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Volumn 23, Issue 1, 2011, Pages 39-46

The sarcomeric cytoskeleton: Who picks up the strain?

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ; CONNECTIN; CYTOSKELETON PROTEIN; MYOMESIN; MYOSIN ADENOSINE TRIPHOSPHATASE; NEBULIN; OBSCURIN;

EID: 79951552050     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.12.001     Document Type: Review
Times cited : (143)

References (81)
  • 1
  • 2
    • 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. The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments. J Cell Biol 1987, 105:2217-2223.
    • (1987) J Cell Biol , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 3
    • 0019990501 scopus 로고
    • Time-resolved X-ray diffraction studies of the myosin layer-line reflections during muscle contraction
    • Huxley H.E., Faruqi A.R., Kress M., Bordas J., Koch M.H. Time-resolved X-ray diffraction studies of the myosin layer-line reflections during muscle contraction. J Mol Biol 1982, 158:637-684.
    • (1982) J Mol Biol , vol.158 , pp. 637-684
    • Huxley, H.E.1    Faruqi, A.R.2    Kress, M.3    Bordas, J.4    Koch, M.H.5
  • 4
    • 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. The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere. Trends Cell Biol 2005, 15:477-485.
    • (2005) Trends Cell Biol , vol.15 , pp. 477-485
    • Agarkova, I.1    Perriard, J.C.2
  • 5
    • 0033525792 scopus 로고    scopus 로고
    • Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy
    • Yoshikawa Y., Yasuike T., Yagi A., Yamada T. Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy. Biochem Biophys Res Commun 1999, 256:13-19.
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 13-19
    • Yoshikawa, Y.1    Yasuike, T.2    Yagi, A.3    Yamada, T.4
  • 6
    • 76249126880 scopus 로고    scopus 로고
    • Transversal stiffness and Young's modulus of single fibers from rat soleus muscle probed by atomic force microscopy
    • Ogneva I.V., Lebedev D.V., Shenkman B.S. Transversal stiffness and Young's modulus of single fibers from rat soleus muscle probed by atomic force microscopy. Biophys J 2010, 98:418-424.
    • (2010) Biophys J , vol.98 , pp. 418-424
    • Ogneva, I.V.1    Lebedev, D.V.2    Shenkman, B.S.3
  • 8
    • 33750100539 scopus 로고    scopus 로고
    • Transverse stiffness of myofibrils of skeletal and cardiac muscles studied by atomic force microscopy
    • Akiyama N., Ohnuki Y., Kunioka Y., Saeki Y., Yamada T. Transverse stiffness of myofibrils of skeletal and cardiac muscles studied by atomic force microscopy. J Physiol Sci 2006, 56:145-151.
    • (2006) J Physiol Sci , vol.56 , pp. 145-151
    • Akiyama, N.1    Ohnuki, Y.2    Kunioka, Y.3    Saeki, Y.4    Yamada, T.5
  • 9
    • 0037195860 scopus 로고    scopus 로고
    • Distinct signaling pathways are activated in response to mechanical stress applied axially and transversely to skeletal muscle fibers
    • Kumar A., Chaudhry I., Reid M.B., Boriek A.M. Distinct signaling pathways are activated in response to mechanical stress applied axially and transversely to skeletal muscle fibers. J Biol Chem 2002, 277:46493-46503.
    • (2002) J Biol Chem , vol.277 , pp. 46493-46503
    • Kumar, A.1    Chaudhry, I.2    Reid, M.B.3    Boriek, A.M.4
  • 10
    • 77953536044 scopus 로고    scopus 로고
    • Proposed role of the M-band in sarcomere mechanics and mechano-sensing: a model study
    • Shabarchin A.A., Tsaturyan A.K. Proposed role of the M-band in sarcomere mechanics and mechano-sensing: a model study. Biomech Model Mechanobiol 2010, 9:163-175.
    • (2010) Biomech Model Mechanobiol , vol.9 , pp. 163-175
    • Shabarchin, A.A.1    Tsaturyan, A.K.2
  • 11
    • 33646081053 scopus 로고    scopus 로고
    • Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures
    • Hoshijima M. Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures. Am J Physiol Heart Circ Physiol 2006, 290:H1313-1325.
    • (2006) Am J Physiol Heart Circ Physiol , vol.290
    • Hoshijima, M.1
  • 12
    • 77955526103 scopus 로고    scopus 로고
    • The giant protein titin as an integrator of myocyte signaling pathways
    • Linke W.A., Kruger M. The giant protein titin as an integrator of myocyte signaling pathways. Physiology (Bethesda) 2010, 25:186-198.
    • (2010) Physiology (Bethesda) , vol.25 , pp. 186-198
    • Linke, W.A.1    Kruger, M.2
  • 13
    • 60549084865 scopus 로고    scopus 로고
    • The sarcomere and the nucleus: functional links to hypertrophy, atrophy and sarcopenia
    • Gautel M. The sarcomere and the nucleus: functional links to hypertrophy, atrophy and sarcopenia. Adv Med Biol Exp 2008, 642:176-191.
    • (2008) Adv Med Biol Exp , vol.642 , pp. 176-191
    • Gautel, M.1
  • 16
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: probing proteins with AFM-based force spectroscopy
    • Puchner E.M., Gaub H.E. Force and function: probing proteins with AFM-based force spectroscopy. Curr Opin Struct Biol 2009, 19:605-614.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 17
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: converting force into biochemical signals
    • Vogel V. Mechanotransduction involving multimodular proteins: converting force into biochemical signals. Annu Rev Biophys Biomol Struct 2006, 35:459-488.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 459-488
    • Vogel, V.1
  • 18
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo K., Young P., Gautel M., Saraste M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 1999, 98:537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 19
    • 16244409866 scopus 로고    scopus 로고
    • The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin
    • Franzot G., Sjoblom B., Gautel M., Djinovic Carugo K. The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin. J Mol Biol 2005, 348:151-165.
    • (2005) J Mol Biol , vol.348 , pp. 151-165
    • Franzot, G.1    Sjoblom, B.2    Gautel, M.3    Djinovic Carugo, K.4
  • 21
    • 0034383951 scopus 로고    scopus 로고
    • The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism
    • Young P., Gautel M. The interaction of titin and alpha-actinin is controlled by a phospholipid-regulated intramolecular pseudoligand mechanism. EMBO J 2000, 19:6331-6340.
    • (2000) EMBO J , vol.19 , pp. 6331-6340
    • Young, P.1    Gautel, M.2
  • 22
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • Young P., Ferguson C., Bañuelos S., Gautel M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO J 1998, 17:1614-1624.
    • (1998) EMBO J , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Bañuelos, S.3    Gautel, M.4
  • 23
    • 75749136013 scopus 로고    scopus 로고
    • The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling
    • Luther P.K. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. J Muscle Res Cell Motil 2009, 30:171-185.
    • (2009) J Muscle Res Cell Motil , vol.30 , pp. 171-185
    • Luther, P.K.1
  • 24
    • 0023805249 scopus 로고
    • Structural states in the Z band of skeletal muscle correlate with states of active and passive tension
    • Goldstein M.A., Michael L.H., Schroeter J.P., Sass R.L. Structural states in the Z band of skeletal muscle correlate with states of active and passive tension. J Gen Physiol 1988, 92:113-119.
    • (1988) J Gen Physiol , vol.92 , pp. 113-119
    • Goldstein, M.A.1    Michael, L.H.2    Schroeter, J.P.3    Sass, R.L.4
  • 25
    • 0025832699 scopus 로고
    • Role of the Z band in the mechanical properties of the heart
    • Goldstein M.A., Schroeter J.P., Michael L.H. Role of the Z band in the mechanical properties of the heart. FASEB J 1991, 5:2167-2174.
    • (1991) FASEB J , vol.5 , pp. 2167-2174
    • Goldstein, M.A.1    Schroeter, J.P.2    Michael, L.H.3
  • 26
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles
    • Rief M., Pascual J., Saraste M., Gaub H.E. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J Mol Biol 1999, 286:553-561.
    • (1999) J Mol Biol , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 28
    • 77955584718 scopus 로고    scopus 로고
    • A gene for speed: the emerging role of alpha-actinin-3 in muscle metabolism
    • Berman Y., North K.N. A gene for speed: the emerging role of alpha-actinin-3 in muscle metabolism. Physiology (Bethesda) 2010, 25:250-259.
    • (2010) Physiology (Bethesda) , vol.25 , pp. 250-259
    • Berman, Y.1    North, K.N.2
  • 30
  • 32
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disk portion of titin interact in a conformation-dependent way with telethonin
    • Mues A., Van der Ven P.F.M., Young P., Fürst D.O., Gautel M. Two immunoglobulin-like domains of the Z-disk portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett 1998, 428:111-114.
    • (1998) FEBS Lett , vol.428 , pp. 111-114
    • Mues, A.1    Van der Ven, P.F.M.2    Young, P.3    Fürst, D.O.4    Gautel, M.5
  • 34
    • 33644846751 scopus 로고    scopus 로고
    • Mechanical strength of the titin Z1Z2-telethonin complex
    • Lee E.H., Gao M., Pinotsis N., Wilmanns M., Schulten K. Mechanical strength of the titin Z1Z2-telethonin complex. Structure 2006, 14:497-509.
    • (2006) Structure , vol.14 , pp. 497-509
    • Lee, E.H.1    Gao, M.2    Pinotsis, N.3    Wilmanns, M.4    Schulten, K.5
  • 35
    • 69449083856 scopus 로고    scopus 로고
    • The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk
    • Bertz M., Wilmanns M., Rief M. The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk. Proc Natl Acad Sci USA 2009, 106:13307-133310.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13307-133310
    • Bertz, M.1    Wilmanns, M.2    Rief, M.3
  • 37
    • 70349994804 scopus 로고    scopus 로고
    • Depletion of zebrafish Tcap leads to muscular dystrophy via disrupting sarcomere-membrane interaction, not sarcomere assembly
    • Zhang R., Yang J., Zhu J., Xu X. Depletion of zebrafish Tcap leads to muscular dystrophy via disrupting sarcomere-membrane interaction, not sarcomere assembly. Hum Mol Genet 2009, 18:4130-4140.
    • (2009) Hum Mol Genet , vol.18 , pp. 4130-4140
    • Zhang, R.1    Yang, J.2    Zhu, J.3    Xu, X.4
  • 38
    • 9344230851 scopus 로고    scopus 로고
    • Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function
    • Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M., Avkiran M. Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function. Circ Res 2004, 95:1091-1099.
    • (2004) Circ Res , vol.95 , pp. 1091-1099
    • Haworth, R.S.1    Cuello, F.2    Herron, T.J.3    Franzen, G.4    Kentish, J.C.5    Gautel, M.6    Avkiran, M.7
  • 39
    • 77949864284 scopus 로고    scopus 로고
    • Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance
    • Sadikot T., Hammond C.R., Ferrari M.B. Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance. Dev Dyn 2010, 239:1124-1135.
    • (2010) Dev Dyn , vol.239 , pp. 1124-1135
    • Sadikot, T.1    Hammond, C.R.2    Ferrari, M.B.3
  • 40
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • Lange S., Ehler E., Gautel M. From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol 2006, 16:11-18.
    • (2006) Trends Cell Biol , vol.16 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 41
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: a structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo K., Gautel M., Ylanne J., Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett 2002, 513:119-123.
    • (2002) FEBS Lett , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 42
    • 1242320058 scopus 로고    scopus 로고
    • At the crossroads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function
    • Pyle W., Solaro R.J. At the crossroads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function. Circ Res 2004, 94:296-305.
    • (2004) Circ Res , vol.94 , pp. 296-305
    • Pyle, W.1    Solaro, R.J.2
  • 43
    • 69249246979 scopus 로고    scopus 로고
    • Myocyte remodelling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein
    • Boateng S.Y., Senyo S.E., Qi L., Goldspink P.H., Russell B. Myocyte remodelling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein. J Mol Cell Cardiol 2009, 47:426-435.
    • (2009) J Mol Cell Cardiol , vol.47 , pp. 426-435
    • Boateng, S.Y.1    Senyo, S.E.2    Qi, L.3    Goldspink, P.H.4    Russell, B.5
  • 44
    • 62449236060 scopus 로고    scopus 로고
    • Back to square one: what do we know about the functions of muscle LIM protein in the heart?
    • Gehmlich K., Geier C., Milting H., Furst D., Ehler E. Back to square one: what do we know about the functions of muscle LIM protein in the heart?. J Muscle Res Cell Motil 2008, 29:155-158.
    • (2008) J Muscle Res Cell Motil , vol.29 , pp. 155-158
    • Gehmlich, K.1    Geier, C.2    Milting, H.3    Furst, D.4    Ehler, E.5
  • 45
  • 46
    • 34248157682 scopus 로고    scopus 로고
    • The cytoskeleton-associated PDZ-LIM protein, ALP, acts on serum response factor activity to regulate muscle differentiation
    • Pomies P., Pashmforoush M., Vegezzi C., Chien K.R., Auffray C., Beckerle M.C. The cytoskeleton-associated PDZ-LIM protein, ALP, acts on serum response factor activity to regulate muscle differentiation. Mol Biol Cell 2007, 18:1723-1733.
    • (2007) Mol Biol Cell , vol.18 , pp. 1723-1733
    • Pomies, P.1    Pashmforoush, M.2    Vegezzi, C.3    Chien, K.R.4    Auffray, C.5    Beckerle, M.C.6
  • 47
    • 0030753648 scopus 로고    scopus 로고
    • Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD
    • Kong Y., Flick M.J., Kudla A.J., Konieczny S.F. Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD. Mol Cell Biol 1997, 17:4750-4760.
    • (1997) Mol Cell Biol , vol.17 , pp. 4750-4760
    • Kong, Y.1    Flick, M.J.2    Kudla, A.J.3    Konieczny, S.F.4
  • 50
    • 69349085039 scopus 로고    scopus 로고
    • " MLP: a stress sensor goes nuclear" by Sylvia Gunkel, Jorg Heineke, Denise Hilfiker-Kleiner, Ralph Knoll
    • J Mol Cell Cardiol 2010, 48:424-425; author reply 426-427
    • Gehmlich K., Ehler E., Perrot A., Furst D.O., Geier C. " MLP: a stress sensor goes nuclear" by Sylvia Gunkel, Jorg Heineke, Denise Hilfiker-Kleiner, Ralph Knoll. J Mol Cell Cardiol 2009, 47:423-425. J Mol Cell Cardiol 2010, 48:424-425; author reply 426-427.
    • (2009) J Mol Cell Cardiol , vol.47 , pp. 423-425
    • Gehmlich, K.1    Ehler, E.2    Perrot, A.3    Furst, D.O.4    Geier, C.5
  • 53
    • 38349085336 scopus 로고    scopus 로고
    • Myomesin 3, a novel structural component of the M-band in striated muscle
    • Epub 2007 Nov 2022
    • Schoenauer R., Lange S., Hirschy A., Ehler E., Perriard J.C., Agarkova I. Myomesin 3, a novel structural component of the M-band in striated muscle. J Mol Biol 2008, 376:338-351. Epub 2007 Nov 2022.
    • (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    Agarkova, I.6
  • 55
    • 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. Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin. EMBO J 2008, 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
  • 57
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • Young P., Ehler E., Gautel M. Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J Cell Biol 2001, 154:123-136.
    • (2001) J Cell Biol , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 58
    • 46749123127 scopus 로고    scopus 로고
    • Interactions with titin and myomesin target obscurin and its small homologue, obscurin-like 1, to the sarcomeric M-band: implications for hereditary myopathies
    • Fukuzawa A., Lange S., Holt M.R., Vihola A., Carmignac V., Ferreiro A., Udd A.B., Gautel M. Interactions with titin and myomesin target obscurin and its small homologue, obscurin-like 1, to the sarcomeric M-band: implications for hereditary myopathies. J Cell Sci 2008, 121:1841-1851.
    • (2008) J Cell Sci , vol.121 , pp. 1841-1851
    • Fukuzawa, A.1    Lange, S.2    Holt, M.R.3    Vihola, A.4    Carmignac, V.5    Ferreiro, A.6    Udd, A.B.7    Gautel, M.8
  • 59
    • 0031882122 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C gene is specifically expressed in heart during murine and human development
    • Fougerousse F., Delezoide A.L., Fiszman M.Y., Schwartz K., Beckmann J.S., Carrier L. Cardiac myosin binding protein C gene is specifically expressed in heart during murine and human development. Circ Res 1998, 82:130-133.
    • (1998) Circ Res , vol.82 , pp. 130-133
    • Fougerousse, F.1    Delezoide, A.L.2    Fiszman, M.Y.3    Schwartz, K.4    Beckmann, J.S.5    Carrier, L.6
  • 60
    • 0345131725 scopus 로고    scopus 로고
    • Isoform transitions of the myosin-binding protein C family in developing human and mouse muscles: lack of isoform transcomplementation in cardiac muscle
    • Gautel M., Fürst D.O., Cocco A., Schiaffino S. Isoform transitions of the myosin-binding protein C family in developing human and mouse muscles: lack of isoform transcomplementation in cardiac muscle. Circ Res 1998, 82:124-129.
    • (1998) Circ Res , vol.82 , pp. 124-129
    • Gautel, M.1    Fürst, D.O.2    Cocco, A.3    Schiaffino, S.4
  • 61
    • 0022899276 scopus 로고
    • The ultrastuctural localization of C-protein X-protein and H-protein in rabbit muscle
    • Bennett P., Craig R., Starr R., Offer G. The ultrastuctural localization of C-protein X-protein and H-protein in rabbit muscle. J Muscle Res Cell Motil 1986, 7:550-567.
    • (1986) J Muscle Res Cell Motil , vol.7 , pp. 550-567
    • Bennett, P.1    Craig, R.2    Starr, R.3    Offer, G.4
  • 62
    • 2642572455 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C: its role in physiology and disease
    • Flashman E., Redwood C., Moolman-Smook J., Watkins H. Cardiac myosin binding protein C: its role in physiology and disease. Circ Res 2004, 94:1279-1289.
    • (2004) Circ Res , vol.94 , pp. 1279-1289
    • Flashman, E.1    Redwood, C.2    Moolman-Smook, J.3    Watkins, H.4
  • 63
    • 77954216973 scopus 로고    scopus 로고
    • Molecular basis of the head-to-tail assembly of giant muscle proteins obscurin-like 1 and titin
    • Sauer F., Vahokoski J., Song Y.H., Wilmanns M. Molecular basis of the head-to-tail assembly of giant muscle proteins obscurin-like 1 and titin. EMBO Rep 2010, 11:534-540.
    • (2010) EMBO Rep , vol.11 , pp. 534-540
    • Sauer, F.1    Vahokoski, J.2    Song, Y.H.3    Wilmanns, M.4
  • 65
    • 69549133935 scopus 로고    scopus 로고
    • Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum
    • Lange S., Ouyang K., Meyer G., Cui L., Cheng H., Lieber R.L., Chen J. Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum. J Cell Sci 2009, 122:2640-2650.
    • (2009) J Cell Sci , vol.122 , pp. 2640-2650
    • Lange, S.1    Ouyang, K.2    Meyer, G.3    Cui, L.4    Cheng, H.5    Lieber, R.L.6    Chen, J.7
  • 67
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit S., Gautel M., Lakey A., Trinick J. Towards a molecular understanding of titin. EMBO J 1992, 11:1711-1716.
    • (1992) EMBO J , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 68
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein and the 250kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann W.M.J., Gautel M., Steiner F., Van der Ven P., Weber K., Fürst D.O. The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein and the 250kD carboxy-terminal region of titin by immunoelectron microscopy. J Cell Biol 1996, 134:1441-1453.
    • (1996) J Cell Biol , vol.134 , pp. 1441-1453
    • Obermann, W.M.J.1    Gautel, M.2    Steiner, F.3    Van der Ven, P.4    Weber, K.5    Fürst, D.O.6
  • 70
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations
    • Grater F., Shen J., Jiang H., Gautel M., Grubmuller H. Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations. Biophys J 2005, 88:790-804.
    • (2005) Biophys J , vol.88 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautel, M.4    Grubmuller, H.5
  • 73
    • 67349216078 scopus 로고    scopus 로고
    • Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover
    • Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M. Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover. FEBS Lett 2009, 583:1846-1852.
    • (2009) FEBS Lett , vol.583 , pp. 1846-1852
    • Waters, S.1    Marchbank, K.2    Solomon, E.3    Whitehouse, C.4    Gautel, M.5
  • 76
    • 49049083353 scopus 로고    scopus 로고
    • Signaling in muscle atrophy and hypertrophy
    • Sandri M. Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda) 2008, 23:160-170.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 160-170
    • Sandri, M.1
  • 78
    • 78549249481 scopus 로고    scopus 로고
    • Myomasp/LRRC39, a heart- and muscle-specific protein, is a novel component of the sarcomeric M-band and is involved in stretch sensing
    • Will R.D., Eden M., Just S., Hansen A., Eder A., Frank D., Kuhn C., Seeger T.S., Oehl U., Wiemann S., et al. Myomasp/LRRC39, a heart- and muscle-specific protein, is a novel component of the sarcomeric M-band and is involved in stretch sensing. Circ Res 2010.
    • (2010) Circ Res
    • Will, R.D.1    Eden, M.2    Just, S.3    Hansen, A.4    Eder, A.5    Frank, D.6    Kuhn, C.7    Seeger, T.S.8    Oehl, U.9    Wiemann, S.10
  • 80
    • 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., Wallimann T. Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein. J Mol Biol 2003, 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    Wallimann, T.6
  • 81


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