메뉴 건너뛰기




Volumn 94, Issue 4, 2008, Pages 1403-1411

Stability and kinetic properties of C5-domain from myosin binding protein candits mutants

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; MYOSIN BINDING PROTEIN C; MYOSIN-BINDING PROTEIN C; UNCLASSIFIED DRUG;

EID: 38949163021     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.106625     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 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
  • 5
    • 2642572455 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C: Its role in physiology and disease
    • Flashman, E., C. Redwood, J. Moolman-Smook, and H. Watkins. 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
  • 6
    • 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., E. Flashman, W. de Lange, Z. L. Li, V. Corfield, C. Redwood, and H. Watkins. 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
  • 7
    • 0033972217 scopus 로고    scopus 로고
    • Myosin binding protein C, a phosphorylation- dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2
    • Kunst, G., K. R. Kress, M. Gruen, D. Uttenweiler, M. Gautel, and R. H. A. Fink. 2000. Myosin binding protein C, a phosphorylation- dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2. Circ. Res. 86:51-58.
    • (2000) Circ. Res , vol.86 , pp. 51-58
    • Kunst, G.1    Kress, K.R.2    Gruen, M.3    Uttenweiler, D.4    Gautel, M.5    Fink, R.H.A.6
  • 8
    • 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, S. M., M. Gautel, S. J. Perkins, and M. Pfuhl. 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
  • 9
    • 0021713707 scopus 로고
    • 2+-calmodulin-dependent protein kinases
    • 2+-calmodulin-dependent protein kinases. J. Biol. Chem. 259: 15587-15596.
    • (1984) J. Biol. Chem , vol.259 , pp. 15587-15596
    • Hartzell, H.C.1    Glass, D.B.2
  • 12
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphospha- tase suggests the importance of topology and contact order in protein folding
    • Chiti, F., N. Taddei, P. M. White, M. Bucciantini, F. Magherini, M. Stefani, and C. M. Dobson. 1999. Mutational analysis of acylphospha- tase 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
  • 13
    • 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., H. Nymeyer, and J. N. Onuchic. 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
  • 14
    • 0035371215 scopus 로고    scopus 로고
    • The structural basis of antiviral drug resistance and role of folding pathways in HIV-1 protease
    • Cecconi, F., C. Micheletti, P. Carloni, and A. Maritan. 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
  • 15
    • 0036073320 scopus 로고    scopus 로고
    • Crucial stages of protein folding through a solvable model: Predicting target sites for enzyme-inhibiting drugs
    • Micheletti, C., F. Cecconi, A. Flammini, and A. Maritan. 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
  • 16
    • 0034319711 scopus 로고    scopus 로고
    • Sequencing of folding events in Go-type proteins
    • Hoang, T. X., and M. Cieplak. 2000. Sequencing of folding events in Go-type proteins. J. Chem. Phys. 113:8319-8328.
    • (2000) J. Chem. Phys , vol.113 , pp. 8319-8328
    • Hoang, T.X.1    Cieplak, M.2
  • 17
    • 33745714381 scopus 로고    scopus 로고
    • Testing simplified protein models of the hPin1 WW domain
    • Cecconi, F., C. Guardiani, and R. Livi. 2006. Testing simplified protein models of the hPin1 WW domain. Biophys. J. 91:694-704.
    • (2006) Biophys. J , vol.91 , pp. 694-704
    • Cecconi, F.1    Guardiani, C.2    Livi, R.3
  • 18
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway
    • Clarke, J., E. Cota, S. B. Fowler, and S. Hamill. 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
  • 19
    • 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., and C. Clementi. 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
  • 20
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of Barnase and the contribution of different interactions to protein stability
    • Serrano, L., J. Kellis, P. Cann, A. Matouschek, and A. R. Fersht. 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
  • 21
    • 0029155994 scopus 로고
    • Hydrophobic potential by pairwise surface area sum
    • Kurochkina, N., and B. Lee. 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
  • 22
    • 0032906553 scopus 로고    scopus 로고
    • Monte Carlo simulations of β-hairpin folding at constant temperature
    • Sung, S. 1999. Monte Carlo simulations of β-hairpin folding at constant temperature. Biophys. J. 76:164-175.
    • (1999) Biophys. J , vol.76 , pp. 164-175
    • Sung, S.1
  • 23
    • 0345827721 scopus 로고    scopus 로고
    • Quantifying the effect of burial of amino acid residues on protein stability
    • Zhou, H., and Y. Zhou. 2004. 2004. Quantifying the effect of burial of amino acid residues on protein stability. Proteins Struct. Funct. Bioinf. 54:315-322.
    • (2004) Proteins Struct. Funct. Bioinf , vol.54 , pp. 315-322
    • Zhou, H.1    Zhou, Y.2
  • 24
    • 33845377127 scopus 로고
    • Estimation of effective inter- residue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S., and R. L. Jernigan. 1985. Estimation of effective inter- residue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules. 18:534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 25
    • 34547709547 scopus 로고    scopus 로고
    • Cieplak, M., and J. I. Sulkowska. 2005. Thermal unfolding of proteins. J. Chem. Phys. 123:194908-1-4.
    • Cieplak, M., and J. I. Sulkowska. 2005. Thermal unfolding of proteins. J. Chem. Phys. 123:194908-1-4.
  • 26
    • 0011804246 scopus 로고
    • Molecular dynamics studies of protein and peptide folding and unfolding
    • Prediction. K. M. Merz Jr. and S. M. Le Grand, editors. Birkhauser, Boston
    • Caflisch, A., and M. Karplus. 1994. Molecular dynamics studies of protein and peptide folding and unfolding. In The Protein Folding Problem and Tertiary Structure Prediction. K. M. Merz Jr. and S. M. Le Grand, editors. Birkhauser, Boston.
    • (1994) The Protein Folding Problem and Tertiary Structure
    • Caflisch, A.1    Karplus, M.2
  • 27
    • 0030775114 scopus 로고    scopus 로고
    • Can protein unfolding simulate protein folding?
    • Finkelstein, A. V. 1997. Can protein unfolding simulate protein folding? Protein Eng. 10:843-845.
    • (1997) Protein Eng , vol.10 , pp. 843-845
    • Finkelstein, A.V.1
  • 28
    • 0033578828 scopus 로고    scopus 로고
    • Is protein unfolding the reverse of protein folding? A lattice simulation analysis
    • Dinner, A. R., and M. Karplus. 1999. Is protein unfolding the reverse of protein folding? A lattice simulation analysis. J. Mol. Biol. 292:403419.
    • (1999) J. Mol. Biol , vol.292 , pp. 403419
    • Dinner, A.R.1    Karplus, M.2
  • 29
    • 2942705984 scopus 로고    scopus 로고
    • Gatekeepers in the ribosomal protein S6: Thermodynamics, kinetics, and folding pathways revealed by a minimalist protein model
    • Stoycheva, A. D., C. L. Brooks III, and J. N. Onuchic. 2004. Gatekeepers in the ribosomal protein S6: thermodynamics, kinetics, and folding pathways revealed by a minimalist protein model. J. Mol. Biol. 340:571-585.
    • (2004) J. Mol. Biol , vol.340 , pp. 571-585
    • Stoycheva, A.D.1    Brooks III, C.L.2    Onuchic, J.N.3
  • 31
    • 33745712768 scopus 로고    scopus 로고
    • Sequence of events in folding mechanism: Beyond the Gō model
    • Sutto, L., G. Tiana, and R. A. Broglia. 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
  • 32
    • 39749148315 scopus 로고    scopus 로고
    • Computational analysis of folding and mutation properties of C5 domain of myosin binding protein C
    • doi 10.1002/prot.21621
    • Guardiani, C., F. Cecconi, and R. Livi. 2007. Computational analysis of folding and mutation properties of C5 domain of myosin binding protein C. Proteins Struct. Funct. Bioinf. doi 10.1002/prot.21621.
    • (2007) Proteins Struct. Funct. Bioinf
    • Guardiani, C.1    Cecconi, F.2    Livi, R.3
  • 34
    • 0034669882 scopus 로고    scopus 로고
    • Why are ''natively unfolded'' proteins unstructured under physiologic conditions?
    • Uversky, V. N., J. R. Gillespie, and A. L. Fink. 2000. Why are ''natively unfolded'' proteins unstructured under physiologic conditions? Proteins Struct. Funct. Genet. 41:415-427.
    • (2000) Proteins Struct. Funct. Genet , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.