메뉴 건너뛰기




Volumn 37, Issue 5, 2008, Pages 683-691

Analyzing pathogenic mutations of C5 domain from cardiac myosin binding protein C through MD simulations

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN BINDING PROTEIN C;

EID: 45249113723     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0308-x     Document Type: Article
Times cited : (7)

References (32)
  • 2
    • 0035371215 scopus 로고    scopus 로고
    • The structural basis of antiviral drug resistance and role of folding pathways in HIV-1 protease
    • Cecconi F, Micheletti C, Carloni P, Maritan A (2001) The structural basis of antiviral drug resistance and role of folding pathways in HIV-1 protease. Proteins Struct Funct Genet 43:365-372
    • (2001) Proteins Struct Funct Genet , vol.43 , pp. 365-372
    • Cecconi, F.1    Micheletti, C.2    Carloni, P.3    Maritan, A.4
  • 5
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM (1999) Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat Struct Biol 6:1005-1009
    • (1999) Nat Struct Biol , vol.6 , pp. 1005-1009
    • Chiti, F.1    Taddei, N.2    White, P.M.3    Bucciantini, M.4    Magherini, F.5    Stefani, M.6    Dobson, C.M.7
  • 6
    • 31444452031 scopus 로고    scopus 로고
    • P versus Q: Structural reaction coordinates capture protein folding on smooth landscapes
    • Cho SS, Levy Y, Wolynes PG (2006) P versus Q: structural reaction coordinates capture protein folding on smooth landscapes. Proc Natl Acad Sci USA 103:586-591
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 586-591
    • Cho, S.S.1    Levy, Y.2    Wolynes, P.G.3
  • 7
    • 0642280767 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: From gene defect to clinical disease
    • Chung MW, Tsoutsman T, Semsarian C (2003) Hypertrophic cardiomyopathy: from gene defect to clinical disease. Cell Res 13:9-20
    • (2003) Cell Res , vol.13 , pp. 9-20
    • Chung, M.W.1    Tsoutsman, T.2    Semsarian, C.3
  • 8
    • 34547709547 scopus 로고    scopus 로고
    • Thermal unfolding of proteins
    • 1-4
    • Cieplak M, Sulkowska JI (2005) Thermal unfolding of proteins. J Chem Phys 123:194908 1-4
    • (2005) J Chem Phys , vol.123 , pp. 194908
    • Cieplak, M.1    Sulkowska, J.I.2
  • 9
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway
    • Clarke J, Cota E, Fowler SB, Hamill S (1999) Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway. Structure 7:1145-1153
    • (1999) Structure , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.4
  • 10
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding?
    • Clementi C, Nymeyer H, Onuchic JN (2000) Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? J Mol Biol 298:937-953
    • (2000) J Mol Biol , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 11
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg AM, Swendsen RH (1989) Optimized Monte Carlo data analysis. Phys Rev Lett 63:1195-1198
    • (1989) Phys Rev Lett , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 12
    • 0026511656 scopus 로고
    • The folding of an enzime. 1. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht AR, Matouschek A, Serrano L (1992) The folding of an enzime. 1. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol 224:771-782
    • (1992) J Mol Biol , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 13
    • 2642572455 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C: Its role in physiology and disease
    • Flashman E, Redwood C, Moolman-Smook J, Watkins H (2004) Cardiac myosin binding protein C: its role in physiology and disease. Circ Res 94:1279-1289
    • (2004) Circ Res , vol.94 , pp. 1279-1289
    • Flashman, E.1    Redwood, C.2    Moolman-Smook, J.3    Watkins, H.4
  • 14
    • 18344362394 scopus 로고
    • On the use of classical statistical mechanics in the treatment of polymer chain conformations
    • Gō N, Scheraga HA (1976) On the use of classical statistical mechanics in the treatment of polymer chain conformations. Macromolecules 9:535-542
    • (1976) Macromolecules , vol.9 , pp. 535-542
    • Go, N.1    Scheraga, H.A.2
  • 15
    • 38949163021 scopus 로고    scopus 로고
    • Stability and kinetic properties of C5-domain of Myosin binding protein C and its mutants
    • Guardiani C, Cecconi F, Livi R (2008) Stability and kinetic properties of C5-domain of Myosin binding protein C and its mutants. Biophys J 94:1403-1411
    • (2008) Biophys J , vol.94 , pp. 1403-1411
    • Guardiani, C.1    Cecconi, F.2    Livi, R.3
  • 18
    • 0038392700 scopus 로고    scopus 로고
    • Structure, stability and dynamics of the central domain of cardiac myosin binding protein c (MyBP-C): Implications for multidomain assembly and causes for cardiomyopathy
    • Idowu SM, Gautel M, Perkins SJ, Pfuhl M (2003) Structure, stability and dynamics of the central domain of cardiac myosin binding protein c (MyBP-C): implications for multidomain assembly and causes for cardiomyopathy. J Mol Biol 329:745-761
    • (2003) J Mol Biol , vol.329 , pp. 745-761
    • Idowu, S.M.1    Gautel, M.2    Perkins, S.J.3    Pfuhl, M.4
  • 19
    • 84893482610 scopus 로고
    • Solution for best rotation to relate two sets of vectors
    • Kabsch W (1976) Solution for best rotation to relate two sets of vectors. Acta Crystallogr 32:922-923
    • (1976) Acta Crystallogr , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 20
    • 0029155994 scopus 로고
    • Hydrophobic potential by pairwise surface area sum
    • Kurochkina N, Lee B (1995) Hydrophobic potential by pairwise surface area sum. Protein Eng 8:437-442
    • (1995) Protein Eng , vol.8 , pp. 437-442
    • Kurochkina, N.1    Lee, B.2
  • 21
    • 4644340168 scopus 로고    scopus 로고
    • Optimal combination of theory and experiment for the characterization of the protein folding landscape of S6: How far can a minimalist model go?
    • Matysiak S, Clementi C (2004) Optimal combination of theory and experiment for the characterization of the protein folding landscape of S6: how far can a minimalist model go? J Mol Biol 343:235-248
    • (2004) J Mol Biol , vol.343 , pp. 235-248
    • Matysiak, S.1    Clementi, C.2
  • 22
    • 0036073320 scopus 로고    scopus 로고
    • Crucial stages of protein folding through a solvable model: Predicting target sites for enzyme-inhibiting drugs
    • Micheletti C, Cecconi F, Flammini A, Maritan A (2002) Crucial stages of protein folding through a solvable model: predicting target sites for enzyme-inhibiting drugs. Protein Sci 11:1878-1887
    • (2002) Protein Sci , vol.11 , pp. 1878-1887
    • Micheletti, C.1    Cecconi, F.2    Flammini, A.3    Maritan, A.4
  • 23
    • 0037131207 scopus 로고    scopus 로고
    • Identification of novel interactions between domains of myosin binding protein-c that are modulated by hypertrophic cardiomyopathy missense mutations
    • Moolman-Smook J, Flashman E, de Lange W, Li ZL, Corfield V, Redwood C, Watkins H (2002) Identification of novel interactions between domains of myosin binding protein-c that are modulated by hypertrophic cardiomyopathy missense mutations. Circ Res 91:704-711
    • (2002) Circ Res , vol.91 , pp. 704-711
    • Moolman-Smook, J.1    Flashman, E.2    De Lange, W.3    Li, Z.L.4    Corfield, V.5    Redwood, C.6    Watkins, H.7
  • 25
    • 0037155413 scopus 로고    scopus 로고
    • Structural and energetic heterogeneity in protein folding. I
    • Plotkin SS, Onuchic JN (2002) Structural and energetic heterogeneity in protein folding I. Theory J Chem Phys 116:5263-5283
    • (2002) Theory J Chem Phys , vol.116 , pp. 5263-5283
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 28
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of Barnase and the contribution of different interactions to protein stability
    • Serrano L, Kellis J, Cann P, Matouschek A, Fersht AR (1992) The folding of an enzyme. II. Substructure of Barnase and the contribution of different interactions to protein stability. J Mol Biol 224:783-804
    • (1992) J Mol Biol , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 29
    • 33646931471 scopus 로고    scopus 로고
    • Protein folding thermodynamics and dynamics: Where physics, chemistry and biology meet
    • Shakhnovich EI (2006) Protein folding thermodynamics and dynamics: where physics, chemistry and biology meet. Chem Rev 106:1559-1588
    • (2006) Chem Rev , vol.106 , pp. 1559-1588
    • Shakhnovich, E.I.1
  • 30
    • 33745712768 scopus 로고    scopus 로고
    • Sequence of events in folding mechanism: Beyond the Gō model
    • Sutto L, Tiana G, Broglia RA (2006) Sequence of events in folding mechanism: beyond the Gō model. Protein Sci 15:1638-1652
    • (2006) Protein Sci , vol.15 , pp. 1638-1652
    • Sutto, L.1    Tiana, G.2    Broglia, R.A.3
  • 31
    • 0033972215 scopus 로고    scopus 로고
    • Myosin binding protein C, a potential regulator of cardiac contractility
    • Winegrad S (2000) Myosin binding protein C, a potential regulator of cardiac contractility. Circ Res 86:6-7
    • (2000) Circ Res , vol.86 , pp. 6-7
    • Winegrad, S.1
  • 32
    • 0345827721 scopus 로고    scopus 로고
    • Quantifying the effect of burial of amino acid residues on protein stability
    • Zhou H, Zhou Y (2004) Quantifying the effect of burial of amino acid residues on protein stability. Proteins Struct Func Bioinf 54:315-322
    • (2004) Proteins Struct Func Bioinf , vol.54 , pp. 315-322
    • Zhou, H.1    Zhou, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.