메뉴 건너뛰기




Volumn 108, Issue 2, 2015, Pages 395-407

Effects of HCM cTnI mutation R145G on troponin structure and modulation by PKA phosphorylation elucidated by molecular dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; TROPONIN I;

EID: 84921473973     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.11.3461     Document Type: Article
Times cited : (39)

References (57)
  • 1
    • 17744382824 scopus 로고    scopus 로고
    • Structural based insights into the role of troponin in cardiac muscle pathophysiology
    • M.X. Li, X. Wang, and B.D. Sykes Structural based insights into the role of troponin in cardiac muscle pathophysiology J. Muscle Res. Cell Motil. 25 2004 559 579
    • (2004) J. Muscle Res. Cell Motil. , vol.25 , pp. 559-579
    • Li, M.X.1    Wang, X.2    Sykes, B.D.3
  • 2
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • C.S. Farah, and F.C. Reinach The troponin complex and regulation of muscle contraction FASEB J. 9 1995 755 767
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 3
    • 84867637621 scopus 로고    scopus 로고
    • Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C
    • S. Lindert, P.M. Kekenes-Huskey, and J.A. McCammon Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C Biophys. J. 103 2012 1784 1789
    • (2012) Biophys. J. , vol.103 , pp. 1784-1789
    • Lindert, S.1    Kekenes-Huskey, P.M.2    McCammon, J.A.3
  • 4
    • 15544390385 scopus 로고    scopus 로고
    • Calcium, thin filaments, and the integrative biology of cardiac contractility
    • T. Kobayashi, and R.J. Solaro Calcium, thin filaments, and the integrative biology of cardiac contractility Annu. Rev. Physiol. 67 2005 39 67
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 39-67
    • Kobayashi, T.1    Solaro, R.J.2
  • 5
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • A.M. Gordon, E. Homsher, and M. Regnier Regulation of contraction in striated muscle Physiol. Rev. 80 2000 853 924
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 6
    • 53549129239 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium
    • B.A. Colson, and T. Bekyarova R.L. Moss Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium Circ. Res. 103 2008 244 251
    • (2008) Circ. Res. , vol.103 , pp. 244-251
    • Colson, B.A.1    Bekyarova, T.2    Moss, R.L.3
  • 7
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin i by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • J.C. Kentish, and D.T. McCloskey R.J. Solaro Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle Circ. Res. 88 2001 1059 1065
    • (2001) Circ. Res. , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Solaro, R.J.3
  • 8
    • 0029037870 scopus 로고
    • Cardiac troponin i phosphorylation increases the rate of cardiac muscle relaxation
    • R. Zhang, and J. Zhao J.D. Potter Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation Circ. Res. 76 1995 1028 1035
    • (1995) Circ. Res. , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Potter, J.D.3
  • 9
    • 84908353054 scopus 로고    scopus 로고
    • PKA phosphorylation of cardiac troponin i modulates activation and relaxation kinetics of ventricular myofibrils
    • V. Rao, and Y. Cheng M. Regnier PKA phosphorylation of cardiac troponin I modulates activation and relaxation kinetics of ventricular myofibrils Biophys. J. 107 2014 1196 1204
    • (2014) Biophys. J. , vol.107 , pp. 1196-1204
    • Rao, V.1    Cheng, Y.2    Regnier, M.3
  • 10
    • 40849096222 scopus 로고    scopus 로고
    • The unique functions of cardiac troponin i in the control of cardiac muscle contraction and relaxation
    • R.J. Solaro, P. Rosevear, and T. Kobayashi The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation Biochem. Biophys. Res. Commun. 369 2008 82 87
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 82-87
    • Solaro, R.J.1    Rosevear, P.2    Kobayashi, T.3
  • 11
    • 0030765610 scopus 로고    scopus 로고
    • Mutations in the cardiac troponin i gene associated with hypertrophic cardiomyopathy
    • A. Kimura, and H. Harada T. Sasazuki Mutations in the cardiac troponin I gene associated with hypertrophic cardiomyopathy Nat. Genet. 16 1997 379 382
    • (1997) Nat. Genet. , vol.16 , pp. 379-382
    • Kimura, A.1    Harada, H.2    Sasazuki, T.3
  • 12
    • 0035807934 scopus 로고    scopus 로고
    • Effects of phosphorylation and mutation R145G on human cardiac troponin i function
    • Y. Deng, and A. Schmidtmann R. Thieleczek Effects of phosphorylation and mutation R145G on human cardiac troponin I function Biochemistry 40 2001 14593 14602
    • (2001) Biochemistry , vol.40 , pp. 14593-14602
    • Deng, Y.1    Schmidtmann, A.2    Thieleczek, R.3
  • 13
    • 0034698086 scopus 로고    scopus 로고
    • Altered regulatory properties of human cardiac troponin i mutants that cause hypertrophic cardiomyopathy
    • K. Elliott, H. Watkins, and C.S. Redwood Altered regulatory properties of human cardiac troponin I mutants that cause hypertrophic cardiomyopathy J. Biol. Chem. 275 2000 22069 22074
    • (2000) J. Biol. Chem. , vol.275 , pp. 22069-22074
    • Elliott, K.1    Watkins, H.2    Redwood, C.S.3
  • 14
    • 0035695803 scopus 로고    scopus 로고
    • Functional consequences of the mutations in human cardiac troponin i gene found in familial hypertrophic cardiomyopathy
    • F. Takahashi-Yanaga, and S. Morimoto I. Ohtsuki Functional consequences of the mutations in human cardiac troponin I gene found in familial hypertrophic cardiomyopathy J. Mol. Cell. Cardiol. 33 2001 2095 2107
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 2095-2107
    • Takahashi-Yanaga, F.1    Morimoto, S.2    Ohtsuki, I.3
  • 15
    • 2442639087 scopus 로고    scopus 로고
    • Effects of protein kinase C dependent phosphorylation and a familial hypertrophic cardiomyopathy-related mutation of cardiac troponin i on structural transition of troponin C and myofilament activation
    • T. Kobayashi, and W.J. Dong R.J. Solaro Effects of protein kinase C dependent phosphorylation and a familial hypertrophic cardiomyopathy-related mutation of cardiac troponin I on structural transition of troponin C and myofilament activation Biochemistry 43 2004 5996 6004
    • (2004) Biochemistry , vol.43 , pp. 5996-6004
    • Kobayashi, T.1    Dong, W.J.2    Solaro, R.J.3
  • 16
    • 33744954871 scopus 로고    scopus 로고
    • Increased Ca2+ affinity of cardiac thin filaments reconstituted with cardiomyopathy-related mutant cardiac troponin i
    • T. Kobayashi, and R.J. Solaro Increased Ca2+ affinity of cardiac thin filaments reconstituted with cardiomyopathy-related mutant cardiac troponin I J. Biol. Chem. 281 2006 13471 13477
    • (2006) J. Biol. Chem. , vol.281 , pp. 13471-13477
    • Kobayashi, T.1    Solaro, R.J.2
  • 17
    • 84908220236 scopus 로고    scopus 로고
    • Computational studies of the effect of the S23D/S24D troponin i mutation on cardiac troponin structural dynamics
    • Y. Cheng, and S. Lindert M. Regnier Computational studies of the effect of the S23D/S24D troponin I mutation on cardiac troponin structural dynamics Biophys. J. 107 2014 1675 1685
    • (2014) Biophys. J. , vol.107 , pp. 1675-1685
    • Cheng, Y.1    Lindert, S.2    Regnier, M.3
  • 19
    • 34249676905 scopus 로고    scopus 로고
    • The troponin C G159D mutation blunts myofilament desensitization induced by troponin i Ser23/24 phosphorylation
    • B.J. Biesiadecki, and T. Kobayashi P.P. de Tombe The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation Circ. Res. 100 2007 1486 1493
    • (2007) Circ. Res. , vol.100 , pp. 1486-1493
    • Biesiadecki, B.J.1    Kobayashi, T.2    De Tombe, P.P.3
  • 20
    • 0029561016 scopus 로고
    • Reconstitution of skinned cardiac fibres with human recombinant cardiac troponin-I mutants and troponin-C
    • C. Dohet, and E. al-Hillawi J.C. Rüegg Reconstitution of skinned cardiac fibres with human recombinant cardiac troponin-I mutants and troponin-C FEBS Lett. 377 1995 131 134
    • (1995) FEBS Lett. , vol.377 , pp. 131-134
    • Dohet, C.1    Al-Hillawi, E.2    Rüegg, J.C.3
  • 21
    • 0032773882 scopus 로고    scopus 로고
    • NMR analysis of cardiac troponin C-troponin i complexes: Effects of phosphorylation
    • N. Finley, and M.B. Abbott P.R. Rosevear NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation FEBS Lett. 453 1999 107 112
    • (1999) FEBS Lett. , vol.453 , pp. 107-112
    • Finley, N.1    Abbott, M.B.2    Rosevear, P.R.3
  • 22
    • 84884284974 scopus 로고    scopus 로고
    • Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24
    • L.M. Hanft, B.J. Biesiadecki, and K.S. McDonald Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24 J. Physiol. 591 2013 4535 4547
    • (2013) J. Physiol. , vol.591 , pp. 4535-4547
    • Hanft, L.M.1    Biesiadecki, B.J.2    McDonald, K.S.3
  • 23
    • 12844260739 scopus 로고    scopus 로고
    • In vivo and in vitro analysis of cardiac troponin i phosphorylation
    • S. Sakthivel, and N.L. Finley J. Robbins In vivo and in vitro analysis of cardiac troponin I phosphorylation J. Biol. Chem. 280 2005 703 714
    • (2005) J. Biol. Chem. , vol.280 , pp. 703-714
    • Sakthivel, S.1    Finley, N.L.2    Robbins, J.3
  • 24
    • 1542343926 scopus 로고    scopus 로고
    • Frequency- and afterload-dependent cardiac modulation in vivo by troponin i with constitutively active protein kinase A phosphorylation sites
    • E. Takimoto, and D.G. Soergel A.M. Murphy Frequency- and afterload-dependent cardiac modulation in vivo by troponin I with constitutively active protein kinase A phosphorylation sites Circ. Res. 94 2004 496 504
    • (2004) Circ. Res. , vol.94 , pp. 496-504
    • Takimoto, E.1    Soergel, D.G.2    Murphy, A.M.3
  • 25
    • 84872425232 scopus 로고    scopus 로고
    • Impact of site-specific phosphorylation of protein kinase A sites Ser23 and Ser24 of cardiac troponin i in human cardiomyocytes
    • P.J. Wijnker, and D.B. Foster J. van der Velden Impact of site-specific phosphorylation of protein kinase A sites Ser23 and Ser24 of cardiac troponin I in human cardiomyocytes Am. J. Physiol. Heart Circ. Physiol. 304 2013 H260 H268
    • (2013) Am. J. Physiol. Heart Circ. Physiol. , vol.304 , pp. H260-H268
    • Wijnker, P.J.1    Foster, D.B.2    Van Der Velden, J.3
  • 26
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • R. Yamasaki, and Y. Wu H. Granzier Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes Circ. Res. 90 2002 1181 1188
    • (2002) Circ. Res. , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    Granzier, H.3
  • 27
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • S. Takeda, and A. Yamashita Y. Maéda Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form Nature 424 2003 35 41
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maéda, Y.3
  • 28
    • 0036310711 scopus 로고    scopus 로고
    • On the role of the crystal environment in determining protein side-chain conformations
    • M.P. Jacobson, and R.A. Friesner B. Honig On the role of the crystal environment in determining protein side-chain conformations J. Mol. Biol. 320 2002 597 608
    • (2002) J. Mol. Biol. , vol.320 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Honig, B.3
  • 29
    • 1842532008 scopus 로고    scopus 로고
    • A hierarchical approach to all-atom protein loop prediction
    • M.P. Jacobson, and D.L. Pincus R.A. Friesner A hierarchical approach to all-atom protein loop prediction Proteins 55 2004 351 367
    • (2004) Proteins , vol.55 , pp. 351-367
    • Jacobson, M.P.1    Pincus, D.L.2    Friesner, R.A.3
  • 30
    • 2442449534 scopus 로고    scopus 로고
    • Modeling structurally variable regions in homologous proteins with rosetta
    • C.A. Rohl, and C.E. Strauss D. Baker Modeling structurally variable regions in homologous proteins with rosetta Proteins 55 2004 656 677
    • (2004) Proteins , vol.55 , pp. 656-677
    • Rohl, C.A.1    Strauss, C.E.2    Baker, D.3
  • 31
    • 33644949935 scopus 로고    scopus 로고
    • Recapitulation and design of protein binding peptide structures and sequences
    • V.D. Sood, and D. Baker Recapitulation and design of protein binding peptide structures and sequences J. Mol. Biol. 357 2006 917 927
    • (2006) J. Mol. Biol. , vol.357 , pp. 917-927
    • Sood, V.D.1    Baker, D.2
  • 32
    • 80051983795 scopus 로고    scopus 로고
    • A model of calcium activation of the cardiac thin filament
    • E.P. Manning, J.C. Tardiff, and S.D. Schwartz A model of calcium activation of the cardiac thin filament Biochemistry 50 2011 7405 7413
    • (2011) Biochemistry , vol.50 , pp. 7405-7413
    • Manning, E.P.1    Tardiff, J.C.2    Schwartz, S.D.3
  • 34
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • A.D. MacKerell Jr., N. Banavali, and N. Foloppe Development and current status of the CHARMM force field for nucleic acids Biopolymers 56 2000-2001 257 265
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • Mackerell, Jr.A.D.1    Banavali, N.2    Foloppe, N.3
  • 36
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 37
    • 84861857352 scopus 로고    scopus 로고
    • Structural and functional consequences of the cardiac troponin C L48Q Ca(2+)-sensitizing mutation
    • D. Wang, and I.M. Robertson M. Regnier Structural and functional consequences of the cardiac troponin C L48Q Ca(2+)-sensitizing mutation Biochemistry 51 2012 4473 4487
    • (2012) Biochemistry , vol.51 , pp. 4473-4487
    • Wang, D.1    Robertson, I.M.2    Regnier, M.3
  • 38
    • 0033536456 scopus 로고    scopus 로고
    • Inclusion of solvation in ligand binding free energy calculations using the generalized-Born model
    • X.Q. Zou, Y.X. Sun, and I.D. Kuntz Inclusion of solvation in ligand binding free energy calculations using the generalized-Born model J. Am. Chem. Soc. 121 1999 8033 8043
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8033-8043
    • Zou, X.Q.1    Sun, Y.X.2    Kuntz, I.D.3
  • 39
    • 79951996670 scopus 로고    scopus 로고
    • Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking
    • T. Hou, and J. Wang W. Wang Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking J. Comput. Chem. 32 2011 866 877
    • (2011) J. Comput. Chem. , vol.32 , pp. 866-877
    • Hou, T.1    Wang, J.2    Wang, W.3
  • 40
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • W.C. Still, and A. Tempczyk T. Hendrickson Semianalytical treatment of solvation for molecular mechanics and dynamics J. Am. Chem. Soc. 112 1990 6127 6129
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hendrickson, T.3
  • 41
    • 80755176366 scopus 로고    scopus 로고
    • Parallel generalized Born implicit solvent calculations with NAMD
    • D.E. Tanner, and K.Y. Chan K. Schulten Parallel generalized Born implicit solvent calculations with NAMD J. Chem. Theory Comput. 7 2011 3635 3642
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 3635-3642
    • Tanner, D.E.1    Chan, K.Y.2    Schulten, K.3
  • 42
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized Born model
    • A. Onufriev, D. Bashford, and D.A. Case Exploring protein native states and large-scale conformational changes with a modified generalized Born model Proteins 55 2004 383 394
    • (2004) Proteins , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 43
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized Born solvation model in macromolecular simulations
    • V. Tsui, and D.A. Case Theory and applications of the generalized Born solvation model in macromolecular simulations Biopolymers 56 2000-2001 275 291
    • (2000) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 44
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • J. Weiser, P.S. Shenkin, and W.C. Still Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO) J. Comput. Chem. 20 1999 217 230
    • (1999) J. Comput. Chem. , vol.20 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 45
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii
    • D. Qiu, and P.S. Shenkin W.C. Still The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii J. Phys. Chem. A 101 1997 3005 3014
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Still, W.C.3
  • 46
    • 0347602124 scopus 로고    scopus 로고
    • Converging free energy estimates: MM-PB(GB)SA studies on the protein-protein complex Ras-Raf
    • H. Gohlke, and D.A. Case Converging free energy estimates: MM-PB(GB)SA studies on the protein-protein complex Ras-Raf J. Comput. Chem. 25 2004 238 250
    • (2004) J. Comput. Chem. , vol.25 , pp. 238-250
    • Gohlke, H.1    Case, D.A.2
  • 47
    • 84907689207 scopus 로고    scopus 로고
    • The cardiac-specific N-terminal region of troponin i positions the regulatory domain of troponin C
    • P.M. Hwang, and F. Cai B.D. Sykes The cardiac-specific N-terminal region of troponin I positions the regulatory domain of troponin C Proc. Natl. Acad. Sci. USA 111 2014 14412 14417
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 14412-14417
    • Hwang, P.M.1    Cai, F.2    Sykes, B.D.3
  • 48
    • 84863513224 scopus 로고    scopus 로고
    • Molecular effects of familial hypertrophic cardiomyopathy-related mutations in the TNT1 domain of cTnT
    • E.P. Manning, J.C. Tardiff, and S.D. Schwartz Molecular effects of familial hypertrophic cardiomyopathy-related mutations in the TNT1 domain of cTnT J. Mol. Biol. 421 2012 54 66
    • (2012) J. Mol. Biol. , vol.421 , pp. 54-66
    • Manning, E.P.1    Tardiff, J.C.2    Schwartz, S.D.3
  • 49
    • 84876930263 scopus 로고    scopus 로고
    • Structural and kinetic effects of hypertrophic cardiomyopathy related mutations R146G/Q and R163W on the regulatory switching activity of rat cardiac troponin i
    • Z. Zhou, and D. Rieck W.J. Dong Structural and kinetic effects of hypertrophic cardiomyopathy related mutations R146G/Q and R163W on the regulatory switching activity of rat cardiac troponin I Arch. Biochem. Biophys. 535 2013 56 67
    • (2013) Arch. Biochem. Biophys. , vol.535 , pp. 56-67
    • Zhou, Z.1    Rieck, D.2    Dong, W.J.3
  • 50
    • 84892387716 scopus 로고    scopus 로고
    • Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes
    • H. Beard, and A. Cholleti K.A. Loving Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes PLoS ONE 8 2013 e82849
    • (2013) PLoS ONE , vol.8 , pp. e82849
    • Beard, H.1    Cholleti, A.2    Loving, K.A.3
  • 51
    • 79952586341 scopus 로고    scopus 로고
    • A computational and experimental approach to investigate bepridil binding with cardiac troponin
    • J.F. Varughese, and T. Baxley Y. Li A computational and experimental approach to investigate bepridil binding with cardiac troponin J. Phys. Chem. B 115 2011 2392 2400
    • (2011) J. Phys. Chem. B , vol.115 , pp. 2392-2400
    • Varughese, J.F.1    Baxley, T.2    Li, Y.3
  • 52
    • 84887117107 scopus 로고    scopus 로고
    • Molecular recognition in a diverse set of protein-ligand interactions studied with molecular dynamics simulations and end-point free energy calculations
    • B. Wang, and L. Li S.O. Meroueh Molecular recognition in a diverse set of protein-ligand interactions studied with molecular dynamics simulations and end-point free energy calculations J. Chem. Inf. Model. 53 2013 2659 2670
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 2659-2670
    • Wang, B.1    Li, L.2    Meroueh, S.O.3
  • 53
    • 84870579518 scopus 로고    scopus 로고
    • Entropy-enthalpy transduction caused by conformational shifts can obscure the forces driving protein-ligand binding
    • A.T. Fenley, H.S. Muddana, and M.K. Gilson Entropy-enthalpy transduction caused by conformational shifts can obscure the forces driving protein-ligand binding Proc. Natl. Acad. Sci. USA 109 2012 20006 20011
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 20006-20011
    • Fenley, A.T.1    Muddana, H.S.2    Gilson, M.K.3
  • 54
    • 17844363735 scopus 로고    scopus 로고
    • Effects of the mutation R145G in human cardiac troponin i on the kinetics of the contraction-relaxation cycle in isolated cardiac myofibrils
    • M. Kruger, and S. Zittrich R. Stehle Effects of the mutation R145G in human cardiac troponin I on the kinetics of the contraction-relaxation cycle in isolated cardiac myofibrils J. Physiol. 564 2005 347 357
    • (2005) J. Physiol. , vol.564 , pp. 347-357
    • Kruger, M.1    Zittrich, S.2    Stehle, R.3
  • 55
    • 84870693969 scopus 로고    scopus 로고
    • Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: A multi-scale simulation study
    • P.M. Kekenes-Huskey, S. Lindert, and J.A. McCammon Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: a multi-scale simulation study PLOS Comput. Biol. 8 2012 e1002777
    • (2012) PLOS Comput. Biol. , vol.8 , pp. e1002777
    • Kekenes-Huskey, P.M.1    Lindert, S.2    McCammon, J.A.3
  • 56
    • 34748818674 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin i in cardiac troponin
    • J.W. Howarth, and J. Meller P.R. Rosevear Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin J. Mol. Biol. 373 2007 706 722
    • (2007) J. Mol. Biol. , vol.373 , pp. 706-722
    • Howarth, J.W.1    Meller, J.2    Rosevear, P.R.3
  • 57
    • 42049094204 scopus 로고    scopus 로고
    • Role of the acidic N' region of cardiac troponin i in regulating myocardial function
    • S. Sadayappan, and N. Finley J. Robbins Role of the acidic N' region of cardiac troponin I in regulating myocardial function FASEB J. 22 2008 1246 1257
    • (2008) FASEB J. , vol.22 , pp. 1246-1257
    • Sadayappan, S.1    Finley, N.2    Robbins, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.