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Volumn 79, Issue 4, 2011, Pages 1240-1250

Is there nascent structure in the intrinsically disordered region of troponin I?

Author keywords

Molecular dynamics; Muscle regulation; NMR; NMR relaxation; Protein dynamics

Indexed keywords

TROPONIN I;

EID: 79952462595     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22959     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 0042624696 scopus 로고    scopus 로고
    • Pulling the calcium trigger
    • Sykes BD. Pulling the calcium trigger. Nat Struct Biol 2003; 10: 588-589.
    • (2003) Nat Struct Biol , vol.10 , pp. 588-589
    • Sykes, B.1
  • 2
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M. Regulation of contraction in striated muscle. Physiol Rev 2000; 80: 853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.1    Homsher, E.2    Regnier, M.3
  • 3
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman LS. Thin filament-mediated regulation of cardiac contraction. Annu Rev Physiol 1996; 58: 447-481.
    • (1996) Annu Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.1
  • 4
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah CS, Reinach FC. The troponin complex and regulation of muscle contraction. FASEB J 1995; 9: 755-767.
    • (1995) FASEB J , vol.9 , pp. 755-767
    • Farah, C.1    Reinach, F.2
  • 5
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the fly-casting mechanism
    • Shoemaker BA, Portman JJ, Wolynes PG. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci USA 2000; 97: 8868-8873.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.1    Portman, J.2    Wolynes, P.3
  • 6
    • 33646203967 scopus 로고    scopus 로고
    • Dynamics of the C-terminal region of TnI in the troponin complex in solution
    • Blumenschein TM, Stone DB, Fletterick RJ, Mendelson RA, Sykes BD. Dynamics of the C-terminal region of TnI in the troponin complex in solution. Biophys J 2006; 90: 2436-2444.
    • (2006) Biophys J , vol.90 , pp. 2436-2444
    • Blumenschein, T.1    Stone, D.2    Fletterick, R.3    Mendelson, R.4    Sykes, B.5
  • 8
    • 4544291412 scopus 로고    scopus 로고
    • Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene
    • Gomes AV, Potter JD. Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene. Mol Cell Biochem 2004; 263: 99-114.
    • (2004) Mol Cell Biochem , vol.263 , pp. 99-114
    • Gomes, A.1    Potter, J.2
  • 9
    • 75649123827 scopus 로고    scopus 로고
    • Defective dynamic properties of human cardiac troponin mutations
    • Lassalle MW. Defective dynamic properties of human cardiac troponin mutations. Biosci Biotechnol Biochem 2010; 74: 82-91.
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 82-91
    • Lassalle, M.1
  • 12
    • 10044268379 scopus 로고    scopus 로고
    • Solution structure of the chicken skeletal muscle troponin complex via small-angle neutron and X-ray scattering
    • King WA, Stone DB, Timmins PA, Narayanan T, von Brasch AA, Mendelson RA, Curmi PM. Solution structure of the chicken skeletal muscle troponin complex via small-angle neutron and X-ray scattering. J Mol Biol 2005; 345: 797-815.
    • (2005) J Mol Biol , vol.345 , pp. 797-815
    • King, W.1    Stone, D.2    Timmins, P.3    Narayanan, T.4    von Brasch, A.5    Mendelson, R.6    Curmi, P.7
  • 14
  • 15
    • 13444253928 scopus 로고    scopus 로고
    • Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras
    • Tiroli AO, Tasic L, Oliveira CL, Bloch CJ, Torriani I, Farah CS, Ramos CH. Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras. FEBS J 2005; 272: 779-790.
    • (2005) FEBS J , vol.272 , pp. 779-790
    • Tiroli, A.1    Tasic, L.2    Oliveira, C.3    Bloch, C.4    Torriani, I.5    Farah, C.6    Ramos, C.7
  • 16
  • 17
  • 19
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993; 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.2
  • 20
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • Im W, Beglov D, Roux B. Continuum solvation model: computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation. Comput Phys Commun 1998; 111: 59-75.
    • (1998) Comput Phys Commun , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 22
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell AD, Feig M, Brooks CL. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comput Chem 2004; 25: 1400-1415.
    • (2004) J Comput Chem , vol.25 , pp. 1400-1415
    • Mackerell, A.1    Feig, M.2    Brooks, C.3
  • 23
    • 0141956090 scopus 로고    scopus 로고
    • Generalized born model with a simple smoothing function
    • Im WP, Lee MS, Brooks CL. Generalized born model with a simple smoothing function. J Comput Chem 2003; 24: 1691-1702.
    • (2003) J Comput Chem , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.2    Brooks, C.3
  • 24
    • 0003943480 scopus 로고
    • The principles of nuclear magnetism
    • Oxford: Clarendon Press.
    • Abragam A. The principles of nuclear magnetism. Oxford: Clarendon Press; 1961.
    • (1961)
    • Abragam, A.1
  • 25
    • 20444436795 scopus 로고    scopus 로고
    • Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex
    • Blumenschein TM, Stone DB, Fletterick RJ, Mendelson RA, Sykes BD. Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex. J Biol Chem 2005; 280: 21924-21932.
    • (2005) J Biol Chem , vol.280 , pp. 21924-21932
    • Blumenschein, T.1    Stone, D.2    Fletterick, R.3    Mendelson, R.4    Sykes, B.5
  • 26
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart DS, Sykes BD. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 1994; 4: 171-180.
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.1    Sykes, B.2
  • 27
    • 38149011312 scopus 로고    scopus 로고
    • 15N magnetic relaxation study of backbone dynamics of the ribosome-associated cold shock response protein Yfia of Escherichia coli
    • Zhukov I, Bayer P, Scholermann B, Ejchart A. 15N magnetic relaxation study of backbone dynamics of the ribosome-associated cold shock response protein Yfia of Escherichia coli. Acta Biochim Pol 2007; 54: 769-775.
    • (2007) Acta Biochim Pol , vol.54 , pp. 769-775
    • Zhukov, I.1    Bayer, P.2    Scholermann, B.3    Ejchart, A.4
  • 28
    • 2142652103 scopus 로고    scopus 로고
    • Human programmed cell death 5 protein has a helical-core and two dissociated structural regions
    • Liu D, Feng Y, Cheng Y, Wang J. Human programmed cell death 5 protein has a helical-core and two dissociated structural regions. Biochem Biophys Res Commun 2004; 318: 391-396.
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 391-396
    • Liu, D.1    Feng, Y.2    Cheng, Y.3    Wang, J.4
  • 29
  • 30
    • 0344490343 scopus 로고    scopus 로고
    • NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers
    • Mercier P, Ferguson RE, Irving M, Corrie JET, Trentham DR, Sykes BD. NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers. Biochemistry 2003; 42: 4333-4348.
    • (2003) Biochemistry , vol.42 , pp. 4333-4348
    • Mercier, P.1    Ferguson, R.2    Irving, M.3    Corrie, J.4    Trentham, D.5    Sykes, B.6
  • 31
    • 0033614841 scopus 로고    scopus 로고
    • Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C
    • Li MX, Spyracopoulos L, Sykes BD. Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C. Biochemistry 1999; 38: 8289-8298.
    • (1999) Biochemistry , vol.38 , pp. 8289-8298
    • Li, M.1    Spyracopoulos, L.2    Sykes, B.3
  • 34
    • 18844478967 scopus 로고    scopus 로고
    • Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity
    • Gagné SM, Tsuda S, Spyracopoulos L, Kay LE, Sykes BD. Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity. J Mol Biol 1998; 278: 667-686.
    • (1998) J Mol Biol , vol.278 , pp. 667-686
    • Gagné, S.1    Tsuda, S.2    Spyracopoulos, L.3    Kay, L.4    Sykes, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.