메뉴 건너뛰기




Volumn 7, Issue 1, 2015, Pages 23-33

TAK1 selective inhibition: State of the art and future opportunities

Author keywords

covalent inhibitor; DFG out; inflammation; kinase; MAPK; NF B; TAK1

Indexed keywords

ENZYME INHIBITOR; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; DFG PEPTIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MAP KINASE KINASE KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; OLIGOPEPTIDE; PROTEIN BINDING; PROTEIN KINASE INHIBITOR;

EID: 84921417645     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.14.138     Document Type: Review
Times cited : (31)

References (57)
  • 1
    • 0029940355 scopus 로고    scopus 로고
    • Tab1: An activator of the tak1 mapkkk in tgf-ß signal transduction
    • Shibuya H, Yamaguchi K, Shirakabe K. et al. TAB1: an activator of the TAK1 MAPKKK in TGF-ß signal transduction. Science 272(5265), 1179-1182 (1996
    • (1996) Science , vol.272 , Issue.5265 , pp. 1179-1182
    • Shibuya, H.1    Yamaguchi, K.2    Shirakabe, K.3
  • 2
    • 84885433426 scopus 로고    scopus 로고
    • Mechanism and consequence of the autoactivation of p38a mitogenactivated protein kinase promoted by tab1
    • De Nicola GF, Martin ED, Chaikuad A. et al. Mechanism and consequence of the autoactivation of p38a mitogenactivated protein kinase promoted by TAB1. Nat. Struct. Mol. Biol. 20(10), 1182-1190 (2013
    • (2013) Nat. Struct. Mol. Biol , vol.20 , Issue.10 , pp. 1182-1190
    • De Nicola, G.F.1    Martin, E.D.2    Chaikuad, A.3
  • 3
    • 0033634977 scopus 로고    scopus 로고
    • Tab2, a novel adaptor protein, mediates activation of tak1 mapkkk by linking tak1 to traf6 in the il-1 signal transduction pathway
    • Takaesu G, Kishida S, Hiyama A. et al. TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol. Cell 5(4), 649-658 (2000
    • (2000) Mol. Cell , vol.5 , Issue.4 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3
  • 4
    • 77449125293 scopus 로고    scopus 로고
    • Transforming growth factor ß-activated kinase 1 (tak1) kinase adaptor, tak1-binding protein 2, plays dual roles in tak1 signaling by recruiting both an activator and an inhibitor of tak1 kinase in tumor necrosis factor signaling pathway
    • Broglie P, Matsumoto K, Akira S, Brautigan DL, Ninomiya- Tsuji J. Transforming growth factor ß-activated kinase 1 (TAK1) kinase adaptor, TAK1-binding protein 2, plays dual roles in TAK1 signaling by recruiting both an activator and an inhibitor of TAK1 kinase in tumor necrosis factor signaling pathway. J. Biol. Chem. 285(4), 2333-2339 (2010
    • (2010) J. Biol. Chem , vol.285 , Issue.4 , pp. 2333-2339
    • Broglie, P.1    Matsumoto, K.2    Akira, S.3    Brautigan, D.L.4    Ninomiya-Tsuji, J.5
  • 6
    • 27744577296 scopus 로고    scopus 로고
    • Tak1, but not tab1 or tab2, plays an essential role in multiple signaling pathways in vivo
    • Shim J-H, Xiao C, Paschal AE. et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev. 19(22), 2668-2681 (2005
    • (2005) Genes Dev , vol.19 , Issue.22 , pp. 2668-2681
    • Shim, J.-H.1    Xiao, C.2    Paschal, A.E.3
  • 7
    • 84856301921 scopus 로고    scopus 로고
    • Tak1 negatively regulates nf-?b and p38 map kinase activation in gr-1+cd11b+ neutrophils
    • Ajibade AA, Wang Q, Cui J. et al. TAK1 negatively regulates NF-?B and p38 MAP kinase activation in Gr-1+CD11b+ neutrophils. Immunity 36(1), 43-54 (2012
    • (2012) Immunity , vol.36 , Issue.1 , pp. 43-54
    • Ajibade, A.A.1    Wang, Q.2    Cui, J.3
  • 8
    • 27544434183 scopus 로고    scopus 로고
    • Essential function for the kinase tak1 in innate and adaptive immune responses
    • Sato S, Sanjo H, Takeda K. et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat. Immunol. 6, 1087-1095 (2005
    • (2005) Nat. Immunol , vol.6 , pp. 1087-1095
    • Sato, S.1    Sanjo, H.2    Takeda, K.3
  • 9
    • 84894024528 scopus 로고    scopus 로고
    • Tak1 kinase switches cell fate from apoptosis to necrosis following tnf stimulation
    • Morioka S, Broglie P, Omori E. et al. TAK1 kinase switches cell fate from apoptosis to necrosis following TNF stimulation. J. Cell Biol. 204(4), 607-623 (2014
    • (2014) J. Cell Biol , vol.204 , Issue.4 , pp. 607-623
    • Morioka, S.1    Broglie, P.2    Omori, E.3
  • 10
    • 80053927315 scopus 로고    scopus 로고
    • The prevalence of tnfa-induced necrosis over apoptosis is determined by tak1-rip1 interplay
    • Arslan SÇ, Scheidereit C. The prevalence of TNFa-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay. PLoS ONE 6(10), e26069 (2011
    • (2011) Plos One , vol.6 , Issue.10 , pp. e26069
    • Arslan S.Ç.1    Scheidereit, C.2
  • 11
    • 84883770753 scopus 로고    scopus 로고
    • Ripk3 contributes to tnfr1-mediated ripk1 kinase-dependent apoptosis in conditions of ciap1/2 depletion or tak1 kinase inhibition
    • Dondelinger Y, Aguileta MA, Goossens V. et al. RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition. Cell Death Differ. 20(10), 1381-1392 (2013
    • (2013) Cell Death Differ , vol.20 , Issue.10 , pp. 1381-1392
    • Dondelinger, Y.1    Aguileta, M.A.2    Goossens, V.3
  • 12
    • 78149342873 scopus 로고    scopus 로고
    • In vivo rnaimediated silencing of tak1 decreases inflammatory th1 and th17 cells through targeting of myeloid cells
    • Courties G, Seiffart V, Presumey J. et al. In vivo RNAimediated silencing of TAK1 decreases inflammatory Th1 and Th17 cells through targeting of myeloid cells. Blood 116(18), 3505-3516 (2010
    • (2010) Blood , vol.116 , Issue.18 , pp. 3505-3516
    • Courties, G.1    Seiffart, V.2    Presumey, J.3
  • 13
    • 84863119109 scopus 로고    scopus 로고
    • Transforming growth factor beta-activated kinase 1 (tak1)-dependent checkpoint in the survival of dendritic cells promotes immune homeostasis and function
    • Wang Y, Huang G, Vogel P, Neale G, Reizis B, Chi H. Transforming growth factor beta-activated kinase 1 (TAK1)-dependent checkpoint in the survival of dendritic cells promotes immune homeostasis and function. Proc. Natl Acad. Sci. USA 109(6), e343-e352 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.6 , pp. e343-e352
    • Wang, Y.1    Huang, G.2    Vogel, P.3    Neale, G.4    Reizis, B.5    Chi, H.6
  • 14
    • 2342629277 scopus 로고    scopus 로고
    • The traf6 ubiquitin ligase and tak1 kinase mediate ikk activation by bcl10 and malt1 in t lymphocytes
    • Sun L, Deng L, Ea C-K, Xia Z-P, Chen ZJ. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14(3), 289-301 (2004
    • (2004) Mol. Cell , vol.14 , Issue.3 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.-K.3    Xia, Z.-P.4    Chen, Z.J.5
  • 15
    • 33748999526 scopus 로고    scopus 로고
    • Tak1 is indispensable for development of t cells and prevention of colitis by the generation of regulatory t cells
    • Sato S, Sanjo H, Tsujimura T. et al. TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells. Int. Immunol. 18(10), 1405-1411 (2006
    • (2006) Int. Immunol , vol.18 , Issue.10 , pp. 1405-1411
    • Sato, S.1    Sanjo, H.2    Tsujimura, T.3
  • 16
    • 66549125216 scopus 로고    scopus 로고
    • A critical role of tak1 in b-cell receptor-mediated nuclear factor kb activation
    • Schuman J, Chen Y, Podd A. et al. A critical role of TAK1 in B-cell receptor-mediated nuclear factor kB activation. Blood 113(19), 4566-4574 (2009
    • (2009) Blood , vol.113 , Issue.19 , pp. 4566-4574
    • Schuman, J.1    Chen, Y.2    Podd, A.3
  • 17
    • 84900406601 scopus 로고    scopus 로고
    • Positive feedback within a kinase signaling complex functions as a switch mechanism for nf-kb activation
    • Shinohara H, Behar M, Inoue K. et al. Positive feedback within a kinase signaling complex functions as a switch mechanism for NF-kB activation. Science 344(6185), 760-764 (2014
    • (2014) Science , vol.344 , Issue.6185 , pp. 760-764
    • Shinohara, H.1    Behar, M.2    Inoue, K.3
  • 18
    • 0242473165 scopus 로고    scopus 로고
    • Feedback control of the protein kinase tak1 by sapk2a/p38a
    • Cheung PCF, Campbell DG, Nebreda AR, Cohen P. Feedback control of the protein kinase TAK1 by SAPK2a/p38a. EMBO J. 22(21), 5793-5805 (2003
    • (2003) Embo J. , vol.22 , Issue.21 , pp. 5793-5805
    • Cheung, P.C.F.1    Campbell, D.G.2    Nebreda, A.R.3    Cohen, P.4
  • 19
    • 84874680253 scopus 로고    scopus 로고
    • In vivo knockdown of TAK1 accelerates bone marrow proliferation/differentiation and induces systemic inflammation
    • Vink PM, Smout WM, Driessen-Engels LJ. et al. In vivo knockdown of TAK1 accelerates bone marrow proliferation/differentiation and induces systemic inflammation. PLoS ONE 8(3), e57348 (2013
    • (2013) Plos One , vol.8 , Issue.3 , pp. e57348
    • Vink, P.M.1    Smout, W.M.2    Driessen-Engels, L.J.3
  • 20
    • 0037903145 scopus 로고    scopus 로고
    • A resorcylic acid lactone, 5z-7-oxozeaenol, prevents inflammation by inhibiting the catalytic activity of tak1 mapk kinase kinase
    • Ninomiya-Tsuji J, Kajino T, Ono K. et al. A resorcylic acid lactone, 5Z-7-oxozeaenol, prevents inflammation by inhibiting the catalytic activity of TAK1 MAPK kinase kinase. J. Biol. Chem. 278, 18485-18490 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 18485-18490
    • Ninomiya-Tsuji, J.1    Kajino, T.2    Ono, K.3
  • 21
    • 33646363800 scopus 로고    scopus 로고
    • Tak1-mediated stress signaling pathways are essential for tnf-a-promoted pulmonary metastasis of murine colon cancer cells
    • Choo M-K, Sakurai H, Koizumi K, Saiki I. TAK1-mediated stress signaling pathways are essential for TNF-a-promoted pulmonary metastasis of murine colon cancer cells. Int. J. Cancer 118(11), 2758-2764 (2006
    • (2006) Int. J. Cancer , vol.118 , Issue.11 , pp. 2758-2764
    • Choo, M.-K.1    Sakurai, H.2    Koizumi, K.3    Saiki, I.4
  • 22
    • 79961223562 scopus 로고    scopus 로고
    • Modulation of pancreatic cancer chemoresistance by inhibition of tak1
    • Melisi D, Xia Q, Paradiso G. et al. Modulation of pancreatic cancer chemoresistance by inhibition of TAK1. J. Natl Cancer Inst. 103(15), 1190-1204 (2011
    • (2011) J. Natl Cancer Inst , vol.103 , Issue.15 , pp. 1190-1204
    • Melisi, D.1    Xia, Q.2    Paradiso, G.3
  • 23
    • 84885427100 scopus 로고    scopus 로고
    • Tak1 inhibitor 5z-7-oxozeaenol sensitizes neuroblastoma to chemotherapy
    • Fan Y, Cheng J, Vasudevan S. et al. TAK1 inhibitor 5Z-7-oxozeaenol sensitizes neuroblastoma to chemotherapy. Apoptosis 18(10), 1224-1234 (2013
    • (2013) Apoptosis , vol.18 , Issue.10 , pp. 1224-1234
    • Fan, Y.1    Cheng, J.2    Vasudevan, S.3
  • 24
    • 84863419728 scopus 로고    scopus 로고
    • Tak1 inhibition promotes apoptosis in kras-dependent colon cancers
    • Singh A, Sweeney MF, Yu M. et al. TAK1 inhibition promotes apoptosis in KRAS-dependent colon cancers. Cell 148, 639-650 (2012
    • (2012) Cell , vol.148 , pp. 639-650
    • Singh, A.1    Sweeney, M.F.2    Yu, M.3
  • 25
    • 84895459238 scopus 로고    scopus 로고
    • Activation of tak1 by myd88 l265p drives malignant b-cell growth in non- hodgkin lymphoma
    • Ansell SM, Hodge LS, Secreto FJ et al. Activation of TAK1 by MYD88 L265P drives malignant B-cell growth in non- Hodgkin lymphoma. Blood Cancer J. 4, e183 (2014
    • (2014) Blood Cancer J. , vol.4 , pp. e183
    • Ansell, S.M.1    Hodge, L.S.2    Secreto, F.J.3
  • 26
    • 84874301754 scopus 로고    scopus 로고
    • Developing irreversible inhibitors of the protein kinase cysteinome
    • Liu Q, Sabnis Y, Zhao Z. et al. Developing irreversible inhibitors of the protein kinase cysteinome. Chem. Biol. 20, 146-159 (2013
    • (2013) Chem. Biol , vol.20 , pp. 146-159
    • Liu, Q.1    Sabnis, Y.2    Zhao, Z.3
  • 27
    • 33845481603 scopus 로고    scopus 로고
    • Chemistry and biology of resorcylic acid lactones
    • Winssinger N, Barluenga S. Chemistry and biology of resorcylic acid lactones. Chem. Commun. 22-36 (2007
    • (2007) Chem. Commun , pp. 22-36
    • Winssinger, N.1    Barluenga, S.2
  • 28
    • 33645233076 scopus 로고    scopus 로고
    • Targeted covalent inactivation of protein kinases by resorcylic acid lactone polyketides
    • Schirmer A, Kennedy J, Murli S, Reid R, Santi DV. Targeted covalent inactivation of protein kinases by resorcylic acid lactone polyketides. Proc. Natl Acad. Sci. USA 103, 4234-4239 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4234-4239
    • Schirmer, A.1    Kennedy, J.2    Murli, S.3    Reid, R.4    Santi, D.V.5
  • 29
    • 84885740180 scopus 로고    scopus 로고
    • Tak1 inhibition in the dfg-out conformation
    • Kilty I, Green MP, Bell AS. et al. TAK1 inhibition in the DFG-out conformation. Chem. Biol. Drug Des. 82, 500-505 (2013
    • (2013) Chem. Biol. Drug des , vol.82 , pp. 500-505
    • Kilty, I.1    Green, M.P.2    Bell, A.S.3
  • 30
    • 70350509085 scopus 로고    scopus 로고
    • Synthesis of a resorcylic acid lactone (ral) library using fluorous-mixture synthesis and profile of its selectivity against a panel of kinases
    • Jogireddy R, Dakas P-Y, Valot G, Barluenga S, Winssinger N. Synthesis of a resorcylic acid lactone (RAL) library using fluorous-mixture synthesis and profile of its selectivity against a panel of kinases. Chem. Eur. J. 15, 11498-11506 (2009
    • (2009) Chem. Eur. J. , vol.15 , pp. 11498-11506
    • Jogireddy, R.1    Dakas, P.-Y.2    Valot, G.3    Barluenga, S.4    Winssinger, N.5
  • 31
    • 84875208605 scopus 로고    scopus 로고
    • Mechanism and in vitro pharmacology of tak1 inhibition by (5z)-7-oxozeaenol
    • Wu J, Powell F, Larsen NA. et al. Mechanism and in vitro pharmacology of TAK1 inhibition by (5Z)-7-oxozeaenol. ACS Chem. Biol. 8, 643-650 (2013
    • (2013) ACS Chem. Biol , vol.8 , pp. 643-650
    • Wu, J.1    Powell, F.2    Larsen, N.A.3
  • 32
    • 67649962669 scopus 로고    scopus 로고
    • Rapid assessment of a novel series of selective cb 2) agonists using parallel synthesis protocols: A lipophilic efficiency (lipe) analysis
    • Ryckmans T, Edwards MP, Horne VA. et al. Rapid assessment of a novel series of selective CB(2) agonists using parallel synthesis protocols: a lipophilic efficiency (LipE) analysis. Bioorg. Med. Chem. Lett. 19, 4406-4409 (2009
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 4406-4409
    • Ryckmans, T.1    Edwards, M.P.2    Horne, V.A.3
  • 33
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • Leeson PD, Springthorpe B. The influence of drug-like concepts on decision-making in medicinal chemistry. Nat. Rev. Drug Disc. 6, 881-890 (2007
    • (2007) Nat. Rev. Drug Disc , vol.6 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 34
    • 84880096320 scopus 로고    scopus 로고
    • Hypothemycin a fungal natural product identifies therapeutic targets in trypanosoma brucei
    • Nishino M, Choy JW, Gushwa NN. et al. Hypothemycin, a fungal natural product, identifies therapeutic targets in Trypanosoma brucei. eLife 2, e00712 (2013
    • (2013) Elife , vol.2 , pp. e00712
    • Nishino, M.1    Choy, J.W.2    Gushwa, N.N.3
  • 35
    • 79957812702 scopus 로고    scopus 로고
    • Resorcylic acid lactones with cytotoxic and nf-?b inhibitory activities and their structure-activity relationships
    • Ayers S, Graf TN, Adcock AF. et al. Resorcylic acid lactones with cytotoxic and NF-?B inhibitory activities and their structure-activity relationships. J. Nat. Prod. 74, 1126-1131 (2011
    • (2011) J. Nat. Prod , vol.74 , pp. 1126-1131
    • Ayers, S.1    Graf, T.N.2    Adcock, A.F.3
  • 37
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • Barglow KT, Cravatt BF. Activity-based protein profiling for the functional annotation of enzymes. Nat. Methods 4, 822-827 (2007
    • (2007) Nat. Methods , vol.4 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 38
    • 84863500157 scopus 로고    scopus 로고
    • Fully functionalized small-molecule probes for integrated phenotypic screening and target identification
    • Cisar JS, Cravatt BF. Fully functionalized small-molecule probes for integrated phenotypic screening and target identification. J. Am. Chem. Soc. 134, 10385-10388 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 10385-10388
    • Cisar, J.S.1    Cravatt, B.F.2
  • 39
    • 84856402803 scopus 로고    scopus 로고
    • How chemoproteomics can enable drug discovery and development
    • Moellering RE, Cravatt BF. How chemoproteomics can enable drug discovery and development. Chem. Biol. 19, 11-22 (2012
    • (2012) Chem. Biol , vol.19 , pp. 11-22
    • Moellering, R.E.1    Cravatt, B.F.2
  • 40
    • 77955591791 scopus 로고    scopus 로고
    • In vivo efficacy of natural product-inspired irreversible kinase inhibitors
    • Barluenga S, Jogireddy R, Koripelly GK, Winssinger N. In vivo efficacy of natural product-inspired irreversible kinase inhibitors. Chembiochem 11, 1692-1699 (2010
    • (2010) Chembiochem , vol.11 , pp. 1692-1699
    • Barluenga, S.1    Jogireddy, R.2    Koripelly, G.K.3    Winssinger, N.4
  • 41
    • 84863281519 scopus 로고    scopus 로고
    • Cis-enone resorcylic acid lactones (rals) as irreversible protein kinase inhibitors
    • Wei L, Wu J, Li G, Shi N. Cis-enone resorcylic acid lactones (RALs) as irreversible protein kinase inhibitors. Curr. Pharm. Des. 18, 1186-1198 (2012
    • (2012) Curr. Pharm. des , vol.18 , pp. 1186-1198
    • Wei, L.1    Wu, J.2    Li, G.3    Shi, N.4
  • 42
    • 43149089385 scopus 로고    scopus 로고
    • Epoxyquinol b shows antiangiogenic and antitumor effects by inhibiting vegfr2, egfr, fgfr, and pdgfr
    • Kamiyama H, Kakeya H, Usui T. et al. Epoxyquinol B shows antiangiogenic and antitumor effects by inhibiting VEGFR2, EGFR, FGFR, and PDGFR. Oncol. Res. 17, 11-21 (2008
    • (2008) Oncol. Res , vol.17 , pp. 11-21
    • Kamiyama, H.1    Kakeya, H.2    Usui, T.3
  • 43
    • 47949093350 scopus 로고    scopus 로고
    • Epoxyquinol b, a naturally occurring pentaketide dimer, inhibits nf-kb signaling by cross linking tak1
    • Kamiyama H, Usui T, Sakurai H. et al. Epoxyquinol B, a naturally occurring pentaketide dimer, inhibits NF-kB signaling by cross linking TAK1. Biosci. Biotechnol. Biochem. 72, 1894-1900 (2008
    • (2008) Biosci. Biotechnol. Biochem , vol.72 , pp. 1894-1900
    • Kamiyama, H.1    Usui, T.2    Sakurai, H.3
  • 44
    • 79251612884 scopus 로고    scopus 로고
    • A comprehensive overview on genomically directed assembly of aromatic polyketides and macrolide lactones using fungal megasynthases
    • Saruwatari T, Praseuth AP, Sato M, Torikai K, Noguchi H, Watanabe K. A comprehensive overview on genomically directed assembly of aromatic polyketides and macrolide lactones using fungal megasynthases. J. Antibiot. 64, 9-17 (2011
    • (2011) J. Antibiot , vol.64 , pp. 9-17
    • Saruwatari, T.1    Praseuth, A.P.2    Sato, M.3    Torikai, K.4    Noguchi, H.5    Watanabe, K.6
  • 47
    • 84864034080 scopus 로고    scopus 로고
    • Essential role of tak1 in regulating mantle cell lymphoma survival
    • Buglio D, Palakurthi S, Byth K et al. Essential role of TAK1 in regulating mantle cell lymphoma survival. Blood 120, 347-355 (2012
    • (2012) Blood , vol.120 , pp. 347-355
    • Buglio, D.1    Palakurthi, S.2    Byth, K.3
  • 48
    • 84880590144 scopus 로고    scopus 로고
    • Discovery and optimization of 7-aminofuro[2,3-c]pyridine inhibitors of tak1
    • Hornberger KR, Berger DM, Crew AP. et al. Discovery and optimization of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1. Bioorg. Med. Chem. Lett. 23, 4517-4522 (2013
    • (2013) Bioorg. Med. Chem. Lett , vol.23 , pp. 4517-4522
    • Hornberger, K.R.1    Berger, D.M.2    Crew, A.P.3
  • 49
    • 84880633668 scopus 로고    scopus 로고
    • Discovery of 7-aminofuro[2,3-c]pyridine inhibitors of tak1: Optimization of kinase selectivity and pharmacokinetics
    • Hornberger KR, Chen X, Crew AP. et al. Discovery of 7-aminofuro[2,3-c]pyridine inhibitors of TAK1: optimization of kinase selectivity and pharmacokinetics. Bioorg. Med. Chem. Lett. 23, 4511-4516 (2013
    • (2013) Bioorg. Med. Chem. Lett , vol.23 , pp. 4511-4516
    • Hornberger, K.R.1    Chen, X.2    Crew, A.P.3
  • 50
    • 79952202090 scopus 로고    scopus 로고
    • The design, annotation, and application of a kinase-targeted library
    • Xi H, Lunney EA. The design, annotation, and application of a kinase-targeted library. Methods Mol. Biol. 685, 279-291 (2011
    • (2011) Methods Mol. Biol , vol.685 , pp. 279-291
    • Xi, H.1    Lunney, E.A.2
  • 51
    • 81555218671 scopus 로고    scopus 로고
    • Design and synthesis of inhaled p38 inhibitors for the treatment of chronic obstructive pulmonary disease
    • Millan DS, Bunnage ME, Burrows JL. et al. Design and synthesis of inhaled p38 inhibitors for the treatment of chronic obstructive pulmonary disease. J. Med. Chem. 54, 7797-7814 (2011
    • (2011) J. Med. Chem , vol.54 , pp. 7797-7814
    • Millan, D.S.1    Bunnage, M.E.2    Burrows, J.L.3
  • 52
    • 84867233413 scopus 로고    scopus 로고
    • Identification of type-II inhibitors using kinase structures
    • Lovering F, McDonald J, Whitlock GA. et al. Identification of type-II inhibitors using kinase structures. Chem. Biol. Drug Des. 80, 657-664 (2012
    • (2012) Chem. Biol. Drug des , vol.80 , pp. 657-664
    • Lovering, F.1    McDonald, J.2    Whitlock, G.A.3
  • 54
    • 84861728909 scopus 로고    scopus 로고
    • Essential role for ikkß in production of type 1 interferons by plasmacytoid dendritic cells
    • Pauls E, Shpiro N, Peggie M. et al. Essential role for IKKß in production of type 1 interferons by plasmacytoid dendritic cells. J. Biol. Chem. 287, 19216-19228 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 19216-19228
    • Pauls, E.1    Shpiro, N.2    Peggie, M.3
  • 55
    • 84862497413 scopus 로고    scopus 로고
    • The ikappab kinase family phosphorylates the parkinson's disease kinase lrrk2 at ser935 and ser910 during toll-like receptor signaling
    • Dzamko N, Inesta-Vaquera F, Zhang J. et al. The IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during Toll-like receptor signaling. PLoS ONE 7, e39132 (2012
    • (2012) Plos One , vol.7 , pp. e39132
    • Dzamko, N.1    Inesta-Vaquera, F.2    Zhang, J.3
  • 56
    • 84893770102 scopus 로고    scopus 로고
    • Synthetic phosphorylation of p38a recapitulates protein kinase activity
    • Chooi KP, Galan SRG, Raj R. et al. Synthetic phosphorylation of p38a recapitulates protein kinase activity. J. Am. Chem. Soc. 136, 1698-1701 (2014
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 1698-1701
    • Chooi, K.P.1    Galan, S.R.G.2    Raj, R.3
  • 57
    • 84900864845 scopus 로고    scopus 로고
    • Insights into the biosynthesis of 12-membered resorcylic acid lactones from heterolygous production in saccharomyces cerevisiae
    • Xu Y, Zhou T, Espinosa-Artiles P, Tang Y, Zhan J, Molnár I. Insights into the biosynthesis of 12-membered resorcylic acid lactones from heterolygous production in saccharomyces cerevisiae. ACS Chem. Biol. 9, 1119-1127 (2014
    • (2014) ACS Chem. Biol , vol.9 , pp. 1119-1127
    • Xu, Y.1    Zhou, T.2    Espinosa-Artiles, P.3    Tang, Y.4    Zhan, J.5    Molnár, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.