메뉴 건너뛰기




Volumn 30, Issue 5-6, 2009, Pages 171-185

The vertebrate muscle Z-disc: Sarcomere anchor for structure and signalling

Author keywords

Actin; Alpha actinin; Electron microscopy; Muscle proteins; Z band; Z line

Indexed keywords

ACTININ; MUSCLE PROTEIN;

EID: 75749136013     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-009-9189-6     Document Type: Article
Times cited : (188)

References (91)
  • 2
    • 33745243854 scopus 로고    scopus 로고
    • Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
    • Bang ML, Li X, Littlefield R, Bremner S, Thor A, Knowlton KU, Lieber RL, Chen J (2006) Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. J Cell Biol 173:905-916.
    • (2006) J Cell Biol , vol.173 , pp. 905-916
    • Bang, M.L.1    Li, X.2    Littlefield, R.3    Bremner, S.4    Thor, A.5    Knowlton, K.U.6    Lieber, R.L.7    Chen, J.8
  • 4
    • 39749136535 scopus 로고    scopus 로고
    • Visualization of cardiac muscle thin filaments and measurement of their lengths by electron tomography
    • Burgoyne T, Muhamad F, Luther PK (2008) Visualization of cardiac muscle thin filaments and measurement of their lengths by electron tomography. Cardiovasc Res 77:707-712.
    • (2008) Cardiovasc Res , vol.77 , pp. 707-712
    • Burgoyne, T.1    Muhamad, F.2    Luther, P.K.3
  • 6
    • 24744432501 scopus 로고    scopus 로고
    • Molecular structure of the sarcomere
    • Engel AC, Franzini-Armstrong C (eds), 3rd edn. McGraw-Hill, New York
    • Craig R, Padron R (2004) Molecular structure of the sarcomere. In: Engel AC, Franzini-Armstrong C (eds) Myology, 3rd edn. McGraw-Hill, New York, p 129.
    • (2004) Myology , pp. 129
    • Craig, R.1    Padron, R.2
  • 7
    • 0024518479 scopus 로고
    • Arrangement of filaments and cross-links in the bee flight muscle Z disk by image analysis of oblique sections
    • Deatherage JF, Cheng NQ, Bullard B (1989) Arrangement of filaments and cross-links in the bee flight muscle Z disk by image analysis of oblique sections. J Cell Biol 108:1775-1782.
    • (1989) J Cell Biol , vol.108 , pp. 1775-1782
    • Deatherage, J.F.1    Cheng, N.Q.2    Bullard, B.3
  • 8
    • 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 (1999) Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 98:537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 9
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman EH, Francis N, DeRosier DJ (1982) F-actin is a helix with a random variable twist. Nature 298:131-135.
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 10
    • 0037462474 scopus 로고    scopus 로고
    • Sensing stretch is fundamental
    • Epstein ND, Davis JS (2003) Sensing stretch is fundamental. Cell 112:147-150.
    • (2003) Cell , vol.112 , pp. 147-150
    • Epstein, N.D.1    Davis, J.S.2
  • 12
    • 0034776199 scopus 로고    scopus 로고
    • Telethonin and other new proteins of the Z-disc of skeletal muscle
    • Faulkner G, Lanfranchi G, Valle G (2001) Telethonin and other new proteins of the Z-disc of skeletal muscle. IUBMB Life 51: 275-282.
    • (2001) IUBMB Life , vol.51 , pp. 275-282
    • Faulkner, G.1    Lanfranchi, G.2    Valle, G.3
  • 13
    • 33744494538 scopus 로고    scopus 로고
    • The sarcomeric Z-disc: A nodal point in signalling and disease
    • Frank D, Kuhn C, Katus HA, Frey N (2006) The sarcomeric Z-disc: a nodal point in signalling and disease. J Mol Med 84:446-468.
    • (2006) J Mol Med , vol.84 , pp. 446-468
    • Frank, D.1    Kuhn, C.2    Katus, H.A.3    Frey, N.4
  • 14
    • 0015894257 scopus 로고
    • The structure of a simple Z line
    • Franzini-Armstrong C (1973) The structure of a simple Z line. J Cell Biol 58:630-642.
    • (1973) J Cell Biol , vol.58 , pp. 630-642
    • Franzini-Armstrong, C.1
  • 15
    • 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 (2005) 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 348:151-165.
    • (2005) J Mol Biol , vol.348 , pp. 151-165
    • Franzot, G.1    Sjoblom, B.2    Gautel, M.3    Djinovic, C.K.4
  • 16
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers
    • Gautel M, Goulding D, Bullard B, Weber K, Furst DO (1996) The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers. J Cell Sci 109(Pt 11):2747-2754.
    • (1996) J Cell Sci , vol.109 , Issue.PART 11 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Furst, D.O.5
  • 17
    • 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 (2008) Back to square one: what do we know about the functions of Muscle LIM Protein in the heart? J Muscle Res Cell Motil 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
  • 20
    • 0023584297 scopus 로고
    • Z band dynamics as a function of sarcomere length and the contractile state of muscle
    • Goldstein MA, Michael LH, Schroeter JP, Sass RL (1987) Z band dynamics as a function of sarcomere length and the contractile state of muscle. FASEB J 1:133-142.
    • (1987) FASEB J , vol.1 , pp. 133-142
    • Goldstein, M.A.1    Michael, L.H.2    Schroeter, J.P.3    Sass, R.L.4
  • 21
    • 0023805249 scopus 로고
    • Structural states in the Z band of skeletal muscle correlate with states of active and passive tension
    • Goldstein MA, Michael LH, Schroeter JP, Sass RL (1988) Structural states in the Z band of skeletal muscle correlate with states of active and passive tension. J Gen Physiol 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
  • 23
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier HL, Labeit S (2004) The giant protein titin: a major player in myocardial mechanics, signaling, and disease. CircRes 94:284-295.
    • (2004) CircRes , vol.94 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 25
    • 33947306552 scopus 로고    scopus 로고
    • Novel structures for alpha-actinin: F-actin interactions and their implications for actin membrane attachment and tension sensing in the cytoskeleton
    • Hampton CM, Taylor DW, Taylor KA (2007) Novel structures for alpha-actinin: F-actin interactions and their implications for actin membrane attachment and tension sensing in the cytoskeleton. J Mol Biol 368:92-104.
    • (2007) J Mol Biol , vol.368 , pp. 92-104
    • Hampton, C.M.1    Taylor, D.W.2    Taylor, K.A.3
  • 26
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris BZ, Lim WA (2001) Mechanism and role of PDZ domains in signaling complex assembly. J Cell Sci 114:3219-3231.
    • (2001) J Cell Sci , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 30
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • Kadrmas JL, Beckerle MC (2004) The LIM domain: from the cytoskeleton to the nucleus. Nat Rev Mol Cell Biol 5:920-931.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 31
    • 0001214483 scopus 로고
    • The ultrastructure of the Z disc in skeletal muscle
    • Knappeis GG, Carlsen F (1962) The ultrastructure of the Z disc in skeletal muscle. J Cell Biol 13:323-335.
    • (1962) J Cell Biol , vol.13 , pp. 323-335
    • Knappeis, G.G.1    Carlsen, F.2
  • 33
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit S, Kolmerer B (1995) The complete primary structure of human nebulin and its correlation to muscle structure. J Mol Biol 248:308-315.
    • (1995) J Mol Biol , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 35
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • Lange S, Ehler E, Gautel M (2006) From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol 16:11-18.
    • (2006) Trends Cell Biol , vol.16 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 37
    • 0036839038 scopus 로고    scopus 로고
    • Mechanisms of muscle injury gleaned from animal models
    • Lieber RL, Friden J (2002) Mechanisms of muscle injury gleaned from animal models. Am J Phys Med Rehabil 81:S70-S79.
    • (2002) Am J Phys Med Rehabil , vol.81
    • Lieber, R.L.1    Friden, J.2
  • 38
    • 39749137483 scopus 로고    scopus 로고
    • Sense and stretchability: The role of titin and titinassociated proteins in myocardial stress-sensing and mechanical dysfunction
    • Linke WA (2008) Sense and stretchability: the role of titin and titinassociated 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
  • 39
    • 54549121277 scopus 로고    scopus 로고
    • Thin filament length regulation in striated muscle sarcomeres: Pointed-end dynamics go beyond a nebulin ruler
    • Littlefield RS, Fowler VM (2008) Thin filament length regulation in striated muscle sarcomeres: pointed-end dynamics go beyond a nebulin ruler. Semin Cell Dev Biol 19:511-519.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 511-519
    • Littlefield, R.S.1    Fowler, V.M.2
  • 40
    • 1842474291 scopus 로고    scopus 로고
    • A 3-D reconstruction of smooth muscle alpha-actinin by CryoEm reveals two different conformations at the actin-binding region
    • Liu J, Taylor DW, Taylor KA (2004) A 3-D reconstruction of smooth muscle alpha-actinin by CryoEm reveals two different conformations at the actin-binding region. J Mol Biol 338:115-125.
    • (2004) J Mol Biol , vol.338 , pp. 115-125
    • Liu, J.1    Taylor, D.W.2    Taylor, K.A.3
  • 41
    • 0025720064 scopus 로고
    • Three-dimensional reconstruction of a simple Z-band in fish muscle
    • Luther PK (1991) Three-dimensional reconstruction of a simple Z-band in fish muscle. J Cell Biol 113:1043-1055.
    • (1991) J Cell Biol , vol.113 , pp. 1043-1055
    • Luther, P.K.1
  • 42
    • 0034010881 scopus 로고    scopus 로고
    • Three-dimensional structure of a vertebrate muscle Z-band: Implications for titin and alpha-actinin binding
    • Luther PK (2000) Three-dimensional structure of a vertebrate muscle Z-band: implications for titin and alpha-actinin binding. J Struct Biol 129:1-16.
    • (2000) J Struct Biol , vol.129 , pp. 1-16
    • Luther, P.K.1
  • 43
    • 0036301051 scopus 로고    scopus 로고
    • Muscle Z-band ultrastructure: Titin Z-repeats and Z-band periodicities do not match
    • Luther PK, Squire JM (2002) Muscle Z-band ultrastructure: titin Z-repeats and Z-band periodicities do not match. J Mol Biol 319:1157-1164.
    • (2002) J Mol Biol , vol.319 , pp. 1157-1164
    • Luther, P.K.1    Squire, J.M.2
  • 44
    • 0036297519 scopus 로고    scopus 로고
    • The three-dimensional structure of a vertebrate wide (slow muscle) Z-band: Lessons on Z-band assembly
    • Luther PK, Barry JS, Squire JM (2002) The three-dimensional structure of a vertebrate wide (slow muscle) Z-band: lessons on Z-band assembly. J Mol Biol 315:9-20.
    • (2002) J Mol Biol , vol.315 , pp. 9-20
    • Luther, P.K.1    Barry, J.S.2    Squire, J.M.3
  • 45
    • 0042235366 scopus 로고    scopus 로고
    • Heterogeneity of Z-band structure within a single muscle sarcomere: Implications for sarcomere assembly
    • Luther PK, Padron R, Ritter S, Craig R, Squire JM (2003) Heterogeneity of Z-band structure within a single muscle sarcomere: implications for sarcomere assembly. J Mol Biol 332:161-169.
    • (2003) J Mol Biol , vol.332 , pp. 161-169
    • Luther, P.K.1    Padron, R.2    Ritter, S.3    Craig, R.4    Squire, J.M.5
  • 47
    • 0028176006 scopus 로고
    • Determination of the alphaactinin-binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough A, Way M, DeRosier D (1994) Determination of the alphaactinin- binding site on actin filaments by cryoelectron microscopy and image analysis. J Cell Biol 126:433-443.
    • (1994) J Cell Biol , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    DeRosier, D.3
  • 48
    • 0015506180 scopus 로고
    • Structure of insect fibrillar flight muscle in the presence and absence of ATP
    • Miller A, Tregear RT (1972) Structure of insect fibrillar flight muscle in the presence and absence of ATP. J Mol Biol 70:85-104.
    • (1972) J Mol Biol , vol.70 , pp. 85-104
    • Miller, A.1    Tregear, R.T.2
  • 50
    • 0028784365 scopus 로고
    • Nebulette: A 107 kD nebulin-like protein in cardiac muscle
    • Moncman CL, Wang K (1995) Nebulette: a 107 kD nebulin-like protein in cardiac muscle. Cell Motil Cytoskeleton 32:205-225.
    • (1995) Cell Motil Cytoskeleton , vol.32 , pp. 205-225
    • Moncman, C.L.1    Wang, K.2
  • 51
    • 0025606398 scopus 로고
    • The three-dimensional structure of the nemaline rod Z-band
    • Morris EP, Nneji G, Squire JM (1990) The three-dimensional structure of the nemaline rod Z-band. J Cell Biol 111:2961-2978.
    • (1990) J Cell Biol , vol.111 , pp. 2961-2978
    • Morris, E.P.1    Nneji, G.2    Squire, J.M.3
  • 52
    • 33751567905 scopus 로고    scopus 로고
    • Structural basis of actin filament capping at the barbed-end: A cryo-electron microscopy study
    • Narita A, Takeda S, Yamashita A, Maeda Y (2006) Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. EMBO J 25:5626-5633.
    • (2006) EMBO J , vol.25 , pp. 5626-5633
    • Narita, A.1    Takeda, S.2    Yamashita, A.3    Maeda, Y.4
  • 53
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T, Iwasa M, Aihara T, Maeda Y, Narita A (2009) The nature of the globular- to fibrous-actin transition. Nature 457:441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maeda, Y.4    Narita, A.5
  • 54
    • 0031560933 scopus 로고    scopus 로고
    • The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of alpha-actinin
    • Ohtsuka H, Yajima H, Maruyama K, Kimura S (1997) The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of alpha-actinin. Biochem Biophys Res Commun 235:1-3.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 1-3
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 55
    • 0016185074 scopus 로고
    • Localization of troponin in thin filament and tropomyosin paracrystal
    • Ohtsuki I (1974) Localization of troponin in thin filament and tropomyosin paracrystal. J Biochem 75:753-765.
    • (1974) J Biochem , vol.75 , pp. 753-765
    • Ohtsuki, I.1
  • 56
    • 2442481067 scopus 로고    scopus 로고
    • Alpha-actinin revisited: A fresh look at an old player
    • Otey CA, Carpen O (2004) Alpha-actinin revisited: a fresh look at an old player. Cell Motil Cytoskeleton 58:104-111.
    • (2004) Cell Motil Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 58
    • 48249127189 scopus 로고    scopus 로고
    • Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc
    • Pappas CT, Bhattacharya N, Cooper JA, Gregorio CC (2008) Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc. Mol Biol Cell 19:1837-1847.
    • (2008) Mol Biol Cell , vol.19 , pp. 1837-1847
    • Pappas, C.T.1    Bhattacharya, N.2    Cooper, J.A.3    Gregorio, C.C.4
  • 59
    • 0034175815 scopus 로고    scopus 로고
    • Oracle, a novel PDZ-LIM domain protein expressed in heart and skeletal muscle
    • Passier R, Richardson JA, Olson EN (2000) Oracle, a novel PDZ-LIM domain protein expressed in heart and skeletal muscle. Mech Dev 92:277-284.
    • (2000) Mech Dev , vol.92 , pp. 277-284
    • Passier, R.1    Richardson, J.A.2    Olson, E.N.3
  • 60
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M, Winder SJ, Pastore A (1994) Nebulin, a helical actin binding protein. EMBO J 13:1782-1789.
    • (1994) EMBO J , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 61
    • 1242320058 scopus 로고    scopus 로고
    • At the crossroads of myocardial signaling: The role of Z-discs in intracellular signaling and cardiac function
    • Pyle WG, Solaro RJ (2004) At the crossroads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function. Circ Res 94:296-305.
    • (2004) Circ Res , vol.94 , pp. 296-305
    • Pyle, W.G.1    Solaro, R.J.2
  • 62
    • 37549005604 scopus 로고    scopus 로고
    • Actin structure and function: What we still do not understand
    • Reisler E, Egelman EH (2007) Actin structure and function: what we still do not understand. J Biol Chem 282:36133-36137.
    • (2007) J Biol Chem , vol.282 , pp. 36133-36137
    • Reisler, E.1    Egelman, E.H.2
  • 63
    • 0015618813 scopus 로고
    • The ultrastructure of Z disks from white, intermediate, and red fibers of mammalian striated muscles
    • Rowe RW (1973) The ultrastructure of Z disks from white, intermediate, and red fibers of mammalian striated muscles. J Cell Biol 57:261-277.
    • (1973) J Cell Biol , vol.57 , pp. 261-277
    • Rowe, R.W.1
  • 65
    • 0029952579 scopus 로고    scopus 로고
    • Threedimensional structure of the Z band in a normal mammalian skeletal muscle
    • Schroeter JP, Bretaudiere JP, Sass RL, Goldstein MA (1996) Threedimensional structure of the Z band in a normal mammalian skeletal muscle. J Cell Biol 133:571-583.
    • (1996) J Cell Biol , vol.133 , pp. 571-583
    • Schroeter, J.P.1    Bretaudiere, J.P.2    Sass, R.L.3    Goldstein, M.A.4
  • 66
    • 1942473823 scopus 로고    scopus 로고
    • Mutations in myotilin cause myofibrillar myopathy
    • Selcen D, Engel AG (2004) Mutations in myotilin cause myofibrillar myopathy. Neurology 62:1363-1371.
    • (2004) Neurology , vol.62 , pp. 1363-1371
    • Selcen, D.1    Engel, A.G.2
  • 67
    • 36049003590 scopus 로고    scopus 로고
    • "Z"eroing in on the role of cypher in striated muscle function, signaling, and human disease
    • Sheikh F, Bang ML, Lange S, Chen J (2007) "Z"eroing in on the role of cypher in striated muscle function, signaling, and human disease. Trends Cardiovasc Med 17:258-262.
    • (2007) Trends Cardiovasc Med , vol.17 , pp. 258-262
    • Sheikh, F.1    Bang, M.L.2    Lange, S.3    Chen, J.4
  • 72
    • 0015527096 scopus 로고
    • Studies on purified alpha-actinin. II. Electron microscopic studies on the competitive binding of alpha-actinin and tropomyosin to Z-line extracted myofibrils
    • Stromer MH, Goll DE (1972) Studies on purified alpha-actinin. II. Electron microscopic studies on the competitive binding of alpha-actinin and tropomyosin to Z-line extracted myofibrils. J Mol Biol 67:489-494.
    • (1972) J Mol Biol , vol.67 , pp. 489-494
    • Stromer, M.H.1    Goll, D.E.2
  • 73
    • 0024560073 scopus 로고
    • Alpha-actinin is a component of the Z-filament, a structural backbone of skeletal muscle Z-disks
    • Takahashi K, Hattori A (1989) Alpha-actinin is a component of the Z-filament, a structural backbone of skeletal muscle Z-disks. J Biochem (Tokyo) 105:529-536.
    • (1989) J Biochem (Tokyo) , vol.105 , pp. 529-536
    • Takahashi, K.1    Hattori, A.2
  • 74
    • 0035919832 scopus 로고    scopus 로고
    • The three-dimensional structure of alpha-actinin obtained by cryoelectron microscopy suggests a model for Ca(2 +)-dependent actin binding
    • Tang J, Taylor DW, Taylor KA (2001) The three-dimensional structure of alpha-actinin obtained by cryoelectron microscopy suggests a model for Ca(2 +)-dependent actin binding. J Mol Biol 310:845-858.
    • (2001) J Mol Biol , vol.310 , pp. 845-858
    • Tang, J.1    Taylor, D.W.2    Taylor, K.A.3
  • 76
    • 0027208163 scopus 로고
    • Filament lengths in frog semitendinosus and tibialis anterior muscle fibres
    • Trombitas K, Frey L, Pollack GH (1993) Filament lengths in frog semitendinosus and tibialis anterior muscle fibres. J Muscle Res Cell Motil 14:167-172.
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 167-172
    • Trombitas, K.1    Frey, L.2    Pollack, G.H.3
  • 77
    • 0025744006 scopus 로고
    • Vertebrate muscle Z-line structure: An electron microscopic study of negatively-stained myofibrils
    • Tskhovrebova LA (1991) Vertebrate muscle Z-line structure: an electron microscopic study of negatively-stained myofibrils. J Muscle Res Cell Motil 12:425-438.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 425-438
    • Tskhovrebova, L.A.1
  • 78
  • 79
    • 0028283285 scopus 로고
    • The muscle Z band: Lessons in stress management
    • Vigoreaux JO (1994) The muscle Z band: lessons in stress management. J Muscle Res Cell Motil 15:237-255.
    • (1994) J Muscle Res Cell Motil , vol.15 , pp. 237-255
    • Vigoreaux, J.O.1
  • 80
    • 59249091710 scopus 로고    scopus 로고
    • A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: A common link for Z-disc myopathies
    • von Nandelstadh P, Ismail M, Gardin C, Suila H, Zara I, Belgrano A, Valle G, Carpen O, Faulkner G (2009) A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies. Mol Cell Biol 29:822-834.
    • (2009) Mol Cell Biol , vol.29 , pp. 822-834
    • Von, N.P.1    Ismail, M.2    Gardin, C.3    Suila, H.4    Zara, I.5    Belgrano, A.6    Valle, G.7    Carpen, O.8    Faulkner, G.9
  • 81
    • 30644474315 scopus 로고    scopus 로고
    • 138th ENMC workshop: Nemaline myopathy, 20-22 May 2005, Naarden, The Netherlands
    • Wallgren-Pettersson C, Laing NG (2006) 138th ENMC workshop: nemaline myopathy, 20-22 May 2005, Naarden, The Netherlands. Neuromuscul Disord 16:54-60.
    • (2006) Neuromuscul Disord , vol.16 , pp. 54-60
    • Wallgren-Pettersson, C.1    Laing, N.G.2
  • 82
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line
    • Wang K, Wright J (1988) Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J Cell Biol 107:2199-2212.
    • (1988) J Cell Biol , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 83
    • 33748058496 scopus 로고    scopus 로고
    • Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo
    • Witt CC, Burkart C, Labeit D, McNabb M, Wu Y, Granzier H, Labeit S (2006) Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J 25:3843-3855.
    • (2006) EMBO J , vol.25 , pp. 3843-3855
    • Witt, C.C.1    Burkart, C.2    Labeit, D.3    McNabb, M.4    Wu, Y.5    Granzier, H.6    Labeit, S.7
  • 84
    • 0020609619 scopus 로고
    • Properties of soleus muscle Z-lines and induced Z-line analogs revealed by dissection with Ca2 + -activated neutral protease
    • Yamaguchi M, Robson RM, Stromer MH, Cholvin NR, Izumimoto M (1983) Properties of soleus muscle Z-lines and induced Z-line analogs revealed by dissection with Ca2 + -activated neutral protease. Anat Rec 206:345-362.
    • (1983) Anat Rec , vol.206 , pp. 345-362
    • Yamaguchi, M.1    Robson, R.M.2    Stromer, M.H.3    Cholvin, N.R.4    Izumimoto, M.5
  • 85
    • 0022259764 scopus 로고
    • Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture
    • Yamaguchi M, Izumimoto M, Robson RM, Stromer MH (1985) Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture. J Mol Biol 184:621-643.
    • (1985) J Mol Biol , vol.184 , pp. 621-643
    • Yamaguchi, M.1    Izumimoto, M.2    Robson, R.M.3    Stromer, M.H.4
  • 86
    • 0037387121 scopus 로고    scopus 로고
    • Crystal structure of CapZ: Structural basis for actin filament barbed end capping
    • Yamashita A, Maeda K, Maeda Y (2003) Crystal structure of CapZ: structural basis for actin filament barbed end capping. EMBO J 22:1529-1538.
    • (2003) EMBO J , vol.22 , pp. 1529-1538
    • Yamashita, A.1    Maeda, K.2    Maeda, Y.3
  • 87
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
    • Ylanne J, Scheffzek K, Young P, Saraste M (2001) Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure (Camb) 9:597-604.
    • (2001) Structure (Camb) , vol.9 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 88
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of alpha-actinin
    • Young P, Ferguson C, Banuelos S, Gautel M (1998) Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. EMBO J 17:1614-1624.
    • (1998) EMBO J , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 90
    • 0034643946 scopus 로고    scopus 로고
    • Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure
    • Zolk O, Caroni P, Bohm M (2000) Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure. Circulation 101:2674-2677.
    • (2000) Circulation , vol.101 , pp. 2674-2677
    • Zolk, O.1    Caroni, P.2    Bohm, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.