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Volumn 391, Issue 1, 2010, Pages 352-356

A mutation in the β-myosin rod associated with hypertrophic cardiomyopathy has an unexpected molecular phenotype

Author keywords

Cardiac hypertrophy; Hypertrophic cardiomyopathy; Mutation

Indexed keywords

MYOSIN;

EID: 72949109318     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.11.062     Document Type: Article
Times cited : (17)

References (14)
  • 2
    • 0037070514 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: a systematic review
    • Maron B.J. Hypertrophic cardiomyopathy: a systematic review. JAMA 287 (2002) 1308-1320
    • (2002) JAMA , vol.287 , pp. 1308-1320
    • Maron, B.J.1
  • 3
    • 0029083650 scopus 로고
    • Prevalence of hypertrophic cardiomyopathy in a general population of young adults. Echocardiographic analysis of 4111 subjects in the CARDIA study. Coronary artery risk development in (Young) adults
    • Maron B.J., Gardin J.M., Flack J.M., Gidding S.S., Kurosaki T.T., and Bild D.E. Prevalence of hypertrophic cardiomyopathy in a general population of young adults. Echocardiographic analysis of 4111 subjects in the CARDIA study. Coronary artery risk development in (Young) adults. Circulation 92 (1995) 785-789
    • (1995) Circulation , vol.92 , pp. 785-789
    • Maron, B.J.1    Gardin, J.M.2    Flack, J.M.3    Gidding, S.S.4    Kurosaki, T.T.5    Bild, D.E.6
  • 5
    • 0032837587 scopus 로고    scopus 로고
    • The inheritance of hypertrophic cardiomyopathy
    • Burch M., and Blair E. The inheritance of hypertrophic cardiomyopathy. Pediatr. Cardiol. 20 (1999) 313-316
    • (1999) Pediatr. Cardiol. , vol.20 , pp. 313-316
    • Burch, M.1    Blair, E.2
  • 6
    • 0035940383 scopus 로고    scopus 로고
    • New concepts in hypertrophic cardiomyopathies, part I
    • Roberts R., and Sigwart U. New concepts in hypertrophic cardiomyopathies, part I. Circulation 104 (2001) 2113-2116
    • (2001) Circulation , vol.104 , pp. 2113-2116
    • Roberts, R.1    Sigwart, U.2
  • 7
    • 44849134159 scopus 로고    scopus 로고
    • Bioinformatics assessment of beta-myosin mutations reveals myosin's high sensitivity to mutations
    • Buvoli M., Hamady M., Leinwand L.A., and Knight R. Bioinformatics assessment of beta-myosin mutations reveals myosin's high sensitivity to mutations. Trends Cardiovasc. Med. 18 (2008) 141-149
    • (2008) Trends Cardiovasc. Med. , vol.18 , pp. 141-149
    • Buvoli, M.1    Hamady, M.2    Leinwand, L.A.3    Knight, R.4
  • 8
    • 77951623814 scopus 로고    scopus 로고
    • Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes
    • 10.1016/j.yjmcc.2009.10.011
    • Armel T.Z., and Leinwand L.A. Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes. J. Mol. Cell. Cardiol. (2009) 10.1016/j.yjmcc.2009.10.011
    • (2009) J. Mol. Cell. Cardiol.
    • Armel, T.Z.1    Leinwand, L.A.2
  • 9
    • 65549098089 scopus 로고    scopus 로고
    • Mutations in the beta-myosin rod cause myosin storage myopathy via multiple mechanisms
    • Armel T.Z., and Leinwand L.A. Mutations in the beta-myosin rod cause myosin storage myopathy via multiple mechanisms. Proc. Natl. Acad. Sci. USA 106 (2009) 6291-6296
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6291-6296
    • Armel, T.Z.1    Leinwand, L.A.2
  • 10
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield N.J. Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 1 (2006) 2876-2890
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 11
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield N.J. Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. 1 (2006) 2527-2535
    • (2006) Nat. Protoc. , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 12
    • 0031897698 scopus 로고    scopus 로고
    • Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band
    • Obermann W.M., van der Ven P.F., Steiner F., Weber K., and Furst D.O. Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band. Mol. Biol. Cell 9 (1998) 829-840
    • (1998) Mol. Biol. Cell , vol.9 , pp. 829-840
    • Obermann, W.M.1    van der Ven, P.F.2    Steiner, F.3    Weber, K.4    Furst, D.O.5
  • 13
    • 33846277638 scopus 로고    scopus 로고
    • Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod
    • Flashman E., Watkins H., and Redwood C. Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod. Biochem. J. 401 (2007) 97-102
    • (2007) Biochem. J. , vol.401 , pp. 97-102
    • Flashman, E.1    Watkins, H.2    Redwood, C.3
  • 14
    • 0036713653 scopus 로고    scopus 로고
    • The C-terminal IgI domains of myosin-binding proteins C and H (MyBP-C and MyBP-H) are both necessary and sufficient for the intracellular crosslinking of sarcomeric myosin in transfected non-muscle cells
    • Welikson R.E., and Fischman D.A. The C-terminal IgI domains of myosin-binding proteins C and H (MyBP-C and MyBP-H) are both necessary and sufficient for the intracellular crosslinking of sarcomeric myosin in transfected non-muscle cells. J. Cell Sci. 115 (2002) 3517-3526
    • (2002) J. Cell Sci. , vol.115 , pp. 3517-3526
    • Welikson, R.E.1    Fischman, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.