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0030091595
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Cytoskeleton: Titin as a scaffold and spring
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Trinick J Cytoskeleton: titin as a scaffold and spring. Curr Biol. 6:1996;258-260.
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Curr Biol
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Trinick, J.1
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0025782315
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Molecular analysis of protein assembly in muscle development
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Epstein HF, Fischman DA Molecular analysis of protein assembly in muscle development. Science. 251:1991;1039-1044.
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Epstein, H.F.1
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0029888857
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Tropomodulin function and thin filament assembly in cardiac myocytes
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Gregorio CC, Fowler VM Tropomodulin function and thin filament assembly in cardiac myocytes. Trends Cardiovasc Med. 6:1996;136-141.
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0029896830
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Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
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Schiaffino S, Reggiani C Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev. 76:1996;371-423.
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Schiaffino, S.1
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0028824480
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Titins, giant proteins in charge of muscle ultrastructure and elasticity
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Labeit S, Kolmerer B Titins, giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:1995;293-296.
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Science
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Labeit, S.1
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12644315058
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Refined localization of the genes for nebulin and titin genes on chromosome 2q allows the assignment of nebulin as a candidate gene for autosomal recessive nemaline myopathy
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High resolution radiation hybrid mapping of the titin and nebulin gene loci in humans demonstrates that both genes are located on the long arm of chromosome 2, a few megabases apart. Nebulin, but not titin, is linked to the most common form of nemaline myopathy (the autosomal recessive 'main stream' form). Affected patients have pronounced muscle weakness and inclusion bodies in their myocytes which represent abnormal Z-disc protein assemblies.
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Pelin K, Ridanpää M, Donner K, Laing N, Kolmerer B, Millevoi S, Labeit S, Chapelle A, Wallgren-Pettersson C Refined localization of the genes for nebulin and titin genes on chromosome 2q allows the assignment of nebulin as a candidate gene for autosomal recessive nemaline myopathy. Eur J Hum Genet. 5:1997;229-234. High resolution radiation hybrid mapping of the titin and nebulin gene loci in humans demonstrates that both genes are located on the long arm of chromosome 2, a few megabases apart. Nebulin, but not titin, is linked to the most common form of nemaline myopathy (the autosomal recessive 'main stream' form). Affected patients have pronounced muscle weakness and inclusion bodies in their myocytes which represent abnormal Z-disc protein assemblies.
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(1997)
Eur J Hum Genet
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Pelin, K.1
Ridanpää, M.2
Donner, K.3
Laing, N.4
Kolmerer, B.5
Millevoi, S.6
Labeit, S.7
Chapelle, A.8
Wallgren-Pettersson, C.9
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7
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0032484034
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The assembly of immunoglobulin-like modules in titin: Implications for muscle elasticity
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A structural study of expressed tandem Ig repeats from I-band titin using nuclear magnetic resonance and small angle X-ray scattering techniques. Shortening of the tandem Ig segments may result from the bending of interdomain linker regions.
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Improta S, Krueger JK, Gautel M, Atkinson RA, Lefevre JF, Moulton S, Trewhella J, Pastore A The assembly of immunoglobulin-like modules in titin: implications for muscle elasticity. J Mol Biol. 284:1998;761-777. A structural study of expressed tandem Ig repeats from I-band titin using nuclear magnetic resonance and small angle X-ray scattering techniques. Shortening of the tandem Ig segments may result from the bending of interdomain linker regions.
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J Mol Biol
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, pp. 761-777
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Improta, S.1
Krueger, J.K.2
Gautel, M.3
Atkinson, R.A.4
Lefevre, J.F.5
Moulton, S.6
Trewhella, J.7
Pastore, A.8
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8
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0038083197
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The three-dimensional structure of a type I module from titin: A prototype of intracellular fibronectin type III domains
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The three-dimensional structure of an A-band FNIII domain was determined by nuclear magnetic resonance. This is the first solved structure of an intracellular member of the FNIII superfamily. Interestingly, the prolines are found to be clustered on one surface of the domain and constitute two polyproline helix II conformations. Since the proline residues are conserved within the titin FNIII family, they might attach titin to the thick filaments in a conserved fashion.
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Muhle-Goll C, Pastore A, Nilges M The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains. Structure. 6:1998;1291-1302. The three-dimensional structure of an A-band FNIII domain was determined by nuclear magnetic resonance. This is the first solved structure of an intracellular member of the FNIII superfamily. Interestingly, the prolines are found to be clustered on one surface of the domain and constitute two polyproline helix II conformations. Since the proline residues are conserved within the titin FNIII family, they might attach titin to the thick filaments in a conserved fashion.
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(1998)
Structure
, vol.6
, pp. 1291-1302
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Muhle-Goll, C.1
Pastore, A.2
Nilges, M.3
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9
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0023924769
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The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
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Fürst DO, Osborn M, Nave R, Weber K The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J Cell Biol. 106:1988;1563-1572.
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J Cell Biol
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Fürst, D.O.1
Osborn, M.2
Nave, R.3
Weber, K.4
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10
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0032538660
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The NH2 terminus of titin spans the Z-disc: Its interaction with a novel 19 kD ligand (T-cap) is required for sarcomeric integrity
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This study focuses on the molecular interactions of Z-line titin. Results demonstrate the molecular layout of titin within the Z-line: mammalian titins have at least four potential binding sites for α-actinin, and the amino-terminal titin Z1 and Z2 repeats bind to a novel 19 kDa protein, referred to as titin-cap (T-cap). Using dominant-negative approaches in cardiac myocytes, the interaction of titin Z1 and Z2 domains with T-cap is shown to be required for the structural integrity of sarcomeres.
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Gregorio CC, Trombitás K, Centner T, Kolmerer B, Stier G, Kunke K, Suzuki K, Obermayr F, Herrmann B, Granzier Het al. The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19 kD ligand (T-cap) is required for sarcomeric integrity. J Cell Biol. 143:1998;1013-1027. This study focuses on the molecular interactions of Z-line titin. Results demonstrate the molecular layout of titin within the Z-line: mammalian titins have at least four potential binding sites for α-actinin, and the amino-terminal titin Z1 and Z2 repeats bind to a novel 19 kDa protein, referred to as titin-cap (T-cap). Using dominant-negative approaches in cardiac myocytes, the interaction of titin Z1 and Z2 domains with T-cap is shown to be required for the structural integrity of sarcomeres.
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(1998)
J Cell Biol
, vol.143
, pp. 1013-1027
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Gregorio, C.C.1
Trombitás, K.2
Centner, T.3
Kolmerer, B.4
Stier, G.5
Kunke, K.6
Suzuki, K.7
Obermayr, F.8
Herrmann, B.9
Granzier, H.10
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11
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0031715047
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A survey of the primary structure and the interspecies conservation of I-band titin's elastic elements in vertebrates
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This study shows that the differentially expressed tandem Ig repeats in I-band titin's elastic region form a specific subgroup of the titin Ig repeat family and differ structurally from those expressed elsewhere in the molecule.
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Witt CC, Olivieri N, Centner T, Kolmerer B, Millevoi S, Labeit D, Jockusch H, Pastore A, Labeit S A survey of the primary structure and the interspecies conservation of I-band titin's elastic elements in vertebrates. J Struct Biol. 122:1998;1-10. This study shows that the differentially expressed tandem Ig repeats in I-band titin's elastic region form a specific subgroup of the titin Ig repeat family and differ structurally from those expressed elsewhere in the molecule.
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(1998)
J Struct Biol
, vol.122
, pp. 1-10
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Witt, C.C.1
Olivieri, N.2
Centner, T.3
Kolmerer, B.4
Millevoi, S.5
Labeit, D.6
Jockusch, H.7
Pastore, A.8
Labeit, S.9
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12
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0029836627
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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
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Obermann WM, Gautel M, Steiner F, van der Ven PF, Weber K, Fürst DO 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. 134:1996;1441-1453.
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J Cell Biol
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Obermann, W.M.1
Gautel, M.2
Steiner, F.3
Van Der Ven, P.F.4
Weber, K.5
Fürst, D.O.6
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13
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0031034775
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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
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A thorough study of the layout and molecular interactions of M-line titin. The carboxy-terminal 200 kDa of the titin filament spans the entire M-line region; Ig repeats inside the M-line region may provide attachment sites for the M-line protein myomesin.
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Obermann WM, Gautel M, Weber K, Fürst DO 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. 16:1997;211-220. A thorough study of the layout and molecular interactions of M-line titin. The carboxy-terminal 200 kDa of the titin filament spans the entire M-line region; Ig repeats inside the M-line region may provide attachment sites for the M-line protein myomesin.
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(1997)
EMBO J
, vol.16
, pp. 211-220
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Obermann, W.M.1
Gautel, M.2
Weber, K.3
Fürst, D.O.4
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14
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0032508463
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Characterization of nebulette and nebulin and emerging concepts of their roles for vertebrate Z-discs
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Millevoi and colleagues report the cloning, full-length sequence and gene mapping of nebulette, a nebulin-related protein from cardiac muscle. Both nebulin and nebulette are filamentous proteins that insert into the periphery of the Z-line. Similar to titin's 45-residue Z-repeats, nebulin/nebulette also contain a family of differentially expressed Z-repeats. It is likely that the differential expression of titin and nebulin/nebulette accounts for Z-line tissue diversity.
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Millevoi S, Trombitas K, Kostin S, Schaper J, Pelin K, Kolmerer B, Granzier H, Labeit S Characterization of nebulette and nebulin and emerging concepts of their roles for vertebrate Z-discs. J Mol Biol. 282:1998;111-123. Millevoi and colleagues report the cloning, full-length sequence and gene mapping of nebulette, a nebulin-related protein from cardiac muscle. Both nebulin and nebulette are filamentous proteins that insert into the periphery of the Z-line. Similar to titin's 45-residue Z-repeats, nebulin/nebulette also contain a family of differentially expressed Z-repeats. It is likely that the differential expression of titin and nebulin/nebulette accounts for Z-line tissue diversity.
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(1998)
J Mol Biol
, vol.282
, pp. 111-123
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Millevoi, S.1
Trombitas, K.2
Kostin, S.3
Schaper, J.4
Pelin, K.5
Kolmerer, B.6
Granzier, H.7
Labeit, S.8
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15
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0028784365
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Nebulette: A 107 kD nebulin-like protein in cardiac muscle
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Moncman CL, Wang K Nebulette: a 107 kD nebulin-like protein in cardiac muscle. Cell Motil Cytoskeleton. 32:1995;205-225.
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Cell Motil Cytoskeleton
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Moncman, C.L.1
Wang, K.2
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16
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0015527081
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Studies on purified α-actinin. I. Effect of temperature and tropomyosin on the α-actinin/F-actin interaction
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Goll DE, Suzuki A, Temple J, Holmes GR Studies on purified α-actinin. I. Effect of temperature and tropomyosin on the α-actinin/F-actin interaction. J Mol Biol. 67:1972;469-488.
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Goll, D.E.1
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Temple, J.3
Holmes, G.R.4
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17
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0030967587
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Architecture and function in the muscle sarcomere
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A very stimulating review on recent progress on the structural biology of the sarcomere.
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Squire JM Architecture and function in the muscle sarcomere. Curr Opin Struct Biol. 7:1997;247-257. A very stimulating review on recent progress on the structural biology of the sarcomere.
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Curr Opin Struct Biol
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Squire, J.M.1
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18
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0028283285
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The muscle Z band: Lessons in stress management
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Vigoreaux JO The muscle Z band: lessons in stress management. J Muscle Res Cell Motil. 15:1994;237-255.
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Vigoreaux, J.O.1
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19
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0032557642
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Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin
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Mues A, van der Ven PFM, Young P, Fürst DO, Gautel M Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett. 428:1998;111-114.
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FEBS Lett
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Mues, A.1
Van Der Ven, P.F.M.2
Young, P.3
Fürst, D.O.4
Gautel, M.5
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20
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0029859276
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The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers
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Gautel M, Goulding D, Bullard B, Weber K, Fürst DO The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers. J Cell Sci. 109:1996;2747-2754.
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Gautel, M.1
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Bullard, B.3
Weber, K.4
Fürst, D.O.5
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22
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0031213849
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Tissue-specific expression and alpha-actinin binding properties of the Z-disc titin: Implications for the nature of vertebrate Z-discs
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••] show that the 10 kDa carboxy-terminal domain of α-actinin binds to titin's 45-residue Z-repeats. Thus, antiparallel α-actinin dimers can attach at both ends to titin filaments, whereas their amino termini can cross-link them to thin filaments. The Z-repeats are shown to be expressed in different copy numbers in different tissues, possibly accounting for the variability of Z-filaments in different muscle types.
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••] show that the 10 kDa carboxy-terminal domain of α-actinin binds to titin's 45-residue Z-repeats. Thus, antiparallel α-actinin dimers can attach at both ends to titin filaments, whereas their amino termini can cross-link them to thin filaments. The Z-repeats are shown to be expressed in different copy numbers in different tissues, possibly accounting for the variability of Z-filaments in different muscle types.
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(1998)
J Mol Biol
, vol.270
, pp. 688-695
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Sorimachi, H.1
Freiburg, A.2
Kolmerer, B.3
Ishiura, S.4
Stier, G.5
Gregorio, C.C.6
Labeit, D.7
Linke, W.A.8
Suzuki, K.9
Labeit, S.10
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23
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0032536770
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Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
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Besides confirming the interaction of titin's Z-repeats with α-actinin, Young and colleagues identified that a single site at the periphery of Z-disc titin also may bind to α-actinin. This site just flanks the Z-repeats and, in contrast to them, does not bind to the carboxy-terminal end of α-actinin, but to the central rod domains (R2-R3) containing spectrin-like repeats. Thus, titin may contain two distinct α-actinin binding motifs.
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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. 17:1998;1614-1624. Besides confirming the interaction of titin's Z-repeats with α-actinin, Young and colleagues identified that a single site at the periphery of Z-disc titin also may bind to α-actinin. This site just flanks the Z-repeats and, in contrast to them, does not bind to the carboxy-terminal end of α-actinin, but to the central rod domains (R2-R3) containing spectrin-like repeats. Thus, titin may contain two distinct α-actinin binding motifs.
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(1998)
EMBO J
, vol.17
, pp. 1614-1624
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Young, P.1
Ferguson, C.2
Bañuelos, S.3
Gautel, M.4
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26
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0030855930
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Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction
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•]. Therefore, this part of I-band titin is predicted to interact with actin.
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•]. Therefore, this part of I-band titin is predicted to interact with actin.
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Biophys J
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Granzier, H.1
Kellermayer, M.2
Trombitas, K.3
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27
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13344285357
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Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence
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Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa N, Sorimachi N, Shimada H, Tagawa K, Maruyama K, Suzuki K Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem. 270:1995;31158-31162.
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Sorimachi, H.1
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Sorimachi, N.7
Shimada, H.8
Tagawa, K.9
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Suzuki, K.11
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0029919189
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Genomic organization of the M line titin and its tissue-specific expression in two distinct isoforms
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Kolmerer B, Olivieri N, Witt CC, Herrmann BG, Labeit S Genomic organization of the M line titin and its tissue-specific expression in two distinct isoforms. J Mol Biol. 256:1996;556-563.
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Towards a molecular understanding of titin
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Labeit S, Gautel M, Lakey A, Trinick J Towards a molecular understanding of titin. EMBO J. 11:1992;1711-1716.
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0030052266
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A molecular map of the interaction between titin and myosin-binding protein C. Implications for sarcomeric assembly in familiar hypertrophic cardiomyopathy
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Freiburg A, Gautel M A molecular map of the interaction between titin and myosin-binding protein C. Implications for sarcomeric assembly in familiar hypertrophic cardiomyopathy. Eur J Biochem. 235:1996;317-323.
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0027515217
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The major myosin-binding domain of skeletal muscle MyBP-C (Cprotein) resides in the COOH-terminal, immunoglobulin C2 motif
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Okagaki T, Weber FE, Fischman DA, Vaughan KT, Mikawa T, Reinach FC The major myosin-binding domain of skeletal muscle MyBP-C (Cprotein) resides in the COOH-terminal, immunoglobulin C2 motif. J Cell Biol. 123:1993;619-626.
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Okagaki, T.1
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33
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0030576501
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Towards a molecular understanding of the elasticity of titin
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Linke WA, Ivemeyer M, Olivieri N, Kolmerer B, Rüegg JC, Labeit S Towards a molecular understanding of the elasticity of titin. J Mol Biol. 261:1996;62-71.
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Linke, W.A.1
Ivemeyer, M.2
Olivieri, N.3
Kolmerer, B.4
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Labeit, S.6
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34
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0031809493
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Characterizing titin's I-band Ig domain region as an entropic spring
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•] use intact myofibrils to characterize the behavior of the tandem Ig and PEVK titin segments, and conclude that they may act as a two-spring system.
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•] use intact myofibrils to characterize the behavior of the tandem Ig and PEVK titin segments, and conclude that they may act as a two-spring system.
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(1998)
J Cell Sci
, vol.111
, pp. 1567-1574
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Linke, W.A.1
Stockmeier, M.R.2
Ivemeyer, M.3
Hosser, H.4
Mundel, P.5
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35
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0027246620
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Phosphorylation of KSP-motifs in the C-terminal region of titin in differentiating myoblasts
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Gautel M, Leonard K, Labeit S Phosphorylation of KSP-motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J. 12:1993;3827-3834.
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EMBO J
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Gautel, M.1
Leonard, K.2
Labeit, S.3
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36
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0029949254
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Partial characterization of zeugmatin indicates that it is part of the Z-band region of titin
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Turnacioglu KK, Mittal B, Sanger JM, Sanger JW Partial characterization of zeugmatin indicates that it is part of the Z-band region of titin. Cell Motil Cytoskeleton. 34:1996;108-121.
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Cell Motil Cytoskeleton
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Turnacioglu, K.K.1
Mittal, B.2
Sanger, J.M.3
Sanger, J.W.4
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37
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0030913881
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Constitutive and variable regions of Z-disk titin/connectin in myofibril formation: A dominant-negative screen
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Peckham M, Young P, Gautel M Constitutive and variable regions of Z-disk titin/connectin in myofibril formation: a dominant-negative screen. Cell Struct Funct. 22:1997;95-101.
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Cell Struct Funct
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Peckham, M.1
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Gautel, M.3
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38
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0032528461
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Dispensability of the actin-binding site and spectrin repeats for targeting sarcomeric α-actinin into maturing Z bands in vivo: Implications for in vitro binding studies
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An elegant study investigating the roles of specific domains of α-actinin in the initial targeting and maintenance of striated myofibrils. This study indicates the limited value of predicting the behavior of sarcomeric components based on in vitro binding studies.
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Lin Z, Kijikata T, Zhang Z, Choi J, Holtzer S, Sweeney HS, Holtzer H Dispensability of the actin-binding site and spectrin repeats for targeting sarcomeric α-actinin into maturing Z bands in vivo: implications for in vitro binding studies. Development. 199:1998;291-308. An elegant study investigating the roles of specific domains of α-actinin in the initial targeting and maintenance of striated myofibrils. This study indicates the limited value of predicting the behavior of sarcomeric components based on in vitro binding studies.
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(1998)
Development
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Lin, Z.1
Kijikata, T.2
Zhang, Z.3
Choi, J.4
Holtzer, S.5
Sweeney, H.S.6
Holtzer, H.7
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41
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0031006659
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Elasticity and unfolding of single molecules of the giant muscle protein titin
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••] are pioneering studies in which single titin molecules were manipulated and titin's force-extension properties were characterized at the molecular level. The results obtained reveal that titin behaves as an entropic spring. Unfolding takes place at high force during stretching of the molecule, and refolding at low force during release of the molecule.
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••] are pioneering studies in which single titin molecules were manipulated and titin's force-extension properties were characterized at the molecular level. The results obtained reveal that titin behaves as an entropic spring. Unfolding takes place at high force during stretching of the molecule, and refolding at low force during release of the molecule.
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(1997)
Nature
, vol.387
, pp. 308-312
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Tskhovrebova, L.1
Trinick, J.2
Sleep, J.A.3
Simmons, R.M.4
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43
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0032493281
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Nature of PEVK-titin elasticity in skeletal muscle
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••] use novel epitope-mapped antibodies to monitor the mechanical behavior of central I-band titin during myofibrillar stretch. They prove that the PEVK (in the single letter code for amino acids) region of titin acts as a highly extensible spring element which is responsible for the passive tension response of the titin filament.
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••] use novel epitope-mapped antibodies to monitor the mechanical behavior of central I-band titin during myofibrillar stretch. They prove that the PEVK (in the single letter code for amino acids) region of titin acts as a highly extensible spring element which is responsible for the passive tension response of the titin filament.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 8052-8057
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Linke, W.A.1
Ivemeyer, M.2
Mundel, P.3
Stockmeyer, M.R.4
Kolmerer, B.5
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44
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0031006187
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Independent assembly of 1.6 Mm long bipolar MHC filaments and I-Z-I bodies
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Holtzer H, Hijikata T, Lin ZX, Zhang ZQ, Holtzer S, Protasi F, Frazini-Armstrong C, Sweeney HL Independent assembly of 1.6 Mm long bipolar MHC filaments and I-Z-I bodies. Cell Struct Funct. 22:1997;83-93.
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(1997)
Cell Struct Funct
, vol.22
, pp. 83-93
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Holtzer, H.1
Hijikata, T.2
Lin, Z.X.3
Zhang, Z.Q.4
Holtzer, S.5
Protasi, F.6
Frazini-Armstrong, C.7
Sweeney, H.L.8
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45
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0032578901
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Structural basis for activation of the titin kinase domain during myofibrillogenesis
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A pioneering study which reports the three-dimensional structure of the titin kinase domain and may provide a molecular understanding of its mode of activation. The Z-disc protein and titin ligand T-cap(telethonin) has been identified as a potential substrate of the titin kinase domain using in vitro phosphorylation assays. Thereby, M-line and Z-disc assembly might be coordinated during myofibrilogenesis.
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Mayans O, van der Ven P, Wilm M, Mues A, Young P, Fürst DO, Wilmanns M, Gautel M Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature. 395:1998;863-869. A pioneering study which reports the three-dimensional structure of the titin kinase domain and may provide a molecular understanding of its mode of activation. The Z-disc protein and titin ligand T-cap(telethonin) has been identified as a potential substrate of the titin kinase domain using in vitro phosphorylation assays. Thereby, M-line and Z-disc assembly might be coordinated during myofibrilogenesis.
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(1998)
Nature
, vol.395
, pp. 863-869
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Mayans, O.1
Van Der Ven, P.2
Wilm, M.3
Mues, A.4
Young, P.5
Fürst, D.O.6
Wilmanns, M.7
Gautel, M.8
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46
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0023584384
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Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. II. Generation of alpha-actinin dots within titin spots at the time of the first myofibril formation
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Tokuyasu KT, Maher PA Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. II. Generation of alpha-actinin dots within titin spots at the time of the first myofibril formation. J Cell Biol. 105:1987;2795-2801.
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(1987)
J Cell Biol
, vol.105
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Tokuyasu, K.T.1
Maher, P.A.2
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47
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0029824001
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Development of connectin/titin and nebulin in striated muscles of chicken
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Shimada Y, Komiyama M, Begum S, Maruyama K Development of connectin/titin and nebulin in striated muscles of chicken. Adv Biophys. 33:1996;223-234.
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(1996)
Adv Biophys
, vol.33
, pp. 223-234
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Shimada, Y.1
Komiyama, M.2
Begum, S.3
Maruyama, K.4
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48
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0024348057
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Myogenesis in the mouse embryo: Differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly
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Fürst DO, Osborn M, Weber K Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly. J Cell Biol. 109:1989;517-527.
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(1989)
J Cell Biol
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Fürst, D.O.1
Osborn, M.2
Weber, K.3
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49
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0030848328
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Myofibrillogenesis visualized in living embryonic cardiomyocytes
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The distribution patterns of green fluorescent protein tagged α-actinin were visualized during myofibril assembly in cultured cardiac myocytes. Nonmuscle myosin IIB is detected at the leading edges of the cells.
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Dabiri GA, Turnacioglu KK, Sanger JM, Sanger JW Myofibrillogenesis visualized in living embryonic cardiomyocytes. Proc Natl Acad Sci USA. 94:1997;9493-9498. The distribution patterns of green fluorescent protein tagged α-actinin were visualized during myofibril assembly in cultured cardiac myocytes. Nonmuscle myosin IIB is detected at the leading edges of the cells.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 9493-9498
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Dabiri, G.A.1
Turnacioglu, K.K.2
Sanger, J.M.3
Sanger, J.W.4
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50
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0030989899
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Organization of protein and mRNA for titin and other myofibril components during myofibrillogenesis in cultured chicken skeletal muscle
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Fulton AB, Alftine C Organization of protein and mRNA for titin and other myofibril components during myofibrillogenesis in cultured chicken skeletal muscle. Cell Struct Funct. 22:1997;51-58.
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(1997)
Cell Struct Funct
, vol.22
, pp. 51-58
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Fulton, A.B.1
Alftine, C.2
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51
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0031005990
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Assemblases and coupling proteins in thick filament assembly
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A thorough review of thick filament assembly and length regulation.
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Liu F, Barral JM, Bauer CC, Ortiz I, Cook RG, Schmid MF, Epstein HF Assemblases and coupling proteins in thick filament assembly. Cell Struct Funct. 22:1997;155-162. A thorough review of thick filament assembly and length regulation.
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(1997)
Cell Struct Funct
, vol.22
, pp. 155-162
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Liu, F.1
Barral, J.M.2
Bauer, C.C.3
Ortiz, I.4
Cook, R.G.5
Schmid, M.F.6
Epstein, H.F.7
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52
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0032567718
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β-filagenin, a newly identified protein coassembling with myosin and paramyosin in Caenorhabditis elegans
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Purification and cloning of a novel protein which coassembles with paramyosin and myosin filaments. β-filagenin may link these two filament systems, comparable to C-protein in vertebrates which links the titin and myosin filaments.
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Liu F, Bauer CC, Ortiz I, Cook RG, Schmid MF, Epstein HF β-filagenin, a newly identified protein coassembling with myosin and paramyosin in Caenorhabditis elegans. J Cell Biol. 140:1998;347-353. Purification and cloning of a novel protein which coassembles with paramyosin and myosin filaments. β-filagenin may link these two filament systems, comparable to C-protein in vertebrates which links the titin and myosin filaments.
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(1998)
J Cell Biol
, vol.140
, pp. 347-353
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Liu, F.1
Bauer, C.C.2
Ortiz, I.3
Cook, R.G.4
Schmid, M.F.5
Epstein, H.F.6
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53
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0032583155
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Unc-45 mutations in Caenorrhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly
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The UNC-45 locus is proposed to act as a protein machine required for myosin assembly. The UNC-45 gene product contains CRO1/She4p-like domains implicated in signal transduction pathways. Mutations in these regulatory domains interfere with the number and structure of thick filaments assembled.
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Barral JM, Bauer CC, Ortiz I, Epstein HF Unc-45 mutations in Caenorrhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly. J Cell Biol. 143:1998;1215-1225. The UNC-45 locus is proposed to act as a protein machine required for myosin assembly. The UNC-45 gene product contains CRO1/She4p-like domains implicated in signal transduction pathways. Mutations in these regulatory domains interfere with the number and structure of thick filaments assembled.
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(1998)
J Cell Biol
, vol.143
, pp. 1215-1225
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Barral, J.M.1
Bauer, C.C.2
Ortiz, I.3
Epstein, H.F.4
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54
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0032407540
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Defining actin filament length in striated muscle
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Interesting chapter discussing several hypothetical mechanisms by which muscle cells can generate uniform actin filament length distributions including a mechanism by which titin and its kinase domain may play a role in this process.
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Littlefield R, Fowler VM Defining actin filament length in striated muscle. Annu Rev Dev Cell Biol. 14:1998;487-525. Interesting chapter discussing several hypothetical mechanisms by which muscle cells can generate uniform actin filament length distributions including a mechanism by which titin and its kinase domain may play a role in this process.
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(1998)
Annu Rev Dev Cell Biol
, vol.14
, pp. 487-525
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Littlefield, R.1
Fowler, V.M.2
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