메뉴 건너뛰기




Volumn 10, Issue 2, 2012, Pages

Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties

Author keywords

[No Author keywords available]

Indexed keywords

MYOMESIN; MYOSIN; MUSCLE PROTEIN;

EID: 84857477240     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001261     Document Type: Article
Times cited : (36)

References (40)
  • 1
    • 79951552050 scopus 로고    scopus 로고
    • The sarcomeric cytoskeleton: who picks up the strain?
    • Gautel M, (2011) The sarcomeric cytoskeleton: who picks up the strain? Curr Opin Cell Biol 23: 39-46.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 39-46
    • Gautel, M.1
  • 2
    • 24344470264 scopus 로고    scopus 로고
    • The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere
    • Agarkova I, Perriard J. C, (2005) The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere. Trends Cell Biol 15: 477-485.
    • (2005) Trends Cell Biol , vol.15 , pp. 477-485
    • Agarkova, I.1    Perriard, J.C.2
  • 3
    • 0031918744 scopus 로고    scopus 로고
    • The filament lattice of striated muscle
    • Millman B. M, (1998) The filament lattice of striated muscle. Physiol Rev 78: 359-391.
    • (1998) Physiol Rev , vol.78 , pp. 359-391
    • Millman, B.M.1
  • 4
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments
    • Horowits R, Podolsky R. J, (1987) The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments. J Cell Biol 105: 2217-2223.
    • (1987) J Cell Biol , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 5
    • 0028586108 scopus 로고
    • M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles
    • Pask H. T, Jones K. L, Luther P. K, Squire J. M, (1994) M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles. J Muscle Res Cell Motil 15: 633-645.
    • (1994) J Muscle Res Cell Motil , vol.15 , pp. 633-645
    • Pask, H.T.1    Jones, K.L.2    Luther, P.K.3    Squire, J.M.4
  • 7
    • 77955397887 scopus 로고    scopus 로고
    • Roles of titin in the structure and elasticity of the sarcomere
    • Tskhovrebova L, Trinick J, (2010) Roles of titin in the structure and elasticity of the sarcomere. J Biomed Biotechnol 2010: 612482.
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 612482
    • Tskhovrebova, L.1    Trinick, J.2
  • 8
    • 39749137483 scopus 로고    scopus 로고
    • Sense and stretchability: the role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction
    • Linke W. A, (2008) Sense and stretchability: the role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction. Cardiovasc Res 77: 637-648.
    • (2008) Cardiovasc Res , vol.77 , pp. 637-648
    • Linke, W.A.1
  • 9
    • 37049012075 scopus 로고    scopus 로고
    • Structure-function relations of the giant elastic protein titin in striated and smooth muscle cells
    • Granzier H, Labeit S, (2007) Structure-function relations of the giant elastic protein titin in striated and smooth muscle cells. Muscle Nerve 36: 740-755.
    • (2007) Muscle Nerve , vol.36 , pp. 740-755
    • Granzier, H.1    Labeit, S.2
  • 10
    • 0018333449 scopus 로고
    • The measurement and dynamic implications of thin filament lengths in heart muscle
    • Robinson T. F, Winegrad S, (1979) The measurement and dynamic implications of thin filament lengths in heart muscle. J Physiol 286: 607-619.
    • (1979) J Physiol , vol.286 , pp. 607-619
    • Robinson, T.F.1    Winegrad, S.2
  • 11
    • 77958502526 scopus 로고    scopus 로고
    • Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis
    • Al-Khayat H. A, Kensler R. W, Morris E. P, Squire J. M, (2010) Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis. J Mol Biol 403: 763-776.
    • (2010) J Mol Biol , vol.403 , pp. 763-776
    • Al-Khayat, H.A.1    Kensler, R.W.2    Morris, E.P.3    Squire, J.M.4
  • 12
    • 38349085336 scopus 로고    scopus 로고
    • Myomesin 3, a novel structural component of the M-band in striated muscle
    • Schoenauer R, Lange S, Hirschy A, Ehler E, Perriard J. C, et al. (2008) Myomesin 3, a novel structural component of the M-band in striated muscle. J Mol Biol 376: 338-351.
    • (2008) J Mol Biol , vol.376 , pp. 338-351
    • Schoenauer, R.1    Lange, S.2    Hirschy, A.3    Ehler, E.4    Perriard, J.C.5
  • 13
    • 9644273940 scopus 로고    scopus 로고
    • Dimerisation of myomesin: implications for the structure of the sarcomeric M-band
    • Lange S, Himmel M, Auerbach D, Agarkova I, Hayess K, et al. (2005) Dimerisation of myomesin: implications for the structure of the sarcomeric M-band. J Mol Biol 345: 289-298.
    • (2005) J Mol Biol , vol.345 , pp. 289-298
    • Lange, S.1    Himmel, M.2    Auerbach, D.3    Agarkova, I.4    Hayess, K.5
  • 14
    • 33751192641 scopus 로고    scopus 로고
    • Targeted homozygous deletion of M-band titin in cardiomyocytes prevents sarcomere formation
    • Musa H, Meek S, Gautel M, Peddie D, Smith A. J, et al. (2006) Targeted homozygous deletion of M-band titin in cardiomyocytes prevents sarcomere formation. J Cell Sci 119: 4322-4331.
    • (2006) J Cell Sci , vol.119 , pp. 4322-4331
    • Musa, H.1    Meek, S.2    Gautel, M.3    Peddie, D.4    Smith, A.J.5
  • 15
    • 46749123127 scopus 로고    scopus 로고
    • Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band-implications for hereditary myopathies
    • Fukuzawa A, Lange S, Holt M, Vihola A, Carmignac V, et al. (2008) Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band-implications for hereditary myopathies. J Cell Sci 121: 1841-1851.
    • (2008) J Cell Sci , vol.121 , pp. 1841-1851
    • Fukuzawa, A.1    Lange, S.2    Holt, M.3    Vihola, A.4    Carmignac, V.5
  • 16
    • 38049006477 scopus 로고    scopus 로고
    • Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin
    • Pinotsis N, Lange S, Perriard J. C, Svergun D. I, Wilmanns M, (2008) Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin. EMBO J 27: 253-264.
    • (2008) EMBO J , vol.27 , pp. 253-264
    • Pinotsis, N.1    Lange, S.2    Perriard, J.C.3    Svergun, D.I.4    Wilmanns, M.5
  • 17
    • 0242571958 scopus 로고    scopus 로고
    • Small angle scattering studies of biological macromolecules in solution
    • Svergun D. I, Koch M. H. J, (2003) Small angle scattering studies of biological macromolecules in solution. Rep Prog Phys 66: 1735-1782.
    • (2003) Rep Prog Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 18
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernado P, Mylonas E, Petoukhov M. V, Blackledge M, Svergun D. I, (2007) Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc 129: 5656-5664.
    • (2007) J Am Chem Soc , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 19
    • 80052140214 scopus 로고    scopus 로고
    • Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin
    • Berkemeier F, Bertz M, Xiao S, Pinotsis N, Wilmanns M, et al. (2011) Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin. Proc Natl Acad Sci U S A 108: 14139-14144.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14139-14144
    • Berkemeier, F.1    Bertz, M.2    Xiao, S.3    Pinotsis, N.4    Wilmanns, M.5
  • 20
    • 31944436148 scopus 로고    scopus 로고
    • Protein structure by mechanical triangulation
    • Dietz H, Rief M, (2006) Protein structure by mechanical triangulation. Proc Natl Acad Sci U S A 103: 1244-1247.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 1244-1247
    • Dietz, H.1    Rief, M.2
  • 22
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann W. M, Gautel M, Steiner F, van der Ven P. F, Weber K, et al. (1996) The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J Cell Biol 134: 1441-1453.
    • (1996) J Cell Biol , vol.134 , pp. 1441-1453
    • Obermann, W.M.1    Gautel, M.2    Steiner, F.3    van der Ven, P.F.4    Weber, K.5
  • 23
    • 77955526103 scopus 로고    scopus 로고
    • The giant protein titin as an integrator of myocyte signaling pathways
    • Linke W. A, Kruger M, (2010) The giant protein titin as an integrator of myocyte signaling pathways. Physiology (Bethesda) 25: 186-198.
    • (2010) Physiology (Bethesda) , vol.25 , pp. 186-198
    • Linke, W.A.1    Kruger, M.2
  • 24
    • 54849406188 scopus 로고    scopus 로고
    • Evidence for the oligomeric state of 'elastic' titin in muscle sarcomeres
    • Houmeida A, Baron A, Keen J, Khan G. N, Knight P. J, et al. (2008) Evidence for the oligomeric state of 'elastic' titin in muscle sarcomeres. J Mol Biol 384: 299-312.
    • (2008) J Mol Biol , vol.384 , pp. 299-312
    • Houmeida, A.1    Baron, A.2    Keen, J.3    Khan, G.N.4    Knight, P.J.5
  • 25
    • 33745726393 scopus 로고    scopus 로고
    • Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules?
    • Tskhovrebova L, Houmeida A, Trinick J, (2005) Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules? J Muscle Res Cell Motil 26: 285-289.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 285-289
    • Tskhovrebova, L.1    Houmeida, A.2    Trinick, J.3
  • 27
    • 0041825389 scopus 로고    scopus 로고
    • Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein
    • Hornemann T, Kempa S, Himmel M, Hayess K, Furst D. O, et al. (2003) Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein. J Mol Biol 332: 877-887.
    • (2003) J Mol Biol , vol.332 , pp. 877-887
    • Hornemann, T.1    Kempa, S.2    Himmel, M.3    Hayess, K.4    Furst, D.O.5
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor V, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, V.2
  • 29
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A, Teplyakov A, (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30: 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 32
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S. J, Baldwin P. R, Chiu W, (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128: 82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 34
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh T. R, Gao H, Baxter W. T, Asturias F. J, Boisset N, et al. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat Protoc 3: 1941-1974.
    • (2008) Nat Protoc , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5
  • 35
  • 36
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D. I, (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25: 495-503.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 37
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D. I, Barberato C, Koch M. H. J, (1995) CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28: 768-773.
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 38
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D. I, (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76: 2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 39
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre K, Sanejouand Y. H, (2004) ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res 32: W610-W614.
    • (2004) Nucleic Acids Res , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2
  • 40
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork P, Downing A. K, Kieffer B, Campbell I. D, (1996) Structure and distribution of modules in extracellular proteins. Q Rev Biophys 29: 119-167.
    • (1996) Q Rev Biophys , vol.29 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.