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Volumn 11, Issue 4, 1995, Pages 434-437

Mutations in the cardiac myosin binding protein–C gene on chromosome 11 cause familial hypertrophic cardiomyopathy

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PROTEIN C;

EID: 0028844204     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1295-434     Document Type: Article
Times cited : (481)

References (24)
  • 1
    • 0023130164 scopus 로고
    • Hypertrophic cardiomyopathy: Interrelations of clinical manifestations, pathophysiology, and therapy
    • Maron, B. J., Bonow, R. O., Cannon, R. Û., Leon, M. B. & Epstein, S. E. Hypertrophic cardiomyopathy: interrelations of clinical manifestations, pathophysiology, and therapy. New Engl. J. Med. 316, 780-89 & 844-52 (1987).
    • (1987) New Engl. J. Med , vol.316
    • Maron, B.J.1    Bonow, R.O.2    Cannon, R.Û.3    Leon, M.B.4    Epstein, S.E.5
  • 2
    • 0002811611 scopus 로고
    • Hypertrophic cardiomyopathy
    • 7th edn (eds Scriver, C.R., Beaudet, A.L., Sly, W.S. & Valle, D.) (McGraw-Hill, New YorK
    • McKenna, W. J. & Watkins, H. Hypertrophic cardiomyopathy, in The Metabolic Basis of Inherited Disease. 7th edn (eds Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D.) 4253-4272 (McGraw-Hill, New YorK 1995).
    • (1995) The Metabolic Basis of Inherited Disease , pp. 4253-4272
    • McKenna, W.J.1    Watkins, H.2
  • 3
    • 0025040392 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: A β cardiac myosin heavy chain gene missense mutation
    • Geisterfer-Lowrance, A. A. T. et al. A molecular basis for familial hypertrophic cardiomyopathy: a β cardiac myosin heavy chain gene missense mutation. Cell 62, 999-1006 (1990).
    • (1990) Cell , vol.62 , pp. 999-1006
    • Geisterfer-Lowrance, A.A.T.1
  • 4
    • 0028178083 scopus 로고
    • Mutations in α-tropomyosin and in cardiac troponin T cause hypertrophic cardiomyopathy: A disease of the sarcomere
    • Thierfelder, L. et al. Mutations in α-tropomyosin and in cardiac troponin T cause hypertrophic cardiomyopathy: a disease of the sarcomere. Cell 77, 701-712(1994).
    • (1994) Cell , vol.77 , pp. 701-712
    • Thierfelder, L.1
  • 5
    • 0028902929 scopus 로고
    • The role of mutations in cardiac troponin T and α tropomyosin in familial hypertrophic cardiomyopathy
    • Watkins, H. et al. The role of mutations in cardiac troponin T and α tropomyosin in familial hypertrophic cardiomyopathy. New Engl. J. Med. 332, 1058-1064(1995).
    • (1995) New Engl. J. Med , vol.332 , pp. 1058-1064
    • Watkins, H.1
  • 6
    • 0027161005 scopus 로고
    • Mapping of a novel gene for familial hypertrophic cardiomyopathy to chromosome 11
    • Carrier, L. et al. Mapping of a novel gene for familial hypertrophic cardiomyopathy to chromosome 11. Nature Genet. 4, 311-313 (1993).
    • (1993) Nature Genet , vol.4 , pp. 311-313
    • Carrier, L.1
  • 7
    • 84966173632 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy with Wolff-Parkinson-White syndrome maps to a locus on chromosome 7q3
    • (in the press)
    • MacRae, C. A. et al. Familial hypertrophic cardiomyopathy with Wolff-Parkinson-White syndrome maps to a locus on chromosome 7q3. J. din. Invest, (in the press).
    • J. din. Invest
    • McRae, C.A.1
  • 8
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: A modulator of cardiac contraction?
    • Gautel, M., Zuffardi, O., Freiburg, A. & Labeit, S. Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction? EMBO J. 14, 1952-1960 (1995).
    • (1995) EMBO J , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 9
    • 0027083562 scopus 로고
    • cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86 kDa protein
    • Vaughan, K. T., Weber, F. E. & Fischman, D. A. cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86 kDa protein. Symp. Soc. exp. Biol. 46, 167-177 (1992).
    • (1992) Symp. Soc. exp. Biol , vol.46 , pp. 167-177
    • Vaughan, K.T.1    Weber, F.E.2    Fischman, D.A.3
  • 10
    • 0027407773 scopus 로고
    • Molecular cloning of chicken myosin-binding protein H (MyB) H (86-kDa protein) reveals extensive homology with the MyB-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs
    • Vaughan, K. T., Weber, F. E., Einheber, S. & Fischman, D. A. Molecular cloning of chicken myosin-binding protein H (MyB) H (86-kDa protein) reveals extensive homology with the MyB-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. J. bioi. Chem. 268, 3670-3676(1993).
    • (1993) J. bioi. Chem , vol.268 , pp. 3670-3676
    • Vaughan, K.T.1    Weber, F.E.2    Einheber, S.3    Fischman, D.A.4
  • 12
    • 0028231090 scopus 로고
    • The 1993-94 Genethon human genetic linkage map
    • Gyapay, G. et al. The 1993-94 Genethon human genetic linkage map. Nature Genet. 7, 246-339 (1994).
    • (1994) Nature Genet , vol.7 , pp. 246-339
    • Gyapay, G.1
  • 13
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro, M. B. & Senapathy, P. RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucl. Adds Res. 15, 7155-7174 (1987).
    • (1987) Nucl. Adds Res , vol.15 , pp. 7155-7174
    • Shapiro, M.B.1    Senapathy, P.2
  • 14
    • 0023004932 scopus 로고
    • Pre-mRNA splicing
    • Green, M. R. Pre-mRNA splicing. A Rev. Genet. 20, 671-708 (1986).
    • (1986) A Rev. Genet , vol.20 , pp. 671-708
    • Green, M.R.1
  • 15
    • 0025098474 scopus 로고
    • Exon definition may facilitate splice site selection in RNAs with multiple exons
    • Robberson, B. L, Cote, G. J., & Berget, S. M. Exon definition may facilitate splice site selection in RNAs with multiple exons. Molec. cell. Biol. 10, 84-94 (1990).
    • (1990) Molec. cell. Biol , vol.10 , pp. 84-94
    • Robberson, B.L.1    Cote, G.J.2    Berget, S.M.3
  • 16
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily: Domains for cel I surface recognition
    • Williams, A. F. & Barclay, A. N. The immunoglobulin superfamily: domains for cel I surface recognition. A. Rev. Immun. 6, 381-405 (1988).
    • (1988) A. Rev. Immun , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 17
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal immunoglobulin C2 motif
    • Okagaki, T. et al. The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal immunoglobulin C2 motif. J. Cell Biol. 123, 619-626 (1993).
    • (1993) J. Cell Biol , vol.123 , pp. 619-626
    • Okagaki, T.1
  • 18
    • 0025228775 scopus 로고
    • Differential distribution of subsets of myofibrillar proteins in cardiac nonstrìated and striated myofibril
    • Schultheiis, T. et al. Differential distribution of subsets of myofibrillar proteins in cardiac nonstrìated and striated myofibril. J. Cell Biol. 110, 1159-1172 (1990).
    • (1990) J. Cell Biol , vol.110 , pp. 1159-1172
    • Schultheiis, T.1
  • 19
    • 0019068808 scopus 로고
    • Effect of C-protein on actomyosin ATPase
    • Moos, C. & Feng, l. M. Effect of C-protein on actomyosin ATPase. Biochim. biophys. Acta 632, 141-149 (1980).
    • (1980) Biochim. biophys. Acta , vol.632 , pp. 141-149
    • Moos, C.1    Feng, L.M.2
  • 20
    • 0025727168 scopus 로고
    • Phosphorylation of chick cardiac C-protein by calcium/calmodulin-dependent protein kinase II
    • Schlender, K. & Bean, L. J. Phosphorylation of chick cardiac C-protein by calcium/calmodulin-dependent protein kinase II. J. bioi. Chem. 266, 2811-2817(1991).
    • (1991) J. bioi. Chem , vol.266 , pp. 2811-2817
    • Schlender, K.1    Bean, L.J.2
  • 21
    • 0026776004 scopus 로고
    • Mammalian skeletal muscle C-proteín: Purification from bovine muscle, binding to titin and the characterization of a full-length cDNA
    • Furst, D. O., Vinkemeyer, U. & Weber, K. Mammalian skeletal muscle C-proteín: purification from bovine muscle, binding to titin and the characterization of a full-length cDNA. J. Cell Sci. 102, 769-778 (1992).
    • (1992) J. Cell Sci , vol.102 , pp. 769-778
    • Furst, D.O.1    Vinkemeyer, U.2    Weber, K.3
  • 22
    • 84993895674 scopus 로고
    • Searching candidate genes for mutations: Amplification of sequences from affected individuals; cleavage of RNA-DNA hybrids at mutation sites using RNase A
    • (eds Dracopoli, N. et al.), (Greene Publishing Associates and John Wiley and Sons
    • Watkins, H. Searching candidate genes for mutations: amplification of sequences from affected individuals; cleavage of RNA-DNA hybrids at mutation sites using RNase A. in Current Protocols in Human Genetics. (eds Dracopoli, N. et al.) 7. 1-7. 2 (Greene Publishing Associates and John Wiley and Sons, 1994).
    • (1994) Current Protocols in Human Genetics
    • Watkins, H.1
  • 24
    • 0027168759 scopus 로고
    • Complete sequence of human fast-type and slow-type muscle myosin-binding protein C (myBP-C)
    • Weber, F. E., Vaughan K. T., Reinach, FC. & Fischmann, D. E. Complete sequence of human fast-type and slow-type muscle myosin-binding protein C (myBP-C). Eur. J. Biochem. 216, 661-669 (1993).
    • (1993) Eur. J. Biochem , vol.216 , pp. 661-669
    • Weber, F.E.1    Vaughan, K.T.2    Reinach, F.C.3    Fischmann, D.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.