메뉴 건너뛰기




Volumn 290, Issue 1, 1999, Pages 61-75

Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: Implications for functional diversity

Author keywords

Human; Isoform; Myosin; Sarcomeric; Sequences

Indexed keywords

MYOSIN HEAVY CHAIN;

EID: 0033516510     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2865     Document Type: Article
Times cited : (197)

References (88)
  • 1
    • 0345139255 scopus 로고    scopus 로고
    • Albert Einstein College of Medicine
    • Acakpo-Satchivi L. J. PhD thesis. 1997;Albert Einstein College of Medicine.
    • (1997) PhD Thesis
    • Acakpo-Satchivi, L.J.1
  • 4
    • 0029956888 scopus 로고    scopus 로고
    • Spatial and temporal patterns of myosin heavy chain expression in developing rat extraocular muscle
    • Brueckner J. K., Itkis O., Porter J. D. Spatial and temporal patterns of myosin heavy chain expression in developing rat extraocular muscle. J. Muscle Res. Cell Motil. 17:1996;297-312.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 297-312
    • Brueckner, J.K.1    Itkis, O.2    Porter, J.D.3
  • 5
    • 0023926813 scopus 로고
    • Adult human masseter muscle fibers express myosin isozymes characteristic of development
    • Butler-Browne G. S., Eriksson P. O., Laurent C., Thornell L. E. Adult human masseter muscle fibers express myosin isozymes characteristic of development. Muscle Nerve. 11:1988;610-620.
    • (1988) Muscle Nerve , vol.11 , pp. 610-620
    • Butler-Browne, G.S.1    Eriksson, P.O.2    Laurent, C.3    Thornell, L.E.4
  • 6
    • 0024461342 scopus 로고
    • Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain
    • Chaussepied P. Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain. Biochemistry. 28:1989;9123-9128.
    • (1989) Biochemistry , vol.28 , pp. 9123-9128
    • Chaussepied, P.1
  • 8
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick F. H. C. The packing of α-helices: simple coiled-coils. Acta Crystallog. 6:1953;689-697.
    • (1953) Acta Crystallog. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 9
    • 0022481699 scopus 로고
    • Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. Persistence of neonatal-type isoforms in the murine muscle
    • d'Albis A., Janmot C., Bechet J. J. Comparison of myosins from the masseter muscle of adult rat, mouse and guinea-pig. Persistence of neonatal-type isoforms in the murine muscle. Eur. J. Biochem. 156:1986;291-296.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 291-296
    • D'Albis, A.1    Janmot, C.2    Bechet, J.J.3
  • 10
    • 0027299224 scopus 로고
    • Rabbit masseter expresses the cardiac alpha myosin heavy chain gene. Evidence from mRNA sequence analysis
    • d'Albis A., Anger M., Lompre A. M. Rabbit masseter expresses the cardiac alpha myosin heavy chain gene. Evidence from mRNA sequence analysis. FEBS Letters. 324:1993;178-180.
    • (1993) FEBS Letters , vol.324 , pp. 178-180
    • D'Albis, A.1    Anger, M.2    Lompre, A.M.3
  • 11
    • 0026093225 scopus 로고
    • Antibody directed against the 142-148 sequence of the myosin heavy chain interferes with myosin-actin interaction
    • Dan-Goor M., Muhlrad A. Antibody directed against the 142-148 sequence of the myosin heavy chain interferes with myosin-actin interaction. Biochemistry. 30:1991;400-405.
    • (1991) Biochemistry , vol.30 , pp. 400-405
    • Dan-Goor, M.1    Muhlrad, A.2
  • 12
    • 0027496356 scopus 로고
    • Thick filament substructures in Caenorhabditis elegans: Evidence for two populations of paramyosin
    • Deitiker P. R., Epstein H. F. Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin. J. Cell Biol. 123:1993;303-311.
    • (1993) J. Cell Biol. , vol.123 , pp. 303-311
    • Deitiker, P.R.1    Epstein, H.F.2
  • 13
    • 0006844340 scopus 로고    scopus 로고
    • Small segmental rearrangements in the myosin head can explain force generation in muscle
    • Diaz B. F., Bordas J., Lowy J., Svensson A. Small segmental rearrangements in the myosin head can explain force generation in muscle. Biophys. J. 71:1996;576-589.
    • (1996) Biophys. J. , vol.71 , pp. 576-589
    • Diaz, B.F.1    Bordas, J.2    Lowy, J.3    Svensson, A.4
  • 14
  • 15
    • 0021964531 scopus 로고
    • Myosin and paramyosin are organized about a newly identified core structure
    • Epstein H. F., Miller D. M., Ortiz I., Berliner G. C. Myosin and paramyosin are organized about a newly identified core structure. J. Cell Biol. 100:1985;904-915.
    • (1985) J. Cell Biol. , vol.100 , pp. 904-915
    • Epstein, H.F.1    Miller, D.M.2    Ortiz, I.3    Berliner, G.C.4
  • 16
    • 0024513698 scopus 로고
    • Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain
    • Feghali R., Leinwand L. A. Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain. J. Cell Biol. 108:1989;1791-1797.
    • (1989) J. Cell Biol. , vol.108 , pp. 1791-1797
    • Feghali, R.1    Leinwand, L.A.2
  • 17
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch M., Geeves M. A., Manstein D. J. Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry. 37:1998;6317-6326.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 18
    • 0028250631 scopus 로고
    • Molecular evolution of the myosin superfamily: Application of phylogenetic techniques to cell biological questions
    • Goodson H. V. Molecular evolution of the myosin superfamily: application of phylogenetic techniques to cell biological questions. Soc. Gen. Physiol. Ser. 49:1994;141-157.
    • (1994) Soc. Gen. Physiol. Ser. , vol.49 , pp. 141-157
    • Goodson, H.V.1
  • 19
    • 0027508927 scopus 로고
    • Molecular evolution of the myosin family: Relationships derived from comparisons of amino acid sequences
    • Goodson H. V., Spudich J. A. Molecular evolution of the myosin family: relationships derived from comparisons of amino acid sequences. Proc. Natl Acad. Sci. USA. 90:1993;659-663.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 659-663
    • Goodson, H.V.1    Spudich, J.A.2
  • 20
    • 0025822785 scopus 로고
    • Isolation and characterization of the mouse cardiac myosin heavy chain genes
    • Gulick J., Subramaniam A., Neumann J., Robbins J. Isolation and characterization of the mouse cardiac myosin heavy chain genes. J. Biol. Chem. 266:1991;9180-9185.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9180-9185
    • Gulick, J.1    Subramaniam, A.2    Neumann, J.3    Robbins, J.4
  • 21
    • 0029911120 scopus 로고    scopus 로고
    • Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly inCaenorhabditis elegans
    • Hoppe P. E., Waterston R. H. Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly inCaenorhabditis elegans. J. Cell Biol. 135:1996;371-382.
    • (1996) J. Cell Biol. , vol.135 , pp. 371-382
    • Hoppe, P.E.1    Waterston, R.H.2
  • 22
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura M., Clore G. M., Gronenborn A. M., Zhu G., Klee C. B., Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science. 256:1992;632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 23
    • 0024974671 scopus 로고
    • Paramyosin gene (unc-15) of Caenorhabditis elegans. Molecular cloning, nucleotide sequence and models for thick filament structure
    • Kagawa H., Gengyo K., McLachlan A. D., Brenner S., Karn J. Paramyosin gene (unc-15) of Caenorhabditis elegans. Molecular cloning, nucleotide sequence and models for thick filament structure. J. Mol. Biol. 207:1989;311-333.
    • (1989) J. Mol. Biol. , vol.207 , pp. 311-333
    • Kagawa, H.1    Gengyo, K.2    McLachlan, A.D.3    Brenner, S.4    Karn, J.5
  • 24
    • 0024383686 scopus 로고
    • Expression and DNA sequence analysis of a human embryonic skeletal muscle myosin heavy chain gene
    • Karsch-Mizrachi I., Travis M., Blau H., Leinwand L. A. Expression and DNA sequence analysis of a human embryonic skeletal muscle myosin heavy chain gene. Nucl. Acids Res. 17:1989;6167-6179.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 6167-6179
    • Karsch-Mizrachi, I.1    Travis, M.2    Blau, H.3    Leinwand, L.A.4
  • 25
    • 0025327985 scopus 로고
    • Generation of a full-length human perinatal myosin heavy-chain-encoding cDNA
    • Karsch-Mizrachi I., Feghali R., Shows T. B., Leinwand L. A. Generation of a full-length human perinatal myosin heavy-chain-encoding cDNA. Gene. 89:1990;289-294.
    • (1990) Gene , vol.89 , pp. 289-294
    • Karsch-Mizrachi, I.1    Feghali, R.2    Shows, T.B.3    Leinwand, L.A.4
  • 26
    • 0028964572 scopus 로고
    • Characterization of myosin II isoforms containing insertions of amino acids in the flexible loop near the ATP-binding pocket
    • Kelley C. A., Adelstein R. S. Characterization of myosin II isoforms containing insertions of amino acids in the flexible loop near the ATP-binding pocket. Biophys. J. 68:1995;225S.
    • (1995) Biophys. J. , vol.68
    • Kelley, C.A.1    Adelstein, R.S.2
  • 27
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley C. A., Takahashi M., Yu J. H., Adelstein R. S. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J. Biol. Chem. 268:1993;12848-12854.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 28
    • 0029837673 scopus 로고    scopus 로고
    • The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition
    • Komiyama M., Soldati T., von Arx P., Perriard J. C. The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition. J. Cell Sci. 109:1996;2089-2099.
    • (1996) J. Cell Sci. , vol.109 , pp. 2089-2099
    • Komiyama, M.1    Soldati, T.2    Von Arx, P.3    Perriard, J.C.4
  • 29
    • 0023645992 scopus 로고
    • Structural and transcriptional analysis of a chicken myosin heavy chain gene subset
    • Kropp K. E., Gulick J., Robbins J. Structural and transcriptional analysis of a chicken myosin heavy chain gene subset. J. Biol. Chem. 262:1987;16536-16545.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16536-16545
    • Kropp, K.E.1    Gulick, J.2    Robbins, J.3
  • 30
    • 0020601766 scopus 로고
    • Multigene family for sarcomeric myosin heavy chain in mouse and human DNA: Localization on a single chromosome
    • Leinwand L. A., Fournier R. E., Nadal-Ginard B., Shows T. B. Multigene family for sarcomeric myosin heavy chain in mouse and human DNA: localization on a single chromosome. Science. 221:1983;766-769.
    • (1983) Science , vol.221 , pp. 766-769
    • Leinwand, L.A.1    Fournier, R.E.2    Nadal-Ginard, B.3    Shows, T.B.4
  • 31
    • 0029757994 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments
    • Levine R. J., Kensler R. W., Yang Z., Stull J. T., Sweeney H. L. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys. J. 71:1996;898-907.
    • (1996) Biophys. J. , vol.71 , pp. 898-907
    • Levine, R.J.1    Kensler, R.W.2    Yang, Z.3    Stull, J.T.4    Sweeney, H.L.5
  • 32
    • 0003421005 scopus 로고    scopus 로고
    • Sunderland: Sinauer Associates, Inc. p. 179-180
    • Li W.-H. Molecular Evolution. 1997;Sinauer Associates, Inc. Sunderland. p. 179-180.
    • (1997) Molecular Evolution
    • Li, W.-H.1
  • 33
    • 0027426228 scopus 로고
    • Skeletal muscle myosin light chains are essential for physiological speeds of shortening
    • Lowey S., Waller G. S., Trybus K. M. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature. 365:1993;454-456.
    • (1993) Nature , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 34
    • 0029091166 scopus 로고
    • Expression of extraocular myosin heavy chain in rabbit laryngeal muscle
    • Lucas C. A., Rughani A., Hoh J. F. Expression of extraocular myosin heavy chain in rabbit laryngeal muscle. J. Muscle Res. Cell Motil. 16:1995;368-378.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 368-378
    • Lucas, C.A.1    Rughani, A.2    Hoh, J.F.3
  • 35
    • 0021207310 scopus 로고
    • Cardiac alpha- And beta-myosin heavy chain genes are organized in tandem
    • Mahdavi V., Chambers A. P., Nadal-Ginard B. Cardiac alpha- and beta-myosin heavy chain genes are organized in tandem. Proc. Natl Acad. Sci. USA. 81:1984;2626-2630.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2626-2630
    • Mahdavi, V.1    Chambers, A.P.2    Nadal-Ginard, B.3
  • 36
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan A. D., Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature. 299:1982;226-231.
    • (1982) Nature , vol.299 , pp. 226-231
    • McLachlan, A.D.1    Karn, J.2
  • 37
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • McLachlan A. D., Karn J. Periodic features in the amino acid sequence of nematode myosin rod. J. Mol. Biol. 164:1983;605-626.
    • (1983) J. Mol. Biol. , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 38
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador W. E., Means A. R., Quiocho F. A. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science. 262:1993;1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 39
    • 0027439382 scopus 로고
    • The evolutionary relationship of avian and mammalian myosin heavy-chain genes
    • Moore L. A., Tidyman W. E., Arrizubieta M. J., Bandman E. The evolutionary relationship of avian and mammalian myosin heavy-chain genes. J. Mol. Evol. 36:1993;21-30.
    • (1993) J. Mol. Evol. , vol.36 , pp. 21-30
    • Moore, L.A.1    Tidyman, W.E.2    Arrizubieta, M.J.3    Bandman, E.4
  • 41
    • 0032510769 scopus 로고    scopus 로고
    • Dictyostelium myosin 25-50 K loop substitutions specifically affect ADP release rates
    • Murphy C. T., Spudich J. A. Dictyostelium myosin 25-50 K loop substitutions specifically affect ADP release rates. Biochemistry. 37:1998;6738-6744.
    • (1998) Biochemistry , vol.37 , pp. 6738-6744
    • Murphy, C.T.1    Spudich, J.A.2
  • 44
    • 0026589213 scopus 로고
    • Structural and developmental analysis of two linked myosin heavy chain genes
    • Parker-Thornburg J., Bauer B., Palermo J., Robbins J. Structural and developmental analysis of two linked myosin heavy chain genes. Dev. Biol. 150:1992;99-107.
    • (1992) Dev. Biol. , vol.150 , pp. 99-107
    • Parker-Thornburg, J.1    Bauer, B.2    Palermo, J.3    Robbins, J.4
  • 45
    • 0029898752 scopus 로고    scopus 로고
    • Cold-sensitive mutations of Dictyostelium myosin heavy chain highlight functional domains of the myosin motor
    • Patterson B., Spudich J. A. Cold-sensitive mutations of Dictyostelium myosin heavy chain highlight functional domains of the myosin motor. Genetics. 143:1996;801-810.
    • (1996) Genetics , vol.143 , pp. 801-810
    • Patterson, B.1    Spudich, J.A.2
  • 46
    • 0029909606 scopus 로고    scopus 로고
    • Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins
    • Perreault-Micale C. L., Kalabokis V. N., Nyitray L., Szent-Gyorgyi A. G. Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins. J. Muscle Res. Cell Motil. 17:1996;543-553.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 543-553
    • Perreault-Micale, C.L.1    Kalabokis, V.N.2    Nyitray, L.3    Szent-Gyorgyi, A.G.4
  • 48
    • 0031023872 scopus 로고    scopus 로고
    • Mammalian skeletal muscle fiber type transitions
    • Pette D., Staron R. S. Mammalian skeletal muscle fiber type transitions. Int. Rev. Cytol. 170:1997;143-223.
    • (1997) Int. Rev. Cytol. , vol.170 , pp. 143-223
    • Pette, D.1    Staron, R.S.2
  • 49
    • 0019319641 scopus 로고
    • The ATPase activities of rat cardiac myosin isoenzymes
    • Pope B., Hoh J. F., Weeds A. The ATPase activities of rat cardiac myosin isoenzymes. FEBS Letters. 118:1980;205-208.
    • (1980) FEBS Letters , vol.118 , pp. 205-208
    • Pope, B.1    Hoh, J.F.2    Weeds, A.3
  • 50
    • 0025221186 scopus 로고
    • Localization of human cardiac beta-myosin heavy chain gene (MYH7) to chromosome 14q12 by in situ hybridization
    • Qin H., Kemp J., Yip M. Y., Lam P. T. P., Hoh J. F., Morris B. J. Localization of human cardiac beta-myosin heavy chain gene (MYH7) to chromosome 14q12 by in situ hybridization. Cytogenet. Cell Genet. 54:1990;74-76.
    • (1990) Cytogenet. Cell Genet. , vol.54 , pp. 74-76
    • Qin, H.1    Kemp, J.2    Yip, M.Y.3    Lam, P.T.P.4    Hoh, J.F.5    Morris, B.J.6
  • 53
    • 0026545683 scopus 로고
    • Genetic map of nine polymorphic loci comprising a single linkage group on rat chromosome 10: Evidence for linkage conservation with human chromosome 17 and mouse chromosome 11
    • Remmers E. F., Goldmuntz E. A., Cash J. M., Crofford L. J., Misiewicz-Poltorak B., Zha H., Wilder R. L. Genetic map of nine polymorphic loci comprising a single linkage group on rat chromosome 10: evidence for linkage conservation with human chromosome 17 and mouse chromosome 11. Genomics. 14:1992;618-623.
    • (1992) Genomics , vol.14 , pp. 618-623
    • Remmers, E.F.1    Goldmuntz, E.A.2    Cash, J.M.3    Crofford, L.J.4    Misiewicz-Poltorak, B.5    Zha, H.6    Wilder, R.L.7
  • 54
    • 0031031962 scopus 로고    scopus 로고
    • An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms
    • Rovner A. S., Freyzon Y., Trybus K. M. An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms. J. Muscle Res. Cell Motil. 18:1997;103-110.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 103-110
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 55
    • 0030035665 scopus 로고    scopus 로고
    • Structure-function studies of the myosin motor domain: Importance of the 50 kDa cleft
    • Ruppel K. M., Spudich J. A. Structure-function studies of the myosin motor domain: importance of the 50 kDa cleft. Mol. Biol. Cell. 7:1996;1123-1136.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1123-1136
    • Ruppel, K.M.1    Spudich, J.A.2
  • 56
  • 57
    • 0022571043 scopus 로고
    • Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle
    • Saez L., Leinwand L. A. Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle. Nucl. Acids Res. 14:1986;2951-2969.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 2951-2969
    • Saez, L.1    Leinwand, L.A.2
  • 59
    • 0025048136 scopus 로고
    • The P-loop: A common motif in ATP- And GTP-binding proteins
    • Saraste M., Sibbald P. R., Wittinghofer A. The P-loop: a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15:1990;430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 62
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino S., Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 76:1996;371-423.
    • (1996) Physiol. Rev. , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 64
    • 0027932493 scopus 로고
    • Fibre type classification and myosin isoforms in the human masseter muscle
    • Sciote J. J., Rowlerson A. M., Hopper C., Hunt N. P. Fibre type classification and myosin isoforms in the human masseter muscle. J. Neurol. Sci. 126:1994;15-24.
    • (1994) J. Neurol. Sci. , vol.126 , pp. 15-24
    • Sciote, J.J.1    Rowlerson, A.M.2    Hopper, C.3    Hunt, N.P.4
  • 66
    • 0028566846 scopus 로고
    • Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle
    • Smerdu V., Karsch-Mizrachi I., Campione M., Leinwand L., Schiaffino S. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. Am. J. Physiol. 267:1994;C1723-C1728.
    • (1994) Am. J. Physiol. , vol.267
    • Smerdu, V.1    Karsch-Mizrachi, I.2    Campione, M.3    Leinwand, L.4    Schiaffino, S.5
  • 67
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Smith C. A., Rayment I. Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys. J. 70:1996;1590-1602.
    • (1996) Biophys. J. , vol.70 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 68
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich J. A. How molecular motors work. Nature. 372:1994;515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 69
    • 0027986615 scopus 로고
    • Differences in myosin composition between human oro-facial, masticatory and limb muscles: Enzyme-, immunohisto- And biochemical studies
    • Stal P., Eriksson P. O., Schiaffino S., Butler-Browne G. S., Thornell L. E. Differences in myosin composition between human oro-facial, masticatory and limb muscles: enzyme-, immunohisto- and biochemical studies. J. Muscle Res. Cell Motil. 15:1994;517-534.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 517-534
    • Stal, P.1    Eriksson, P.O.2    Schiaffino, S.3    Butler-Browne, G.S.4    Thornell, L.E.5
  • 70
    • 0025248687 scopus 로고
    • The human embryonic myosin heavy chain. Complete primary structure reveals evolutionary relationships with other developmental isoforms
    • Stedman H. H., Eller M., Jullian E. H., Fertels S. H., Sarkar S., Sylvester J. E., Kelly A. M., Rubinstein N. A. The human embryonic myosin heavy chain. Complete primary structure reveals evolutionary relationships with other developmental isoforms. J. Biol. Chem. 265:1990;3568-3576.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3568-3576
    • Stedman, H.H.1    Eller, M.2    Jullian, E.H.3    Fertels, S.H.4    Sarkar, S.5    Sylvester, J.E.6    Kelly, A.M.7    Rubinstein, N.A.8
  • 72
    • 0020563473 scopus 로고
    • Mapping of actin-binding sites on the heavy chain of myosin subfragment 1
    • Sutoh K. Mapping of actin-binding sites on the heavy chain of myosin subfragment 1. Biochemistry. 22:1983;1579-1585.
    • (1983) Biochemistry , vol.22 , pp. 1579-1585
    • Sutoh, K.1
  • 74
    • 0026774648 scopus 로고
    • Evidence for inserted sequences in the head region of nonmuscle myosin specific to the nervous system. Cloning of the cDNA encoding the myosin heavy chain-B isoform of vertebrate nonmuscle myosin
    • Takahashi M., Kawamoto S., Adelstein R. S. Evidence for inserted sequences in the head region of nonmuscle myosin specific to the nervous system. Cloning of the cDNA encoding the myosin heavy chain-B isoform of vertebrate nonmuscle myosin. J. Biol. Chem. 267:1992;17864-17871.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17864-17871
    • Takahashi, M.1    Kawamoto, S.2    Adelstein, R.S.3
  • 75
    • 0027091176 scopus 로고
    • Evolutionarily conserved promoter motifs and enhancer organization in the mouse gene encoding the IIB myosin heavy chain isoform expressed in adult fast skeletal muscle
    • Takeda S., North D. L., Lakich M. M., Russell S. D., Kahng L. S., Whalen R. G. Evolutionarily conserved promoter motifs and enhancer organization in the mouse gene encoding the IIB myosin heavy chain isoform expressed in adult fast skeletal muscle. CR Acad. Sci. III. 315:1992;467-472.
    • (1992) CR Acad. Sci. III. , vol.315 , pp. 467-472
    • Takeda, S.1    North, D.L.2    Lakich, M.M.3    Russell, S.D.4    Kahng, L.S.5    Whalen, R.G.6
  • 76
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda T. Q., Ruppel K. M., Spudich J. A. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature. 368:1994;567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.1    Ruppel, K.M.2    Spudich, J.A.3
  • 77
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda T. Q., Abramson P. D., Spudich J. A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl Acad. Sci. USA. 93:1996;4459-4464.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.1    Abramson, P.D.2    Spudich, J.A.3
  • 79
    • 0030046902 scopus 로고    scopus 로고
    • Contractile protein mutations and heart disease
    • Vikstrom K. L., Leinwand L. A. Contractile protein mutations and heart disease. Curr. Opin. Cell Biol. 8:1996;97-105.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 97-105
    • Vikstrom, K.L.1    Leinwand, L.A.2
  • 80
    • 0019448156 scopus 로고
    • Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains
    • Wagner P. D., Giniger E. Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains. Nature. 292:1981;560-562.
    • (1981) Nature , vol.292 , pp. 560-562
    • Wagner, P.D.1    Giniger, E.2
  • 81
    • 0029751987 scopus 로고    scopus 로고
    • The mammalian myosin heavy chain gene family
    • Weiss A., Leinwand L. A. The mammalian myosin heavy chain gene family. Annu. Rev. Cell Dev. Biol. 12:1996;417-439.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 417-439
    • Weiss, A.1    Leinwand, L.A.2
  • 83
    • 0021021632 scopus 로고
    • Sequential accumulation of mRNAs encoding different myosin heavy chain isoforms during skeletal muscle development in vivo detected with a recombinant plasmid identified as coding for an adult fast myosin heavy chain from mouse skeletal muscle
    • Weydert A., Daubas P., Caravatti M., Minty A., Bugaisky G., Cohen A., Robert B., Buckingham M. Sequential accumulation of mRNAs encoding different myosin heavy chain isoforms during skeletal muscle development in vivo detected with a recombinant plasmid identified as coding for an adult fast myosin heavy chain from mouse skeletal muscle. J. Biol. Chem. 258:1983;13867-13874.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13867-13874
    • Weydert, A.1    Daubas, P.2    Caravatti, M.3    Minty, A.4    Bugaisky, G.5    Cohen, A.6    Robert, B.7    Buckingham, M.8
  • 85
    • 0021925453 scopus 로고
    • Co-expression of multiple myosin heavy chain genes, in addition to a tissue-specific one, in extraocular musculature
    • Wieczorek D. F., Periasamy M., Butler-Browne G. S., Whalen R. G., Nadal-Ginard B. Co-expression of multiple myosin heavy chain genes, in addition to a tissue-specific one, in extraocular musculature. J. Cell Biol. 101:1985;618-629.
    • (1985) J. Cell Biol. , vol.101 , pp. 618-629
    • Wieczorek, D.F.1    Periasamy, M.2    Butler-Browne, G.S.3    Whalen, R.G.4    Nadal-Ginard, B.5
  • 87
    • 0024352016 scopus 로고
    • Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP
    • Yamamoto K. Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP. Biochemistry. 28:1989;5573-5577.
    • (1989) Biochemistry , vol.28 , pp. 5573-5577
    • Yamamoto, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.