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Volumn 4, Issue , 2014, Pages

Structural dynamic analysis of apo and ATP-bound IRAK4 kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; APOENZYME; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE; IRAK4 PROTEIN, HUMAN; MAGNESIUM; PROTEIN BINDING;

EID: 84904626297     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep05748     Document Type: Article
Times cited : (35)

References (83)
  • 1
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S.,akeda, K. Toll-like receptor signalling. Nat. Rev. Immunol. 4, 499-511 (2004). (Pubitemid 38931765)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.7 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 3
    • 67649422321 scopus 로고    scopus 로고
    • Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer
    • O'Neill, L. A., Bryant, C. E. & Doyle, S. L. Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer. Pharmacol. Rev. 61, 177-197 (2009).
    • (2009) Pharmacol. Rev. , vol.61 , pp. 177-197
    • O'Neill, L.A.1    Bryant, C.E.2    Doyle, S.L.3
  • 4
    • 70350689747 scopus 로고    scopus 로고
    • The potential use of Toll-like receptor (TLR) agonists and antagonists as prophylactic and/or therapeutic agents
    • Makkouk, A. & Abdelnoor, A. M. The potential use of Toll-like receptor (TLR) agonists and antagonists as prophylactic and/or therapeutic agents. Immunopharmacol. Immunotoxicol. 31, 331-338 (2009).
    • (2009) Immunopharmacol. Immunotoxicol. , vol.31 , pp. 331-338
    • Makkouk, A.1    Abdelnoor, A.M.2
  • 5
    • 84870189452 scopus 로고    scopus 로고
    • Therapeutic applications of nucleic acids and their analogues in Toll-like receptor signaling
    • Gosu, V., Basith, S., Kwon, O. P. & Choi, S. Therapeutic applications of nucleic acids and their analogues in Toll-like receptor signaling. Molecules 17, 13503-13529 (2012).
    • (2012) Molecules , vol.17 , pp. 13503-13529
    • Gosu, V.1    Basith, S.2    Kwon, O.P.3    Choi, S.4
  • 7
    • 0037292275 scopus 로고    scopus 로고
    • Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members
    • DOI 10.1016/S1097-2765(03)00053-4
    • Janssens, S. & Beyaert, R. Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members. Mol. Cell 11, 293-302 (2003). (Pubitemid 36293825)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 293-302
    • Janssens, S.1    Beyaert, R.2
  • 8
    • 84869108498 scopus 로고    scopus 로고
    • Molecular evolution and structural features of irak family members
    • Gosu, V., Basith, S., Durai, P. & Choi, S. Molecular evolution and structural features of IRAK family members. PLoS One 7, e49771 (2012).
    • (2012) PLoS One , vol.7
    • Gosu, V.1    Basith, S.2    Durai, P.3    Choi, S.4
  • 11
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • DOI 10.1016/S0167-4889(02)00320-8, PII S0167488902003208
    • Martin, M. U. & Wesche, H. Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family. Biochim. Biophys. Acta. 1592, 265-280 (2002). (Pubitemid 35284883)
    • (2002) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1592 , Issue.3 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 13
    • 34848844641 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the endogenous type I interlukin-1 (IL-1) receptor signaling complex formed after IL-1 binding identifies IL-1RAcP, MyD88, and IRAK-4 as the stable components
    • DOI 10.1074/mcp.M600455-MCP200
    • Brikos, C.,Wait, R., Begum, S., O'Neill, L. A. J. & Saklatvala, J. Mass Spectrometric Analysis of the Endogenous Type I Interleukin-1 (IL-1) Receptor Signaling Complex Formed after IL-1 Binding Identifies IL-1RAcP, MyD88, and IRAK-4 as the Stable Components. Mol. Cell. Proteomics 6, 1551-1559 (2007). (Pubitemid 47506166)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1551-1559
    • Briskos, C.1    Wait, R.2    Begum, S.3    O'Neil, L.A.J.4    Saklatvala, J.5
  • 15
    • 0037129212 scopus 로고    scopus 로고
    • Severe impairment of interleukin-1 and Toll-like receptor signalling in mice lacking IRAK-4
    • Suzuki, N. et al. Severe impairment of interleukin-1 and Toll-like receptor signalling in mice lacking IRAK-4. Nature 416, 750-756 (2002).
    • (2002) Nature , vol.416 , pp. 750-756
    • Suzuki, N.1
  • 17
    • 18944391904 scopus 로고    scopus 로고
    • Cutting edge: Expression of IL-1 receptor-associated kinase-4 (IRAK-4) proteins with mutations identified in a patient with recurrent bacterial infections alters normal IRAK-4 interaction with components of the IL-1 receptor complex
    • Medvedev, A. E. et al. Cutting edge: Expression of IL-1 receptor-associated kinase-4 (IRAK-4) proteins with mutations identified in a patient with recurrent bacterial infections alters normal IRAK-4 interaction with components of the IL-1 receptor complex. J. Immunol. 174, 6587-6591 (2005). (Pubitemid 40705618)
    • (2005) Journal of Immunology , vol.174 , Issue.11 , pp. 6587-6591
    • Medvedev, A.E.1    Thomas, K.2    Awomoyi, A.3    Kuhns, D.B.4    Gallin, J.I.5    Li, X.6    Vogel, S.N.7
  • 18
    • 34948904198 scopus 로고    scopus 로고
    • Selective predisposition to bacterial infections in IRAK-4-deficient children: IRAK-4-dependent TLRs are otherwise redundant in protective immunity
    • Ku, C. L. et al. Selective predisposition to bacterial infections in IRAK-4-deficient children: IRAK-4-dependent TLRs are otherwise redundant in protective immunity. J. Exp. Med. 204, 2407-2422 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 2407-2422
    • Ku, C.L.1
  • 19
    • 19944431742 scopus 로고    scopus 로고
    • Inherited disorders of human Toll-like receptor signaling: Immunological implications
    • Ku, C. L. et al. Inherited disorders of human Toll-like receptor signaling: immunological implications. Immunol. Rev. 203, 10-20 (2005).
    • (2005) Immunol. Rev. , vol.203 , pp. 10-20
    • Ku, C.L.1
  • 20
    • 4644333526 scopus 로고    scopus 로고
    • The role of interleukin 1 receptor-associated kinase-4 (IRAK-4) kinase activity in IRAK-4-mediated signaling
    • DOI 10.1074/jbc.M402666200
    • Lye, E., Mirtsos, C., Suzuki, N., Suzuki, S. & Yeh, W. C. The role of interleukin 1 receptor-associated kinase-4 (IRAK-4) kinase activity in IRAK-4-mediated signaling. J. Biol. Chem. 279, 40653-40658 (2004). (Pubitemid 39287659)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40653-40658
    • Lye, E.1    Mirtsos, C.2    Suzuki, N.3    Suzuki, S.4    Yeh, W.-C.5
  • 22
    • 45149105507 scopus 로고    scopus 로고
    • Solving the IRAK-4 enigma: Application of kinase-dead knock-in mice
    • Koziczak-Holbro, M. et al. Solving the IRAK-4 enigma: Application of kinase-dead knock-in mice. Ernst Schering Found. Symp. Proc. 3, 63-82 (2007).
    • (2007) Ernst Schering Found. Symp. Proc. , vol.3 , pp. 63-82
    • Koziczak-Holbro, M.1
  • 23
    • 34249078495 scopus 로고    scopus 로고
    • A critical role for IRAK4 kinase activity in Toll-like receptormediated innate immunity
    • Kim, T. W. et al. A critical role for IRAK4 kinase activity in Toll-like receptormediated innate immunity. J. Exp. Med. 204, 1025-1036 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 1025-1036
    • Kim, T.W.1
  • 24
    • 43649107807 scopus 로고    scopus 로고
    • IRAK-4 kinase activity is required for IRAK-4-dependent innate and adaptive immune responses
    • Lye, E., Dhanji, S., Calzascia, T., Elford, A. R. & Ohashi, P. S. IRAK-4 kinase activity is required for IRAK-4-dependent innate and adaptive immune responses. Eur. J. Immunol. 38, 870-876 (2008).
    • (2008) Eur. J. Immunol. , vol.38 , pp. 870-876
    • Lye, E.1    Dhanji, S.2    Calzascia, T.3    Elford, A.R.4    Ohashi, P.S.5
  • 26
    • 55349142293 scopus 로고    scopus 로고
    • IRAK-4-and MyD88-dependent pathways are essential for the removal of developing autoreactive B cells in humans
    • Isnardi, I. et al. IRAK-4-and MyD88-dependent pathways are essential for the removal of developing autoreactive B cells in humans. Immunity 29, 746-757 (2008).
    • (2008) Immunity , vol.29 , pp. 746-757
    • Isnardi, I.1
  • 27
    • 37549066665 scopus 로고    scopus 로고
    • Treatment of lupus-prone mice with a dual inhibitor of TLR7 and TLR9 leads to reduction of autoantibody production and amelioration of disease symptoms
    • Barrat, F. J., Meeker, T., Chan, J. H., Guiducci, C. & Coffman, R. L. Treatment of lupus-prone mice with a dual inhibitor of TLR7 and TLR9 leads to reduction of autoantibody production and amelioration of disease symptoms. Eur. J. Immunol. 37, 3582-3586 (2007).
    • (2007) Eur. J. Immunol. , vol.37 , pp. 3582-3586
    • Barrat, F.J.1    Meeker, T.2    Chan, J.H.3    Guiducci, C.4    Coffman, R.L.5
  • 28
    • 84898657461 scopus 로고    scopus 로고
    • The role of interleukin-1 receptorassociated kinases in Vogt-Koyanagi-Harada disease
    • Sun, M., Yang, P., Du, L., Yang, Y. & Ye, J. The role of interleukin-1 receptorassociated kinases in Vogt-Koyanagi-Harada disease. PLoS One 9, e93214 (2014).
    • (2014) PLoS One , vol.9
    • Sun, M.1    Yang, P.2    Du, L.3    Yang, Y.4    Ye, J.5
  • 29
    • 0029865142 scopus 로고    scopus 로고
    • IRAK: A kinase associated with the interleukin-1 receptor
    • Cao, Z., Henzel, W. J. & Gao, X. IRAK: A kinase associated with the interleukin-1 receptor. Science 271, 1128-1131 (1996). (Pubitemid 26075229)
    • (1996) Science , vol.271 , Issue.5252 , pp. 1128-1131
    • Cao, Z.1    Henzel, W.J.2    Gao, X.3
  • 30
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL- 1 signaling
    • DOI 10.1126/science.278.5343.1612
    • Muzio, M. IRAK (Pelle) Family Member IRAK-2 and MyD88 as Proximal Mediators of IL-1 Signaling. Science 278, 1612-1615 (1997). (Pubitemid 27516277)
    • (1997) Science , vol.278 , Issue.5343 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 31
    • 0033516561 scopus 로고    scopus 로고
    • IRAK-M is a novel member of the Pelle/interleukin-1 receptorassociated kinase (IRAK) family
    • Wesche, H. et al. IRAK-M is a novel member of the Pelle/interleukin-1 receptorassociated kinase (IRAK) family. J. Biol. Chem. 274, 19403-19410 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 19403-19410
    • Wesche, H.1
  • 32
    • 33845231575 scopus 로고    scopus 로고
    • Crystal Structures of IRAK-4 Kinase in Complex with Inhibitors: A Serine/Threonine Kinase with Tyrosine as a Gatekeeper
    • DOI 10.1016/j.str.2006.11.001, PII S0969212606004370
    • Wang, Z. et al. Crystal Structures of IRAK-4 Kinase in Complex with Inhibitors: A Serine/Threonine Kinase with Tyrosine as a Gatekeeper. Structure 14, 1835-1844 (2006). (Pubitemid 44855630)
    • (2006) Structure , vol.14 , Issue.12 , pp. 1835-1844
    • Wang, Z.1    Liu, J.2    Sudom, A.3    Ayres, M.4    Li, S.5    Wesche, H.6    Powers, J.P.7    Walker, N.P.C.8
  • 35
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • DOI 10.1021/cr000225s
    • Johnson, L. N. & Lewis, R. J. Structural basis for control by phosphorylation. Chem. Rev. 101, 2209-2242 (2001). (Pubitemid 35373017)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 36
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • Nolen, B., Taylor, S. & Ghosh, G. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15, 661-675 (2004). (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 38
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • DOI 10.1016/S0092-8674(00)81066-1
    • Goldberg, J., Nairn, A. C. & Kuriyan, J. Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. Cell 84, 875-887 (1996). (Pubitemid 26106857)
    • (1996) Cell , vol.84 , Issue.6 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 39
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • DOI 10.1038/385602a0
    • Sicheri, F., Moarefi, I. & Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609 (1997). (Pubitemid 27087567)
    • (1997) Nature , vol.385 , Issue.6617 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 40
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • DOI 10.1038/385595a0
    • Xu, W., Harrison, S. C. & Eck, M. J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602 (1997). (Pubitemid 27087566)
    • (1997) Nature , vol.385 , Issue.6617 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 41
    • 69349101321 scopus 로고    scopus 로고
    • Atomistic view of the conformational activation of Src kinase using the string method with swarms-of-trajectories
    • Gan, W., Yang, S. & Roux, B. Atomistic view of the conformational activation of Src kinase using the string method with swarms-of-trajectories. Biophys.J. 97, L8-L10 (2009).
    • (2009) Biophys. J. , vol.97
    • Gan, W.1    Yang, S.2    Roux, B.3
  • 42
    • 62549151081 scopus 로고    scopus 로고
    • Protein conformational transitions: The closure mechanism of a kinase explored by atomistic simulations
    • Berteotti, A. et al. Protein conformational transitions: the closure mechanism of a kinase explored by atomistic simulations. J. Am. Chem. Soc. 131, 244-250 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 244-250
    • Berteotti, A.1
  • 43
    • 33646266474 scopus 로고    scopus 로고
    • Conformational changes in protein loops and helices induced by post-translational phosphorylation
    • Groban, E. S., Narayanan, A. & Jacobson, M. P. Conformational changes in protein loops and helices induced by post-translational phosphorylation. PLoS Comput. Biol. 2, e32 (2006).
    • (2006) PLoS Comput. Biol. , vol.2
    • Groban, E.S.1    Narayanan, A.2    Jacobson, M.P.3
  • 44
    • 34248532092 scopus 로고    scopus 로고
    • Anatomy of a structural pathway for activation of the catalytic domain of Src kinase Hck
    • DOI 10.1002/prot.21334
    • Banavali, N. K. & Roux, B. Anatomy of a structural pathway for activation of the catalytic domain of Src kinase Hck. Proteins 67, 1096-1112 (2007). (Pubitemid 46753954)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.4 , pp. 1096-1112
    • Banavali, N.K.1    Roux, B.2
  • 45
    • 77955660530 scopus 로고    scopus 로고
    • Phosphorylationi and ATP-binding induced conformational changes in the PrkC, Ser/Thr kinase from B. Subtilis
    • Gruszczynski, P., Obuchowski, M. & Kazmierkiewicz, R. Phosphorylation and ATP-binding induced conformational changes in the PrkC, Ser/Thr kinase from B. subtilis. J. Comput. Aided. Mol. Des. 24, 733-747 (2010).
    • (2010) J. Comput. Aided. Mol. Des. , vol.24 , pp. 733-747
    • Gruszczynski, P.1    Obuchowski, M.2    Kazmierkiewicz, R.3
  • 47
    • 77950482089 scopus 로고    scopus 로고
    • Global consequences of activation loop phosphorylation on protein kinase A
    • Steichen, J. M. et al. Global consequences of activation loop phosphorylation on protein kinase A. J. Biol. Chem. 285, 3825-3832 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 3825-3832
    • Steichen, J.M.1
  • 48
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • DOI 10.1016/S0092-8674(00)81092-2
    • Johnson, L. N., Noble, M. E. & Owen, D. J. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158 (1996). (Pubitemid 26118158)
    • (1996) Cell , vol.85 , Issue.2 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 49
    • 0032524350 scopus 로고    scopus 로고
    • Autoregulatory mechanisms in protein-tyrosine kinases
    • DOI 10.1074/jbc.273.20.11987
    • Hubbard, S. R.,Mohammadi, M.,Schlessinger, J. Autoregulatory mechanisms in protein-tyrosine kinases. J. Biol. Chem. 273, 11987-11990 (1998). (Pubitemid 28240552)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 11987-11990
    • Hubbard, S.R.1    Mohammadi, M.2    Schlessinger, J.3
  • 51
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • DOI 10.1038/nsb0896-696
    • Russo, A. A., Jeffrey, P. D. & Pavletich, N. P. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700 (1996). (Pubitemid 26260060)
    • (1996) Nature Structural Biology , vol.3 , Issue.8 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 52
    • 3042584697 scopus 로고    scopus 로고
    • Structural modes of stabilization of permissive phosphorylation sites in protein kinases: Distinct strategies in Ser/Thr and Tyr kinases
    • DOI 10.1016/j.jmb.2004.04.043, PII S002228360400484X
    • Krupa, A., Preethi, G. & Srinivasan, N. Structural modes of stabilization of permissive phosphorylation sites in protein kinases: distinct strategies in Ser/Thr and Tyr kinases. J. Mol. Biol. 339, 1025-1039 (2004). (Pubitemid 39303246)
    • (2004) Journal of Molecular Biology , vol.339 , Issue.5 , pp. 1025-1039
    • Krupa, A.1    Preethi, G.2    Srinivasan, N.3
  • 53
    • 77957241496 scopus 로고    scopus 로고
    • Molecular dynamics simulations and elastic network analysis of protein kinase B (Akt/PKB) inactivation
    • Cheng, S. & Niv, M. Y. Molecular dynamics simulations and elastic network analysis of protein kinase B (Akt/PKB) inactivation. J. Chem. Inf. Model. 50, 1602-1610 (2010).
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 1602-1610
    • Cheng, S.1    Niv, M.Y.2
  • 54
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey, P. D. et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320 (1995).
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1
  • 55
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • Huse, M. & Kuriyan, J. The conformational plasticity of protein kinases. Cell 109, 275-282 (2002). (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 57
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • DOI 10.1021/cr000230w
    • Adams, J. A. Kinetic and catalytic mechanisms of protein kinases. Chem. Rev. 101, 2271-2290 (2001). (Pubitemid 35373019)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2271-2290
    • Adams, J.A.1
  • 58
    • 0025739664 scopus 로고
    • Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions
    • Gibbs, C. S. & Zoller, M. J. Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J. Biol. Chem. 266, 8923-8931 (1991). (Pubitemid 21906599)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.14 , pp. 8923-8931
    • Gibbs, C.S.1    Zoller, M.J.2
  • 59
    • 0036215864 scopus 로고    scopus 로고
    • Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase
    • DOI 10.1038/nsb780
    • Madhusudan Akamine, P., Xuong, N. H. & Taylor, S. S. Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase. Nat. Struct. Biol. 9, 273-277 (2002). (Pubitemid 34289899)
    • (2002) Nature Structural Biology , vol.9 , Issue.4 , pp. 273-277
    • Madhusudan Akamine, P.1    Xuong, N.-H.2    Taylor, S.S.3
  • 60
    • 33645523760 scopus 로고    scopus 로고
    • How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: A theoretical study
    • Cheng, Y., Zhang, Y. & McCammon, J. A. How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: A theoretical study. Protein Sci. 15, 672-683 (2006).
    • (2006) Protein Sci. , vol.15 , pp. 672-683
    • Cheng, Y.1    Zhang, Y.2    McCammon, J.A.3
  • 61
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura, N. et al. Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms. Mol. Cell 42, 9-22 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 9-22
    • Jura, N.1
  • 62
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • Taylor, S. S. & Kornev, A. P. Protein kinases: Evolution of dynamic regulatory proteins. Trends Biochem. Sci. 36, 65-77 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 63
    • 79960121968 scopus 로고    scopus 로고
    • Infectious diseases in patients with IRAK-4, MyD88, NEMO, or IkappaBalpha deficiency
    • Picard, C., Casanova, J. L. & Puel, A. Infectious diseases in patients with IRAK-4, MyD88, NEMO, or IkappaBalpha deficiency. Clin. Microbiol. Rev. 24, 490-497 (2011).
    • (2011) Clin. Microbiol. Rev. , vol.24 , pp. 490-497
    • Picard, C.1    Casanova, J.L.2    Puel, A.3
  • 66
    • 84883487963 scopus 로고    scopus 로고
    • Autophosphorylation of gatekeeper tyrosine by symbiosis receptor kinase
    • Samaddar, S. et al. Autophosphorylation of gatekeeper tyrosine by symbiosis receptor kinase. FEBS Lett. 587, 2972-2979 (2013).
    • (2013) FEBS Lett. , vol.587 , pp. 2972-2979
    • Samaddar, S.1
  • 67
    • 79953189068 scopus 로고    scopus 로고
    • Structure-function similarities between a plant receptorlike kinase and the human interleukin-1 receptor-associated kinase-4
    • Klaus-Heisen, D. et al. Structure-function similarities between a plant receptorlike kinase and the human interleukin-1 receptor-associated kinase-4. J. Biol. Chem. 286, 11202-11210 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 11202-11210
    • Klaus-Heisen, D.1
  • 69
    • 18944386711 scopus 로고    scopus 로고
    • The active conformation of the PAK1 kinase domain
    • DOI 10.1016/j.str.2005.03.007, PII S0969212605001279
    • Lei, M., Robinson, M. A. & Harrison, S. C. The active conformation of the PAK1 kinase domain. Structure 13, 769-778 (2005). (Pubitemid 40704665)
    • (2005) Structure , vol.13 , Issue.5 , pp. 769-778
    • Lei, M.1    Robinson, M.A.2    Harrison, S.C.3
  • 70
    • 77449154335 scopus 로고    scopus 로고
    • Steady-state kinetic characterization of kinase activity and requirements for Mg21of interleukin-1 receptor-associated kinase-4
    • Hekmat-Nejad, M., Cai, T. & Swinney, D. C. Steady-state kinetic characterization of kinase activity and requirements for Mg21of interleukin-1 receptor-associated kinase-4. Biochemistry 49, 1495-1506 (2010).
    • (2010) Biochemistry , vol.49 , pp. 1495-1506
    • Hekmat-Nejad, M.1    Cai, T.2    Swinney, D.C.3
  • 71
    • 81255169335 scopus 로고    scopus 로고
    • Role of Mg21 ions in protein kinase phosphorylation: Insights from molecular dynamics simulations of ATP-kinase complexes
    • Yu, L. et al. Role of Mg21 ions in protein kinase phosphorylation: insights from molecular dynamics simulations of ATP-kinase complexes. Molecular Simulation 37, 1143-1150 (2011).
    • (2011) Molecular Simulation , vol.37 , pp. 1143-1150
    • Yu, L.1
  • 72
    • 84861205906 scopus 로고    scopus 로고
    • Cotranslational cis-phosphorylation of the COOHterminal tail is a key priming step in the maturation of cAMP-dependent protein kinase
    • Keshwani, M. M. et al. Cotranslational cis-phosphorylation of the COOHterminal tail is a key priming step in the maturation of cAMP-dependent protein kinase. Proc. Natl. Acad. Sci. U. S. A. 109, E1221-1229 (2012).
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Keshwani, M.M.1
  • 74
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B.,Kutzner,C., van der Spoel, D.,Lindahl, E.GROMACS4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J. Chem. Theory Comput. 4, 435-447 (2008).
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 76
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems
    • Darden, T., York, D. & Pedersen, L. Particle mesh Ewald: An N [center-dot] log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092 (1993).
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 78
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 81
    • 0032522136 scopus 로고    scopus 로고
    • Essential dynamics of DNA containing a cis.syn cyclobutane thymine dimer lesion
    • DOI 10.1093/nar/26.8.1939
    • Yamaguchi, H., van Aalten, D. M., Pinak, M., Furukawa, A. ,Osman, R. Essential dynamics of DNA containing a cis.syn cyclobutane thymine dimer lesion. Nucleic Acids Res. 26, 1939-1946 (1998). (Pubitemid 28291726)
    • (1998) Nucleic Acids Research , vol.26 , Issue.8 , pp. 1939-1946
    • Yamaguchi, H.1    Van Aalten, D.M.F.2    Pinak, M.3    Furukawa, A.4    Osman, R.5
  • 82
    • 0029586726 scopus 로고
    • Essential dynamics of the cellular retinol-binding protein - Evidence for ligand-induced conformational changes
    • van Aalten, D. M., Findlay, J. B., Amadei, A.,Berendsen,H. J. Essential dynamics of the cellular retinol-binding protein-evidence for ligand-induced conformational changes. Protein Eng. 8, 1129-1135 (1995). (Pubitemid 26066519)
    • (1995) Protein Engineering , vol.8 , Issue.11 , pp. 1129-1135
    • Van Aalten, D.M.F.1    Findlay, J.B.C.2    Amadei, A.3    Berendsen, H.J.C.4


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