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Volumn 10, Issue 1, 2013, Pages

Homology modeling and ligand docking of Mitogen-activated protein kinase-activated protein kinase 5 (MK5)

Author keywords

Docking; Homology modeling; ICM program package; MAPKAPK5; Molecular dynamics; PRAK

Indexed keywords

VERTEBRATA;

EID: 84883682129     PISSN: None     EISSN: 17424682     Source Type: Journal    
DOI: 10.1186/1742-4682-10-56     Document Type: Article
Times cited : (14)

References (63)
  • 1
    • 79952435349 scopus 로고    scopus 로고
    • Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
    • 10.1128/MMBR.00031-10 21372320
    • Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. Cargnello M, Roux PP, Microbiol Mol Biol Rev 2011 75 1 50 83 10.1128/MMBR.00031-10 21372320
    • (2011) Microbiol Mol Biol Rev , vol.75 , Issue.1 , pp. 50-83
    • Cargnello, M.1    Roux, P.P.2
  • 2
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases - MKs - two's company, three's a crowd
    • 10.1038/nrm1834 16421520
    • MAPKAP kinases-MKs-two's company, three's a crowd. Gaestel M, Nat Rev Mol Cell Biol 2006 7 2 120 30 10.1038/nrm1834 16421520
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.2 , pp. 120-130
    • Gaestel, M.1
  • 3
    • 83755166163 scopus 로고    scopus 로고
    • Physiological roles of mitogen-activated-protein-kinase-activated p38-regulated/activated protein kinase
    • 10.4331/wjbc.v2.i5.73 21666810
    • Physiological roles of mitogen-activated-protein-kinase-activated p38-regulated/activated protein kinase. Kostenko S, et al. World J Biol Chem 2011 2 5 73 89 10.4331/wjbc.v2.i5.73 21666810
    • (2011) World J Biol Chem , vol.2 , Issue.5 , pp. 73-89
    • Kostenko, S.1
  • 4
    • 0032512546 scopus 로고    scopus 로고
    • MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase
    • 10.1006/bbrc.1998.8135 9480836
    • MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. Ni H, et al. Biochem Biophys Res Commun 1998 243 2 492 6 10.1006/bbrc.1998.8135 9480836
    • (1998) Biochem Biophys Res Commun , vol.243 , Issue.2 , pp. 492-496
    • Ni, H.1
  • 5
    • 0032526694 scopus 로고    scopus 로고
    • PRAK, a novel protein kinase regulated by the p38 MAP kinase
    • 10.1093/emboj/17.12.3372 9628874
    • PRAK, a novel protein kinase regulated by the p38 MAP kinase. New L, et al. EMBO J 1998 17 12 3372 84 10.1093/emboj/17.12.3372 9628874
    • (1998) EMBO J , vol.17 , Issue.12 , pp. 3372-3384
    • New, L.1
  • 6
    • 42549091024 scopus 로고    scopus 로고
    • Does MK5 reconcile classical and atypical MAP kinases?
    • 18508533
    • Does MK5 reconcile classical and atypical MAP kinases? Perander M, Keyse SM, Seternes OM, Front Biosci 2008 13 4617 24 18508533
    • (2008) Front Biosci , vol.13 , pp. 4617-4624
    • Perander, M.1    Keyse, S.M.2    Seternes, O.M.3
  • 7
    • 70349895664 scopus 로고    scopus 로고
    • The transcriptional regulation and cell-specific expression of the MAPK-activated protein kinase MK5
    • 10.2478/s11658-009-0020-6 19484198
    • The transcriptional regulation and cell-specific expression of the MAPK-activated protein kinase MK5. Gerits N, et al. Cell Mol Biol Lett 2009 14 4 548 74 10.2478/s11658-009-0020-6 19484198
    • (2009) Cell Mol Biol Lett , vol.14 , Issue.4 , pp. 548-574
    • Gerits, N.1
  • 8
    • 0036789457 scopus 로고    scopus 로고
    • Both binding and activation of p38 mitogen-activated protein kinase (MAPK) play essential roles in regulation of the nucleocytoplasmic distribution of MAPK-activated protein kinase 5 by cellular stress
    • 10.1128/MCB.22.20.6931-6945.2002 12242275
    • Both binding and activation of p38 mitogen-activated protein kinase (MAPK) play essential roles in regulation of the nucleocytoplasmic distribution of MAPK-activated protein kinase 5 by cellular stress. Seternes OM, et al. Mol Cell Biol 2002 22 20 6931 45 10.1128/MCB.22.20.6931-6945.2002 12242275
    • (2002) Mol Cell Biol , vol.22 , Issue.20 , pp. 6931-6945
    • Seternes, O.M.1
  • 9
    • 0037971054 scopus 로고    scopus 로고
    • Regulation of PRAK subcellular location by p38 MAP kinases
    • 10.1091/mbc.E02-08-0538 12808055
    • Regulation of PRAK subcellular location by p38 MAP kinases. New L, Jiang Y, Han J, Mol Biol Cell 2003 14 6 2603 16 10.1091/mbc.E02-08-0538 12808055
    • (2003) Mol Biol Cell , vol.14 , Issue.6 , pp. 2603-2616
    • New, L.1    Jiang, Y.2    Han, J.3
  • 10
    • 11244276988 scopus 로고    scopus 로고
    • Scaffolding by ERK3 regulates MK5 in development
    • 10.1038/sj.emboj.7600467 15538386
    • Scaffolding by ERK3 regulates MK5 in development. Schumacher S, et al. EMBO J 2004 23 24 4770 9 10.1038/sj.emboj.7600467 15538386
    • (2004) EMBO J , vol.23 , Issue.24 , pp. 4770-4779
    • Schumacher, S.1
  • 11
    • 33845966056 scopus 로고    scopus 로고
    • Characterization of the atypical MAPK ERK4 and its activation of the MAPK-activated protein kinase MK5
    • 10.1074/jbc.M606693200 16973613
    • Characterization of the atypical MAPK ERK4 and its activation of the MAPK-activated protein kinase MK5. Kant S, et al. J Biol Chem 2006 281 46 35511 9 10.1074/jbc.M606693200 16973613
    • (2006) J Biol Chem , vol.281 , Issue.46 , pp. 35511-35519
    • Kant, S.1
  • 12
    • 37549041719 scopus 로고    scopus 로고
    • Modulation of F-actin rearrangement by the cyclic AMP/cAMP-dependent protein kinase (PKA) pathway is mediated by MAPK-activated protein kinase 5 and requires PKA-induced nuclear export of MK5
    • 10.1074/jbc.M704873200 17947239
    • Modulation of F-actin rearrangement by the cyclic AMP/cAMP-dependent protein kinase (PKA) pathway is mediated by MAPK-activated protein kinase 5 and requires PKA-induced nuclear export of MK5. Gerits N, et al. J Biol Chem 2007 282 51 37232 43 10.1074/jbc.M704873200 17947239
    • (2007) J Biol Chem , vol.282 , Issue.51 , pp. 37232-37243
    • Gerits, N.1
  • 13
    • 54049134823 scopus 로고    scopus 로고
    • Activation loop phosphorylation of the atypical MAP kinases ERK3 and ERK4 is required for binding, activation and cytoplasmic relocalization of MK5
    • 10.1002/jcp.21560 18720373
    • Activation loop phosphorylation of the atypical MAP kinases ERK3 and ERK4 is required for binding, activation and cytoplasmic relocalization of MK5. Deleris P, et al. J Cell Physiol 2008 217 3 778 88 10.1002/jcp.21560 18720373
    • (2008) J Cell Physiol , vol.217 , Issue.3 , pp. 778-788
    • Deleris, P.1
  • 14
    • 40549097761 scopus 로고    scopus 로고
    • A functional link between the human cell cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase Erk3
    • 10.4161/cc.7.3.5354 18235225
    • A functional link between the human cell cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase Erk3. Hansen CA, Bartek J, Jensen S, Cell Cycle 2008 7 3 325 34 10.4161/cc.7.3.5354 18235225
    • (2008) Cell Cycle , vol.7 , Issue.3 , pp. 325-334
    • Hansen, C.A.1    Bartek, J.2    Jensen, S.3
  • 15
    • 77955490044 scopus 로고    scopus 로고
    • Mechanisms regulating the nuclear translocation of p38 MAP kinase
    • 10.1002/jcb.22675 20506250
    • Mechanisms regulating the nuclear translocation of p38 MAP kinase. Gong X, et al. J Cell Biochem 2010 110 6 1420 9 10.1002/jcb.22675 20506250
    • (2010) J Cell Biochem , vol.110 , Issue.6 , pp. 1420-1429
    • Gong, X.1
  • 16
    • 79951579535 scopus 로고    scopus 로고
    • Serine residue 115 of MAPK-activated protein kinase MK5 is crucial for its PKA-regulated nuclear export and biological function
    • 10.1007/s00018-010-0496-2 20734105
    • Serine residue 115 of MAPK-activated protein kinase MK5 is crucial for its PKA-regulated nuclear export and biological function. Kostenko S, et al. Cell Mol Life Sci 2011 68 5 847 62 10.1007/s00018-010-0496-2 20734105
    • (2011) Cell Mol Life Sci , vol.68 , Issue.5 , pp. 847-862
    • Kostenko, S.1
  • 17
    • 77953021835 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: Menage a trois or menage a quatre?
    • 10.1016/j.cellsig.2010.03.002 20227494
    • Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: menage a trois or menage a quatre? Shiryaev A, Moens U, Cell Signal 2010 22 8 1185 92 10.1016/j.cellsig.2010.03.002 20227494
    • (2010) Cell Signal , vol.22 , Issue.8 , pp. 1185-1192
    • Shiryaev, A.1    Moens, U.2
  • 18
    • 34548411669 scopus 로고    scopus 로고
    • 14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin polymerization
    • 10.1016/j.cellsig.2007.07.016 17728103
    • 14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin polymerization. Tak H, et al. Cell Signal 2007 19 11 2379 87 10.1016/j.cellsig.2007.07.016 17728103
    • (2007) Cell Signal , vol.19 , Issue.11 , pp. 2379-2387
    • Tak, H.1
  • 19
    • 60549113678 scopus 로고    scopus 로고
    • PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5
    • 10.1016/j.cellsig.2009.01.009 19166925
    • PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5. Kostenko S, Johannessen M, Moens U, Cell Signal 2009 21 5 712 8 10.1016/j.cellsig.2009.01.009 19166925
    • (2009) Cell Signal , vol.21 , Issue.5 , pp. 712-718
    • Kostenko, S.1    Johannessen, M.2    Moens, U.3
  • 20
    • 84864386249 scopus 로고    scopus 로고
    • Absence of a human DnaJ protein hTid-1S correlates with aberrant actin cytoskeleton organization in lesional psoriatic skin
    • 10.1074/jbc.M111.313809 22692211
    • Absence of a human DnaJ protein hTid-1S correlates with aberrant actin cytoskeleton organization in lesional psoriatic skin. Choi JH, et al. The Journal of biological chemistry 2012 287 31 25954 63 10.1074/jbc.M111.313809 22692211
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.31 , pp. 25954-25963
    • Choi, J.H.1
  • 21
    • 0034671847 scopus 로고    scopus 로고
    • The p38 pathway provides negative feedback for Ras proliferative signaling
    • 10.1074/jbc.M002856200 10978313
    • The p38 pathway provides negative feedback for Ras proliferative signaling. Chen G, et al. J Biol Chem 2000 275 50 38973 80 10.1074/jbc. M002856200 10978313
    • (2000) J Biol Chem , vol.275 , Issue.50 , pp. 38973-38980
    • Chen, G.1
  • 22
    • 44849109379 scopus 로고    scopus 로고
    • Determinants that control the distinct subcellular localization of p38alpha-PRAK and p38beta-PRAK complexes
    • 10.1074/jbc.M709682200 18268017
    • Determinants that control the distinct subcellular localization of p38alpha-PRAK and p38beta-PRAK complexes. Li Q, et al. J Biol Chem 2008 283 16 11014 23 10.1074/jbc.M709682200 18268017
    • (2008) J Biol Chem , vol.283 , Issue.16 , pp. 11014-11023
    • Li, Q.1
  • 23
    • 33846282393 scopus 로고    scopus 로고
    • PRAK is essential for ras-induced senescence and tumor suppression
    • 10.1016/j.cell.2006.11.050 17254968
    • PRAK is essential for ras-induced senescence and tumor suppression. Sun P, et al. Cell 2007 128 2 295 308 10.1016/j.cell.2006.11.050 17254968
    • (2007) Cell , vol.128 , Issue.2 , pp. 295-308
    • Sun, P.1
  • 24
    • 79951472912 scopus 로고    scopus 로고
    • The MK5/PRAK kinase and Myc form a negative feedback loop that is disrupted during colorectal tumorigenesis
    • 10.1016/j.molcel.2011.01.023 21329882
    • The MK5/PRAK kinase and Myc form a negative feedback loop that is disrupted during colorectal tumorigenesis. Kress TR, et al. Mol Cell 2011 41 4 445 57 10.1016/j.molcel.2011.01.023 21329882
    • (2011) Mol Cell , vol.41 , Issue.4 , pp. 445-457
    • Kress, T.R.1
  • 25
    • 0038721214 scopus 로고    scopus 로고
    • Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation
    • 10.1128/MCB.23.13.4542-4558.2003 12808096
    • Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation. Coulombe P, et al. Mol Cell Biol 2003 23 13 4542 58 10.1128/MCB.23.13.4542-4558.2003 12808096
    • (2003) Mol Cell Biol , vol.23 , Issue.13 , pp. 4542-4558
    • Coulombe, P.1
  • 26
    • 0142242155 scopus 로고    scopus 로고
    • Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression
    • 10.1074/jbc.M302724200 12915405
    • Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression. Julien C, Coulombe P, Meloche S, J Biol Chem 2003 278 43 42615 24 10.1074/jbc.M302724200 12915405
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 42615-42624
    • Julien, C.1    Coulombe, P.2    Meloche, S.3
  • 27
    • 84856255165 scopus 로고    scopus 로고
    • IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling
    • 10.1101/gad.177642.111 22279049
    • IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling. Stohr N, et al. Genes Dev 2012 26 2 176 89 10.1101/gad.177642.111 22279049
    • (2012) Genes Dev , vol.26 , Issue.2 , pp. 176-189
    • Stohr, N.1
  • 28
    • 84862570702 scopus 로고    scopus 로고
    • PRAK suppresses oncogenic ras-induced hematopoietic cancer development by antagonizing the JNK pathway
    • 10.1158/1541-7786.MCR-11-0576 22665523
    • PRAK suppresses oncogenic ras-induced hematopoietic cancer development by antagonizing the JNK pathway. Yoshizuka N, et al. Mol Cancer Res 2012 10 6 810 20 10.1158/1541-7786.MCR-11-0576 22665523
    • (2012) Mol Cancer Res , vol.10 , Issue.6 , pp. 810-820
    • Yoshizuka, N.1
  • 29
    • 84863024247 scopus 로고    scopus 로고
    • A novel function of p38-regulated/activated kinase in endothelial cell migration and tumor angiogenesis
    • 10.1128/MCB.06301-11 22124154
    • A novel function of p38-regulated/activated kinase in endothelial cell migration and tumor angiogenesis. Yoshizuka N, et al. Mol Cell Biol 2012 32 3 606 18 10.1128/MCB.06301-11 22124154
    • (2012) Mol Cell Biol , vol.32 , Issue.3 , pp. 606-618
    • Yoshizuka, N.1
  • 30
    • 79952281400 scopus 로고    scopus 로고
    • Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1
    • 10.1038/ncb2168 21336308
    • Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1. Zheng M, et al. Nat Cell Biol 2011 13 3 263 72 10.1038/ncb2168 21336308
    • (2011) Nat Cell Biol , vol.13 , Issue.3 , pp. 263-272
    • Zheng, M.1
  • 31
    • 39049110141 scopus 로고    scopus 로고
    • Transgenic mice expressing constitutive active MAPKAPK5 display gender-dependent differences in exploration and activity
    • 10.1186/1744-9081-3-58 17997833
    • Transgenic mice expressing constitutive active MAPKAPK5 display gender-dependent differences in exploration and activity. Gerits N, Van Belle W, Moens U, Behav Brain Funct 2007 3 58 10.1186/1744-9081-3-58 17997833
    • (2007) Behav Brain Funct , vol.3 , pp. 58
    • Gerits, N.1    Van Belle, W.2    Moens, U.3
  • 32
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • 10.1006/jmbi.2000.4042 10964570
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment. Notredame C, Higgins DG, Heringa J, J Mol Biol 2000 302 1 205 17 10.1006/jmbi.2000.4042 10964570
    • (2000) J Mol Biol , vol.302 , Issue.1 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 33
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • 10.1093/nar/gkg522 12824354
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments. Poirot O, O'Toole E, Notredame C, Nucleic Acids Res 2003 31 13 3503 6 10.1093/nar/gkg522 12824354
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 34
    • 9144232912 scopus 로고    scopus 로고
    • UniProt: The Universal Protein knowledgebase
    • 10.1093/nar/gng157
    • UniProt: the Universal Protein knowledgebase. Apweiler R, et al. Nucleic Acids Res 2004 32 9 115 10.1093/nar/gng157
    • (2004) Nucleic Acids Res , vol.32 , pp. 9-115
    • Apweiler, R.1
  • 35
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • 10.1093/nar/28.1.235 10592235
    • The Protein Data Bank. Berman HM, et al. Nucleic Acids Res 2000 28 1 235 42 10.1093/nar/28.1.235 10592235
    • (2000) Nucleic Acids Res , vol.28 , Issue.1 , pp. 235-242
    • Berman, H.M.1
  • 36
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • 2231712
    • Basic local alignment search tool. Altschul SF, et al. J Mol Biol 1990 215 3 403 10 2231712
    • (1990) J Mol Biol , vol.215 , Issue.3 , pp. 403-410
    • Altschul, S.F.1
  • 37
    • 78651346193 scopus 로고    scopus 로고
    • The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5 (MK5/PRAK) inhibitor
    • 10.1007/s00018-010-0452-1 20640477
    • The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5 (MK5/PRAK) inhibitor. Kostenko S, et al. Cellular and molecular life sciences: CMLS 2011 68 2 289 301 10.1007/s00018-010-0452-1 20640477
    • (2011) Cellular and Molecular Life Sciences: CMLS , vol.68 , Issue.2 , pp. 289-301
    • Kostenko, S.1
  • 38
    • 84986522918 scopus 로고
    • ICM-A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • 10.1002/jcc.540150503
    • ICM-A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation. Abagyan R, Totrov M, et al. Journal of Computational Chemistry 1994 15 5 488 506 10.1002/jcc.540150503
    • (1994) Journal of Computational Chemistry , vol.15 , Issue.5 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2
  • 39
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • 10.1006/jmbi.1994.1052 8289329
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. Abagyan R, Totrov M, J Mol Biol 1994 235 3 983 1002 10.1006/jmbi.1994.1052 8289329
    • (1994) J Mol Biol , vol.235 , Issue.3 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 40
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 10.1107/S0021889892009944
    • PROCHECK: a program to check the stereochemical quality of protein structures. Laskowski RA, et al. Journal of Applied Crystallography 1993 26 2 283 291 10.1107/S0021889892009944
    • (1993) Journal of Applied Crystallography , vol.26 , Issue.2 , pp. 283-291
    • Laskowski, R.A.1
  • 41
    • 0344186399 scopus 로고    scopus 로고
    • Errors in protein structures
    • 8692262
    • Errors in protein structures. Hooft RW, et al. Nature 1996 381 6580 272 8692262
    • (1996) Nature , vol.381 , Issue.6580 , pp. 272
    • Hooft, R.W.1
  • 42
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • 10.1002/pro.5560020916 8401235
    • Verification of protein structures: patterns of nonbonded atomic interactions. Colovos C, Yeates TO, Protein Sci 1993 2 9 1511 9 10.1002/pro.5560020916 8401235
    • (1993) Protein Sci , vol.2 , Issue.9 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 43
    • 0025398721 scopus 로고
    • A molecular modeling and drug design program
    • 29 10.1016/0263-7855(90)80070-V 2268628
    • a molecular modeling and drug design program. Vriend G, WHAT IF, J Mol Graph 1990 8 1 52 6 29 10.1016/0263-7855(90)80070-V 2268628
    • (1990) J Mol Graph , vol.8 , Issue.1 , pp. 52-56
    • Vriend, G.1    What, I.F.2
  • 44
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • 10.1093/bioinformatics/16.6.566 10980157
    • DaliLite workbench for protein structure comparison. Holm L, Park J, Bioinformatics 2000 16 6 566 7 10.1093/bioinformatics/16.6.566 10980157
    • (2000) Bioinformatics , vol.16 , Issue.6 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 45
    • 21044444449 scopus 로고    scopus 로고
    • Pocketome via comprehensive identification and classification of ligand binding envelopes
    • 10.1074/mcp.M400159-MCP200 15757999
    • Pocketome via comprehensive identification and classification of ligand binding envelopes. An J, Totrov M, Abagyan R, Mol Cell Proteomics 2005 4 6 752 61 10.1074/mcp.M400159-MCP200 15757999
    • (2005) Mol Cell Proteomics , vol.4 , Issue.6 , pp. 752-761
    • An, J.1    Totrov, M.2    Abagyan, R.3
  • 46
    • 0034294901 scopus 로고    scopus 로고
    • Better decisions through science
    • 10.1038/scientificamerican1000-82 11011389
    • Better decisions through science. Swets JA, Dawes RM, Monahan J, Sci Am 2000 283 4 82 7 10.1038/scientificamerican1000-82 11011389
    • (2000) Sci Am , vol.283 , Issue.4 , pp. 82-87
    • Swets, J.A.1    Dawes, R.M.2    Monahan, J.3
  • 47
    • 33646023117 scopus 로고    scopus 로고
    • An introduction to ROC analysis
    • 10.1016/j.patrec.2005.10.010
    • An introduction to ROC analysis. Fawcett T, Pattern Recognition Letters 2006 27 8 861 874 10.1016/j.patrec.2005.10.010
    • (2006) Pattern Recognition Letters , vol.27 , Issue.8 , pp. 861-874
    • Fawcett, T.1
  • 49
    • 0029956468 scopus 로고    scopus 로고
    • Development of interpretive criteria and quality control limits for macrolide and clindamycin susceptibility testing of Streptococcus pneumoniae
    • 8897164
    • Development of interpretive criteria and quality control limits for macrolide and clindamycin susceptibility testing of Streptococcus pneumoniae. Jorgensen JH, et al. Journal of clinical microbiology 1996 34 11 2679 84 8897164
    • (1996) Journal of Clinical Microbiology , vol.34 , Issue.11 , pp. 2679-2684
    • Jorgensen, J.H.1
  • 50
    • 36449000062 scopus 로고
    • Nosé-Hoover chains: The canonical ensemble via continuous dynamics
    • Nosé-Hoover chains: The canonical ensemble via continuous dynamics. Martyna GJK ML, Tuckerman M, Journal of Chemical Physics 1992 97 4 9
    • (1992) Journal of Chemical Physics , vol.97 , Issue.4 , pp. 9
    • Martyna Gjk, M.L.1    Tuckerman, M.2
  • 51
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Constant pressure molecular dynamics algorithms. Martyna GJDJTKML, Journal of Chemical Physics 1994 101 5 13
    • (1994) Journal of Chemical Physics , vol.101 , Issue.5 , pp. 13
    • Martyna, G.1
  • 53
    • 0000504254 scopus 로고
    • A Multiple-Time-Step Molecular Dynamics Algorithm for Macromolecules
    • 10.1021/j100078a035
    • A Multiple-Time-Step Molecular Dynamics Algorithm for Macromolecules. Humphreys DDFRA, Berne BJ, Journal of Physical Chemistry 1994 98 27 6885 6892 10.1021/j100078a035
    • (1994) Journal of Physical Chemistry , vol.98 , Issue.27 , pp. 6885-6892
    • Humphreys, D.1    Berne, B.J.2
  • 54
    • 34447295963 scopus 로고    scopus 로고
    • Molecular basis of MAPK-activated protein kinase 2: P38 assembly
    • 10.1073/pnas.0701679104 17395714
    • Molecular basis of MAPK-activated protein kinase 2:p38 assembly. White A, et al. Proc Natl Acad Sci U S A 2007 104 15 6353 8 10.1073/pnas.0701679104 17395714
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.15 , pp. 6353-6358
    • White, A.1
  • 55
    • 77955421113 scopus 로고    scopus 로고
    • In vivo and in vitro SAR of tetracyclic MAPKAP-K2 (MK2) inhibitors
    • 10.1016/j.bmcl.2010.04.023
    • In vivo and in vitro SAR of tetracyclic MAPKAP-K2 (MK2) inhibitors. Revesz L, et al. Part II. Bioorg Med Chem Lett 2010 20 15 4719 23 10.1016/j.bmcl.2010.04.023
    • (2010) Part II. Bioorg Med Chem Lett , vol.20 , Issue.15 , pp. 4719-4723
    • Revesz, L.1
  • 56
    • 75149153517 scopus 로고    scopus 로고
    • High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand
    • 19937655
    • High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand. Cheng R, et al. Protein Sci 2010 19 1 168 73 19937655
    • (2010) Protein Sci , vol.19 , Issue.1 , pp. 168-173
    • Cheng, R.1
  • 57
    • 34248176277 scopus 로고    scopus 로고
    • Structural basis for a high affinity inhibitor bound to protein kinase MK2
    • 10.1016/j.jmb.2007.03.004 17449059
    • Structural basis for a high affinity inhibitor bound to protein kinase MK2. Hillig RC, et al. J Mol Biol 2007 369 3 735 45 10.1016/j.jmb.2007.03.004 17449059
    • (2007) J Mol Biol , vol.369 , Issue.3 , pp. 735-745
    • Hillig, R.C.1
  • 58
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • 10.1016/S0092-8674(02)00741-9 12015977
    • The conformational plasticity of protein kinases. Huse M, Kuriyan J, Cell 2002 109 3 275 82 10.1016/S0092-8674(02)00741-9 12015977
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 59
    • 73349093728 scopus 로고    scopus 로고
    • High-performance drug discovery: Computational screening by combining docking and molecular dynamics simulations
    • 10.1371/journal.pcbi.1000528 19816553
    • High-performance drug discovery: computational screening by combining docking and molecular dynamics simulations. Okimoto N, et al. PLoS computational biology 2009 5 10 1000528 10.1371/journal.pcbi.1000528 19816553
    • (2009) PLoS Computational Biology , vol.5 , Issue.10 , pp. 51000528
    • Okimoto, N.1
  • 60
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • 10.1038/nchembio799 16783341
    • Rational design of inhibitors that bind to inactive kinase conformations. Liu Y, Gray NS, Nat Chem Biol 2006 2 7 358 64 10.1038/nchembio799 16783341
    • (2006) Nat Chem Biol , vol.2 , Issue.7 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 61
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • 19104514
    • Targeting cancer with small molecule kinase inhibitors. Zhang J, Yang PL, Gray NS, Nature reviews. Cancer 2009 9 1 28 39 19104514
    • (2009) Nature Reviews. Cancer , vol.9 , Issue.1 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 62
    • 84874301754 scopus 로고    scopus 로고
    • Developing irreversible inhibitors of the protein kinase cysteinome
    • 10.1016/j.chembiol.2012.12.006 24052895
    • Developing irreversible inhibitors of the protein kinase cysteinome. Liu Q, et al. Chemistry & biology 2013 20 2 146 59 10.1016/j.chembiol.2012.12. 006 24052895
    • (2013) Chemistry & Biology , vol.20 , Issue.2 , pp. 146-159
    • Liu, Q.1
  • 63
    • 84865166160 scopus 로고    scopus 로고
    • Tumour promoting and suppressing roles of the atypical MAP kinase signalling pathway ERK3/4-MK5
    • 10.1186/1750-2187-7-9 22800433
    • Tumour promoting and suppressing roles of the atypical MAP kinase signalling pathway ERK3/4-MK5. Kostenko S, Dumitriu G, Moens U, J Mol Signal 2012 7 1 9 10.1186/1750-2187-7-9 22800433
    • (2012) J Mol Signal , vol.7 , Issue.1 , pp. 9
    • Kostenko, S.1    Dumitriu, G.2    Moens, U.3


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