J, Wu H, Dyckman AJ, Li T, Wityak J, Gillooly KM et al.. (2010) Discovery of 4-(5-(cyclopropylcarbamoyl)-2-methylphenylamino)-5-methyl-N-propylpyrrolo[1,2-f][1,2,4]triazine-6-carboxamide (BMS-582949), a clinical p38α MAP kinase inhibitor for the treatment of inflammatory diseases. J. Med. Chem., 53 (18): 6629-39. [PMID:20804198]

25. Mader M, de Dios A, Shih C, Bonjouklian R, Li T, White W, López de Uralde B, Sánchez-Martinez C, del Prado M, Jaramillo C et al.. (2008) Imidazolyl benzimidazoles and imidazo[4,5-b]pyridines as potent p38alpha MAP kinase inhibitors with excellent in vivo antiinflammatory properties. Bioorg. Med. Chem. Lett., 18 (1): 179-83. [PMID:18039577]

26. Millan DS, Bunnage ME, Burrows JL, Butcher KJ, Dodd PG, Evans TJ, Fairman DA, Hughes SJ, Kilty IC, Lemaitre A et al.. (2011) Design and synthesis of inhaled p38 inhibitors for the treatment of chronic obstructive pulmonary disease. J. Med. Chem., 54 (22): 7797-814. [PMID:21888439]

27. Miwatashi S, Arikawa Y, Kotani E, Miyamoto M, Naruo K, Kimura H, Tanaka T, Asahi S, Ohkawa S. (2005) Novel inhibitor of p38 MAP kinase as an anti-TNF-alpha drug: discovery of N-[4-[2-ethyl-4-(3-methylphenyl)-1,3-thiazol-5-yl]-2-pyridyl]benzamide (TAK-715) as a potent and orally active anti-rheumatoid arthritis agent. J Med Chem, 48 (19): 5966-79. [PMID:16162000]

28. Moffett K, Konteatis Z, Nguyen D, Shetty R, Ludington J, Fujimoto T, Lee KJ, Chai X, Namboodiri H, Karpusas M et al.. (2011) Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD). Bioorg. Med. Chem. Lett., 21 (23): 7155-65. [PMID:22014550]

29. Pearson G, Robinson F, Beers Gibson T, Xu BE, Karandikar M, Berman K, Cobb MH. (2001) Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr. Rev., 22 (2): 153-83. [PMID:11294822]

30. Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ. (1995) Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem., 270 (13): 7420-6. [PMID:7535770]

31. Reinhardt HC, Aslanian AS, Lees JA, Yaffe MB. (2007) p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage. Cancer Cell, 11 (2): 175-89. [PMID:17292828]

32. Roy SM, Grum-Tokars VL, Schavocky JP, Saeed F, Staniszewski A, Teich AF, Arancio O, Bachstetter AD, Webster SJ, Van Eldik LJ et al.. (2015) Targeting human central nervous system protein kinases: An isoform selective p38αMAPK inhibitor that attenuates disease progression in Alzheimer's disease mouse models. ACS Chem Neurosci, 6 (4): 666-80. [PMID:25676389]

33. Tan X, Tester RW, Luedtke GR, Chakravarty S, Mavunkel BJ, Perumattam JJ, Lu Q, Nashashibi I, Jung J, Hu J et al.. (2010) Design and synthesis of piperazine-indole p38 alpha MAP kinase inhibitors with improved pharmacokinetic profiles. Bioorg. Med. Chem. Lett., 20 (3): 828-31. [PMID:20071169]

34. Wang XZ, Ron D. (1996) Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science, 272 (5266): 1347-9. [PMID:8650547]

35. 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]

36. Xing L, Shieh HS, Selness SR, Devraj RV, Walker JK, Devadas B, Hope HR, Compton RP, Schindler JF, Hirsch JL et al.. (2009) Structural bioinformatics-based prediction of exceptional selectivity of p38 MAP kinase inhibitor PH-797804. Biochemistry, 48 (27): 6402-11. [PMID:19496616]

How to cite this page

p38 subfamily: mitogen-activated protein kinase 14. Last modified on 30/10/2019. Accessed on 04/08/2020. IUPHAR/BPS Guide to PHARMACOLOGY,