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Volumn 9, Issue 8, 2009, Pages 2139-2148

Mapping of O-linked β-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle

Author keywords

Contractile proteins; Mass spectrometry; O linked N acetylglucosamine; Sitemapping

Indexed keywords

CONTRACTILE PROTEIN; MYOSIN HEAVY CHAIN; N ACETYL BETA GLUCOSAMINIDASE;

EID: 65349126348     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800617     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells, L., Vosseler, K., Hart, G. W., Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc. Science 2001, 291, 2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseler, K.2    Hart, G.W.3
  • 2
    • 0842347416 scopus 로고    scopus 로고
    • Ogtdependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability
    • O'Donnell, N., Zachara, N. E., Hart, G. W., Marth, J. D., Ogtdependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol. Cell. Biol. 2004, 24, 1680-1690.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 3
    • 0031943723 scopus 로고    scopus 로고
    • Insulin and glucosamine infusions increase O-linked Nacetyl-glucosamine in skeletal muscle proteins in vivo
    • Yki-Jarvinen, H., Virkamäki, A., Daniels, M. C., McClain, D. et al., Insulin and glucosamine infusions increase O-linked Nacetyl-glucosamine in skeletal muscle proteins in vivo. Metabolism 1998, 47, 449-455.
    • (1998) Metabolism , vol.47 , pp. 449-455
    • Yki-Jarvinen, H.1    Virkamäki, A.2    Daniels, M.C.3    McClain, D.4
  • 4
    • 15244345550 scopus 로고    scopus 로고
    • Relationship between protein Olinked glycosylation and insulin-stimulated glucose transport in rat skeletal muscle following calorie restriction or exposure to O-(2-acetamido-2-deoxy-d- glucopyranosylidene)amino-Nphenylcarbamate
    • Arias, E. B., Cartee, G. D., Relationship between protein Olinked glycosylation and insulin-stimulated glucose transport in rat skeletal muscle following calorie restriction or exposure to O-(2-acetamido-2-deoxy-d- glucopyranosylidene)amino-Nphenylcarbamate. Acta Physiol. Scand. 2005, 183, 281-289.
    • (2005) Acta Physiol. Scand , vol.183 , pp. 281-289
    • Arias, E.B.1    Cartee, G.D.2
  • 5
    • 33646433939 scopus 로고    scopus 로고
    • O-GlcNAc level variations are associated with the development of skeletal muscle atrophy
    • Cieniewski-Bernard, C., Mounier, Y., Michalski, J. C., Bastide, B., O-GlcNAc level variations are associated with the development of skeletal muscle atrophy. J. Appl. Physiol. 2006, 100, 1499-1505.
    • (2006) J. Appl. Physiol , vol.100 , pp. 1499-1505
    • Cieniewski-Bernard, C.1    Mounier, Y.2    Michalski, J.C.3    Bastide, B.4
  • 6
    • 33845582766 scopus 로고    scopus 로고
    • Role of protein Olinked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system
    • Fülöp, N., Marchase, R. B., Chatham, J. C., Role of protein Olinked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system. Cardiovasc. Res. 2007, 73, 288-297.
    • (2007) Cardiovasc. Res , vol.73 , pp. 288-297
    • Fülöp, N.1    Marchase, R.B.2    Chatham, J.C.3
  • 7
    • 3042815335 scopus 로고    scopus 로고
    • Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry
    • Cieniewski, C., Bastide, B., Lefebvre, T., Lemoine, J. et al., Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry. Mol. Cell. Proteomics 2004, 3, 577-585.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 577-585
    • Cieniewski, C.1    Bastide, B.2    Lefebvre, T.3    Lemoine, J.4
  • 9
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta
    • Cheng, X., Cole, R. N., Zaia, J., Hart, G. W., Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta. Biochemistry 2000, 39, 11609-11620.
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 10
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • Comer, F. I., Hart, G. W., Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 2001, 40, 7845-7852.
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.I.1    Hart, G.W.2
  • 11
    • 0028007599 scopus 로고
    • Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain
    • Lee, R. J., Egelhoff, T. T., Spudich, J. A., Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain. J. Cell Sci. 1994, 107, 2875-2886.
    • (1994) J. Cell Sci , vol.107 , pp. 2875-2886
    • Lee, R.J.1    Egelhoff, T.T.2    Spudich, J.A.3
  • 12
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., Homsher, E., Regnier, M., Regulation of contraction in striated muscle. Physiol. Rev. 2000, 8, 853-924.
    • (2000) Physiol. Rev , vol.8 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 13
    • 0015851141 scopus 로고
    • A phosphorylated light-chain component of myosin from skeletal muscle
    • Perrie, W. T., Smillie, L. B., Perry, S. B., A phosphorylated light-chain component of myosin from skeletal muscle. Biochem. J. 1973, 135, 151-164.
    • (1973) Biochem. J , vol.135 , pp. 151-164
    • Perrie, W.T.1    Smillie, L.B.2    Perry, S.B.3
  • 14
    • 0021961219 scopus 로고
    • The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers
    • Persechini, A., Stull, J. T., Cooke, R., The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers. J. Biol. Chem. 1985, 260, 7951-7954.
    • (1985) J. Biol. Chem , vol.260 , pp. 7951-7954
    • Persechini, A.1    Stull, J.T.2    Cooke, R.3
  • 15
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function
    • Sweeney, H. L., Bowman, B. F., Stull, J. T., Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function. Am. J. Physiol. 1993, 264, C1085-C1095.
    • (1993) Am. J. Physiol , vol.264
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 16
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry
    • Greis, K. D., Hayes, B. K., Comer, F. I., Kirk, M. et al., Selective detection and site analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry. Anal. Biochem. 1996, 234, 38-49.
    • (1996) Anal. Biochem , vol.234 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4
  • 17
    • 0034329621 scopus 로고    scopus 로고
    • Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry
    • Haynes, P. A., Aebersold, R., Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry. Anal. Chem. 2000, 72, 5402-5410.
    • (2000) Anal. Chem , vol.72 , pp. 5402-5410
    • Haynes, P.A.1    Aebersold, R.2
  • 18
    • 0035567107 scopus 로고    scopus 로고
    • Identification of GlcNAcylation sites of peptides and α-cristallin using O-TOF mass spectrometry
    • Chalkley, R. J., Burlingame, A. L., Identification of GlcNAcylation sites of peptides and α-cristallin using O-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 2001, 12, 1106-1113.
    • (2001) J. Am. Soc. Mass Spectrom , vol.12 , pp. 1106-1113
    • Chalkley, R.J.1    Burlingame, A.L.2
  • 19
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using tags for serine and threonine post-translational modifications
    • Wells, L., Vosseler, K., Cole, R. N., Cronshaw, J. M. et al., Mapping sites of O-GlcNAc modification using tags for serine and threonine post-translational modifications. Mol. Cell. Proteomics 2002, 1, 791-804.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseler, K.2    Cole, R.N.3    Cronshaw, J.M.4
  • 20
    • 33644698706 scopus 로고    scopus 로고
    • Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrat-1
    • Ball, L. E., Berkaw, M. N., Buse, M. G., Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrat-1. Mol. Cell. Proteomics 2006, 5, 313-323.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 313-323
    • Ball, L.E.1    Berkaw, M.N.2    Buse, M.G.3
  • 21
    • 0033369257 scopus 로고    scopus 로고
    • Timedependent changes in myosin heavy chain mRNA and protein isoforms in unloaded soleus muscle of rat
    • Stevens, L., Sultan, K. R., Peuker, H., Gohlsch, B. et al., Timedependent changes in myosin heavy chain mRNA and protein isoforms in unloaded soleus muscle of rat. Am. J. Physiol. 1999, 277, C1044-C1049.
    • (1999) Am. J. Physiol , vol.277
    • Stevens, L.1    Sultan, K.R.2    Peuker, H.3    Gohlsch, B.4
  • 22
    • 0035117741 scopus 로고    scopus 로고
    • Expression and functional behavior of troponin C in soleus muscle fibers of rat after hindlimb unloading
    • Kischel, P., Bastide, B., Stevens, L., Mounier, Y., Expression and functional behavior of troponin C in soleus muscle fibers of rat after hindlimb unloading. J. Appl. Physiol. 2001, 90, 1095-1101.
    • (2001) J. Appl. Physiol , vol.90 , pp. 1095-1101
    • Kischel, P.1    Bastide, B.2    Stevens, L.3    Mounier, Y.4
  • 23
    • 0036452887 scopus 로고    scopus 로고
    • Expression and functional implications of troponin T isoforms in soleus muscle fibers of rat after unloading
    • Bastide, B., Kischel, P., Puterflam, J., Stevens, L. et al., Expression and functional implications of troponin T isoforms in soleus muscle fibers of rat after unloading. Pflugers Arch. 2002, 444, 345-352.
    • (2002) Pflugers Arch , vol.444 , pp. 345-352
    • Bastide, B.1    Kischel, P.2    Puterflam, J.3    Stevens, L.4
  • 24
    • 0036080586 scopus 로고    scopus 로고
    • Time-dependent changes in expression of troponin subunit isoforms in unloaded rat soleus muscle
    • Stevens, L., Bastide, B., Kischel, P., Pette, D. et al., Time-dependent changes in expression of troponin subunit isoforms in unloaded rat soleus muscle. Am. J. Physiol. 2002, 282, C1025-C1030.
    • (2002) Am. J. Physiol , vol.282
    • Stevens, L.1    Bastide, B.2    Kischel, P.3    Pette, D.4
  • 25
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • Vosseller, K., Hansen, K. C., Chalkley, R. J., Trinidad, J. C. et al., Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 2005, 5, 388-398.
    • (2005) Proteomics , vol.5 , pp. 388-398
    • Vosseller, K.1    Hansen, K.C.2    Chalkley, R.J.3    Trinidad, J.C.4
  • 26
    • 33646900710 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G. et al., O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 2006, 5, 923-934.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3    Specht, C.G.4
  • 27
    • 0030772457 scopus 로고    scopus 로고
    • O-glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions
    • Roos, M. D, Su,, K., Baker, J. R, Kudlow, J. E., O-glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions. Mol. Cell. Biol. 1997, 17, 6472-6480.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 6472-6480
    • Roos, M.D.1    Su, K.2    Baker, J.R.3    Kudlow, J.E.4
  • 28
    • 0011678547 scopus 로고    scopus 로고
    • Interaction of the transcription factor Sp1 with the nuclear pore protein p62 requires the C-terminal domain of p62
    • Han, I., Roos, M. D., Kudlow, J. E., Interaction of the transcription factor Sp1 with the nuclear pore protein p62 requires the C-terminal domain of p62. J. Cell. Biochem. 1998, 68, 50-61.
    • (1998) J. Cell. Biochem , vol.68 , pp. 50-61
    • Han, I.1    Roos, M.D.2    Kudlow, J.E.3
  • 29
    • 0035811072 scopus 로고    scopus 로고
    • O-linkage of Nacetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
    • Yang, X., Su, K., Roos, M. D., Chang, O. et al., O-linkage of Nacetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc. Natl. Acad. Sci. 2001, 98, 6611-6616.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 6611-6616
    • Yang, X.1    Su, K.2    Roos, M.D.3    Chang, O.4
  • 30
    • 0029593486 scopus 로고
    • Studies of the interaction between titin and myosin
    • Houmeida, A., Holt, J., Tskhovrebova, L., Trinick, J., Studies of the interaction between titin and myosin. J. Cell Biol. 1995, 131, 1471-1481.
    • (1995) J. Cell Biol , vol.131 , pp. 1471-1481
    • Houmeida, A.1    Holt, J.2    Tskhovrebova, L.3    Trinick, J.4
  • 31
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann, W. M., Gautel, M., Weber, K., Fürst, D. O., Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J. 1997, 16, 211-220.
    • (1997) EMBO J , vol.16 , pp. 211-220
    • Obermann, W.M.1    Gautel, M.2    Weber, K.3    Fürst, D.O.4
  • 32
    • 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. et al., 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. 1998, 9, 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
  • 33
    • 0031581843 scopus 로고    scopus 로고
    • A 29 residue region of the sarcomeric myosin rod is necessary for filament formation
    • Sohn, R. L., Vikstrom, K. L., Strauss, M., Cohen, C. et al., A 29 residue region of the sarcomeric myosin rod is necessary for filament formation. J. Mol. Biol. 1997, 266, 317-330.
    • (1997) J. Mol. Biol , vol.266 , pp. 317-330
    • Sohn, R.L.1    Vikstrom, K.L.2    Strauss, M.3    Cohen, C.4
  • 34
    • 65349142302 scopus 로고    scopus 로고
    • Hereditary myosin myopathies
    • Oldfors, A., Hereditary myosin myopathies. Neuromuscul. Disord. 2007, 173, 55-67.
    • (2007) Neuromuscul. Disord , vol.173 , pp. 55-67
    • Oldfors, A.1
  • 35
    • 4544374719 scopus 로고    scopus 로고
    • Mutations in the slow skeletal muscle fiber myosin heavy chain gene (MYH7) cause laing early-onset distal myopathy (MPD1)
    • Meredith, C., Herrmann, R., Parry, C., Liyanage, K. et al., Mutations in the slow skeletal muscle fiber myosin heavy chain gene (MYH7) cause laing early-onset distal myopathy (MPD1). Am. J. Hum. Genet. 2004, 75, 703-708.
    • (2004) Am. J. Hum. Genet , vol.75 , pp. 703-708
    • Meredith, C.1    Herrmann, R.2    Parry, C.3    Liyanage, K.4
  • 36
    • 34648854435 scopus 로고    scopus 로고
    • Congenital myopathies
    • Laing, N. G., Congenital myopathies. Curr. Opin. Neurol. 2007, 20, 583-589.
    • (2007) Curr. Opin. Neurol , vol.20 , pp. 583-589
    • Laing, N.G.1
  • 37
    • 0028787131 scopus 로고
    • Allostery, cooperativity, and different structural states in F-actin
    • Egelman, E. H., Orlova, A., Allostery, cooperativity, and different structural states in F-actin. J. Structural Biol. 1995, 115, 159-162.
    • (1995) J. Structural Biol , vol.115 , pp. 159-162
    • Egelman, E.H.1    Orlova, A.2
  • 38
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels
    • Lorenz, M., Poole, K. J., Popp, D., Rosenbaum, G. et al., An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 1995, 246, 108-119.
    • (1995) J. Mol. Biol , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.2    Popp, D.3    Rosenbaum, G.4
  • 39
    • 0026672241 scopus 로고
    • Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules
    • Hill, L. E., Mehegan, J. P., Butters, C. A., Tobacman, L. S., Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules. J. Biol. Chem. 1992, 267, 16106-16113.
    • (1992) J. Biol. Chem , vol.267 , pp. 16106-16113
    • Hill, L.E.1    Mehegan, J.P.2    Butters, C.A.3    Tobacman, L.S.4
  • 40
    • 0027082784 scopus 로고
    • Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly
    • Willadsen, K. A., Butters, C. A., Hill, L. E., Tobacman, L. S., Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly. J. Biol. Chem. 1992, 267, 23746-23752.
    • (1992) J. Biol. Chem , vol.267 , pp. 23746-23752
    • Willadsen, K.A.1    Butters, C.A.2    Hill, L.E.3    Tobacman, L.S.4
  • 41
    • 0033917257 scopus 로고    scopus 로고
    • The effect of single residue substitutions of serine-283 on the strength of headto-tail interaction and actin binding properties of rabbit skeletal muscle alpha-tropomyosin
    • Sano, K., Maeda, K., Oda, T., Maeda, Y., The effect of single residue substitutions of serine-283 on the strength of headto-tail interaction and actin binding properties of rabbit skeletal muscle alpha-tropomyosin. J. Biochem. 2000, 27, 1095-1102.
    • (2000) J. Biochem , vol.27 , pp. 1095-1102
    • Sano, K.1    Maeda, K.2    Oda, T.3    Maeda, Y.4
  • 42
    • 0023645981 scopus 로고
    • Effect of different troponin T-tropomyosin combinations on thin filament activation
    • Schachat, F. H., Diamond, M. S., Brandt, P. W., Effect of different troponin T-tropomyosin combinations on thin filament activation. J. Mol. Biol. 1987, 198, 551-554.
    • (1987) J. Mol. Biol , vol.198 , pp. 551-554
    • Schachat, F.H.1    Diamond, M.S.2    Brandt, P.W.3
  • 43
    • 34547605959 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity
    • Rajan, S., Ahmed, R. P., Jagatheesan, G., Petrashevskaya, N. et al., Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity. Circ. Res. 2007, 101, 205-214.
    • (2007) Circ. Res , vol.101 , pp. 205-214
    • Rajan, S.1    Ahmed, R.P.2    Jagatheesan, G.3    Petrashevskaya, N.4
  • 44
    • 0031883848 scopus 로고    scopus 로고
    • A mutant tropomyosin that causes hypertrophic cardiomyopathy is expressed in vivo and associated with an increased calcium sensitivity
    • Bottinelli, R., Coviello, D. A., Redwood, C. S., Pellegrino, M. A. et al., A mutant tropomyosin that causes hypertrophic cardiomyopathy is expressed in vivo and associated with an increased calcium sensitivity. Circ. Res. 1998, 82, 106-115.
    • (1998) Circ. Res , vol.82 , pp. 106-115
    • Bottinelli, R.1    Coviello, D.A.2    Redwood, C.S.3    Pellegrino, M.A.4
  • 45
    • 34250174756 scopus 로고    scopus 로고
    • Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments
    • Boussouf, S. E., Maytum, R., Jaquet, K., Geeves, M. A., Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments. J. Muscle Res. Cell Motil. 2007, 28, 49-58.
    • (2007) J. Muscle Res. Cell Motil , vol.28 , pp. 49-58
    • Boussouf, S.E.1    Maytum, R.2    Jaquet, K.3    Geeves, M.A.4


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