메뉴 건너뛰기




Volumn 8, Issue 1, 1996, Pages 86-96

Regulation of actin filament length in erythrocytes and striated muscle

Author keywords

[No Author keywords available]

Indexed keywords

NEBULIN; TROPOMODULIN;

EID: 0030021105     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80052-4     Document Type: Article
Times cited : (136)

References (73)
  • 1
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • Edited by Handin RI, Lux SE, Stossel TP. Philadelphia: JB Lippincott Co
    • Lux SE, Palek J: Disorders of the red cell membrane. In Blood: Principles and Practice of Hematology. Edited by Handin RI, Lux SE, Stossel TP. Philadelphia: JB Lippincott Co; 1995:1701-1818.
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1818
    • Lux, S.E.1    Palek, J.2
  • 2
    • 0028362281 scopus 로고
    • Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: Myofilament lengths
    • Sosa H, Popp D, Ouyang G, Huxley H: Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: myofilament lengths. Biophys J 1994, 67:283-292.
    • (1994) Biophys J , vol.67 , pp. 283-292
    • Sosa, H.1    Popp, D.2    Ouyang, G.3    Huxley, H.4
  • 3
    • 0022172245 scopus 로고
    • Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border
    • Mooseker MS: Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Annu Rev Cell Biol 1985, 1:209-241.
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 4
    • 0026677618 scopus 로고
    • Actin filaments, stereocilia, and hair cells: How cells count and measure
    • Tilney LQ, Tilney MS, DeRosier DJ: Actin filaments, stereocilia, and hair cells: how cells count and measure. Annu Rev Cell Biol 1992, 8:257-274.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 257-274
    • Tilney, L.Q.1    Tilney, M.S.2    DeRosier, D.J.3
  • 5
    • 0029156887 scopus 로고
    • F actin bundles in Drosophila bristles I. Two filament cross-links are involved in bundling
    • Tilney LG, Tilney MS, Guild GM: F actin bundles in Drosophila bristles I. Two filament cross-links are involved in bundling. J Cell Biol 1995, 130:629-638.
    • (1995) J Cell Biol , vol.130 , pp. 629-638
    • Tilney, L.G.1    Tilney, M.S.2    Guild, G.M.3
  • 6
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. a critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA: Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem 1986, 55:987-1035.
    • (1986) Annu Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 7
    • 0004164816 scopus 로고
    • London: Academic Press; Horecker B, Kaplan NO, Marmur J, Scheraga HA (Series Editors)
    • Oosawa F, Asakura S: Thermodynamics of the polymerization of protein. London: Academic Press; 1975:1-204. [Horecker B, Kaplan NO, Marmur J, Scheraga HA (Series Editors)]
    • (1975) Thermodynamics of the Polymerization of Protein , pp. 1-204
    • Oosawa, F.1    Asakura, S.2
  • 8
    • 0022975904 scopus 로고
    • Study of actin filament ends in the human red cell membrane
    • Pinder JC, Weeds AG, Gratzer WB: Study of actin filament ends in the human red cell membrane. J Mol Biol 1986, 191:461-468.
    • (1986) J Mol Biol , vol.191 , pp. 461-468
    • Pinder, J.C.1    Weeds, A.G.2    Gratzer, W.B.3
  • 9
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett V, Gilligan DM: The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol 1993, 9:27-66.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 10
    • 0027992919 scopus 로고
    • Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: Demonstration of unipolar α-actinin-F-actin crosslinking
    • Taylor KA, Taylor DW: Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar α-actinin-F-actin crosslinking. Biophys J 1994, 67:1976-1983.
    • (1994) Biophys J , vol.67 , pp. 1976-1983
    • Taylor, K.A.1    Taylor, D.W.2
  • 11
    • 0029022939 scopus 로고
    • Adducin: A physical model with implications for function in assembly of spectrin-actin complexes
    • Hughes CA, Bennett V: Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. J Biol Chem 1995, 270:18990-18996.
    • (1995) J Biol Chem , vol.270 , pp. 18990-18996
    • Hughes, C.A.1    Bennett, V.2
  • 12
    • 0000488695 scopus 로고
    • Interactions of tensin with actin and Identification of Its three distinct actin-binding domains
    • Lo SH, Janmey PA, Hartwig JH, Chen LB: Interactions of tensin with actin and Identification of Its three distinct actin-binding domains. J Cell Biol 1994, 125:1067-1075.
    • (1994) J Cell Biol , vol.125 , pp. 1067-1075
    • Lo, S.H.1    Janmey, P.A.2    Hartwig, J.H.3    Chen, L.B.4
  • 13
    • 0028956756 scopus 로고
    • Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin
    • Chuang J-Z, Lin DC, Li S: Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin. J Cell Biol 1995, 128:1095-1109.
    • (1995) J Cell Biol , vol.128 , pp. 1095-1109
    • Chuang, J.-Z.1    Lin, D.C.2    Li, S.3
  • 14
    • 0028153227 scopus 로고
    • An end in sight: Tropomodulin
    • Coluccio LM: An end in sight: tropomodulin. J Cell Biol 1994, 127:1497-1499.
    • (1994) J Cell Biol , vol.127 , pp. 1497-1499
    • Coluccio, L.M.1
  • 15
    • 0023272783 scopus 로고
    • r 43,000 tropomyosin-binding protein from human erythrocyte membranes
    • r 43,000 tropomyosin-binding protein from human erythrocyte membranes. J Biol Chem 1987, 262:12792-12800.
    • (1987) J Biol Chem , vol.262 , pp. 12792-12800
    • Fowler, V.M.1
  • 16
    • 0028246498 scopus 로고
    • Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons
    • Ursitti JA, Fowler VM: Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons. J Cell Biol 1994, 107:1633-1639.
    • (1994) J Cell Biol , vol.107 , pp. 1633-1639
    • Ursitti, J.A.1    Fowler, V.M.2
  • 17
    • 0025314680 scopus 로고
    • Tropomodulin: A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin
    • Fowler VM: Tropomodulin: a cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin. J Cell Biol 1990, 111:471-482.
    • (1990) J Cell Biol , vol.111 , pp. 471-482
    • Fowler, V.M.1
  • 18
  • 19
    • 0023857288 scopus 로고
    • Association of deoxyribonuclease I with the pointed ends of actin filaments in human red blood cell membrane skeletons
    • Podolski JL, Steck TL: Association of deoxyribonuclease I with the pointed ends of actin filaments In human red blood cell membrane skeletons. J Biol Chem 1988, 263:638-645.
    • (1988) J Biol Chem , vol.263 , pp. 638-645
    • Podolski, J.L.1    Steck, T.L.2
  • 20
    • 0028116302 scopus 로고
    • Isofom-specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins
    • Babcock GG, Fowler VM: Isofom-specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins. J Biol Chem 1994, 269:27510-27518.
    • (1994) J Biol Chem , vol.269 , pp. 27510-27518
    • Babcock, G.G.1    Fowler, V.M.2
  • 21
    • 0029166140 scopus 로고
    • Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes
    • Gregorio CC, Weber A, Bondad M, Pennise CR, Fowler VM: Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature 1995, 377:83-86.
    • (1995) Nature , vol.377 , pp. 83-86
    • Gregorio, C.C.1    Weber, A.2    Bondad, M.3    Pennise, C.R.4    Fowler, V.M.5
  • 23
    • 0028365626 scopus 로고
    • Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development
    • Sussman MA, Sakhi S, Barrientos P, Ito M, Kedes L: Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development. Circ Res 1994, 75:221-232.
    • (1994) Circ Res , vol.75 , pp. 221-232
    • Sussman, M.A.1    Sakhi, S.2    Barrientos, P.3    Ito, M.4    Kedes, L.5
  • 24
    • 0028837458 scopus 로고
    • Cloning of tropomodulin cDNA and localization of gene transcripts during mouse embryogenesis
    • Ito M, Swanson B, Sussman MA, Kedes L, Lyons G: Cloning of tropomodulin cDNA and localization of gene transcripts during mouse embryogenesis. Dev Biol 1995, 167:317-328.
    • (1995) Dev Biol , vol.167 , pp. 317-328
    • Ito, M.1    Swanson, B.2    Sussman, M.A.3    Kedes, L.4    Lyons, G.5
  • 25
    • 0028242534 scopus 로고
    • Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the γ-tropomyosin gene
    • Sung LA Lin JJ-C: Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the γ-tropomyosin gene. Biochem Biophys Res Commun 1994, 201:627-634.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 627-634
    • Sung, L.A.1    Lin, J.J.-C.2
  • 26
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller JP, Helfman DM: The molecular basis for tropomyosin isoform diversity. BioEssays 1991, 13:429-437.
    • (1991) BioEssays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 28
    • 0026525482 scopus 로고
    • Tropomodulin binding to tropomyosins. Isoform-specific difference in affinity and stoichiometry
    • Sussman MA, Fowler VM: Tropomodulin binding to tropomyosins. Isoform-specific difference in affinity and stoichiometry. Eur J Biochem 1992, 205:355-362.
    • (1992) Eur J Biochem , vol.205 , pp. 355-362
    • Sussman, M.A.1    Fowler, V.M.2
  • 29
    • 0021351389 scopus 로고
    • Erythrocyte membrane tropomyosin
    • Fowler VM, Bennett V: Erythrocyte membrane tropomyosin. J Biol Chem 1984, 259:5978-5989.
    • (1984) J Biol Chem , vol.259 , pp. 5978-5989
    • Fowler, V.M.1    Bennett, V.2
  • 30
    • 0022486512 scopus 로고
    • Ultrastructure of the intact skeleton of the human erythrocyte membrane
    • Shen BW, Josephs R, Steck TH: Ultrastructure of the intact skeleton of the human erythrocyte membrane. J Cell Biol 1986, 102:997-1006.
    • (1986) J Cell Biol , vol.102 , pp. 997-1006
    • Shen, B.W.1    Josephs, R.2    Steck, T.H.3
  • 31
    • 0024427604 scopus 로고
    • Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization
    • Broschat KO, Weber A, Burgess DR: Tropomyosin stabilizes the pointed end of actin filaments by slowing depolymerization. Biochemistry 1989, 28:8501-8506.
    • (1989) Biochemistry , vol.28 , pp. 8501-8506
    • Broschat, K.O.1    Weber, A.2    Burgess, D.R.3
  • 32
    • 0025613855 scopus 로고
    • Tropomyosin prevents depolymerization of actin filaments from the pointed end
    • Broschat KO: Tropomyosin prevents depolymerization of actin filaments from the pointed end. J Biol Chem 1990, 265:21323-21329.
    • (1990) J Biol Chem , vol.265 , pp. 21323-21329
    • Broschat, K.O.1
  • 36
    • 0001425662 scopus 로고
    • Muscle cells
    • Edited by Brachet J, Mirsky AE. New York: Academic Press
    • Huxley HE: Muscle cells. In: The Cell: Biochemistry, Physiology, Morphology. Edited by Brachet J, Mirsky AE. New York: Academic Press; 1960:365-481 [vol 1].
    • (1960) The Cell: Biochemistry, Physiology, Morphology , vol.1 , pp. 365-481
    • Huxley, H.E.1
  • 37
    • 0021999557 scopus 로고
    • Does actin bind to the ends of thin filaments in skeletal muscle?
    • Ishiwata S, Funatsu T: Does actin bind to the ends of thin filaments In skeletal muscle? J Cell Biol 1985, 100:282-291.
    • (1985) J Cell Biol , vol.100 , pp. 282-291
    • Ishiwata, S.1    Funatsu, T.2
  • 38
    • 0023372284 scopus 로고
    • (36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • (36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J Cell Biol 1987, 105:371-379.
    • (1987) J Cell Biol , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 39
    • 0027178964 scopus 로고
    • Localization of capZ during myofibrillogenesis in cultured chicken muscle
    • Schafer DA, Waddle JA, Cooper JA: Localization of capZ during myofibrillogenesis in cultured chicken muscle. Cell Motil Cytoskel 1993, 25:317-335.
    • (1993) Cell Motil Cytoskel , vol.25 , pp. 317-335
    • Schafer, D.A.1    Waddle, J.A.2    Cooper, J.A.3
  • 41
    • 0029612323 scopus 로고
    • Control of actin assembly at filament ends
    • Schafer DA, Cooper JA: Control of actin assembly at filament ends. Annu Rev Cell Dev Biol 1995, 11:497-518.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 497-518
    • Schafer, D.A.1    Cooper, J.A.2
  • 42
    • 0028891855 scopus 로고
    • Inhibition of capZ during myofibrillogenesis alters assembly of actin filaments
    • Schafer DA, Hug C, Cooper JA: Inhibition of capZ during myofibrillogenesis alters assembly of actin filaments. J Cell Biol 1995, 128:61-70.
    • (1995) J Cell Biol , vol.128 , pp. 61-70
    • Schafer, D.A.1    Hug, C.2    Cooper, J.A.3
  • 43
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein β-subunit isoforms of vertebrates
    • Schafer DA, Korshunova YO, Schroer TA, Cooper JA: Differential localization and sequence analysis of capping protein β-subunit isoforms of vertebrates. J Cell Biol 1994, 127:453-465.
    • (1994) J Cell Biol , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 45
    • 0028173631 scopus 로고
    • Interaction of cap Z with actin
    • Casella JF, Torres MA: Interaction of cap Z with actin. J Biol Chem 1994, 269:6992-6998.
    • (1994) J Biol Chem , vol.269 , pp. 6992-6998
    • Casella, J.F.1    Torres, M.A.2
  • 46
  • 48
    • 0027535632 scopus 로고
    • Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle
    • Fowler VM, Sussman MA, Miller PG, Rucher BE, Daniels MP: Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle. J Cell Biol 1993, 120:411-420.
    • (1993) J Cell Biol , vol.120 , pp. 411-420
    • Fowler, V.M.1    Sussman, M.A.2    Miller, P.G.3    Rucher, B.E.4    Daniels, M.P.5
  • 49
    • 0028914944 scopus 로고
    • Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: Tropomodulin requires tropomyosln for assembly
    • Gregorio CC, Fowler VM: Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosln for assembly. J Cell Biol 1995, 129:683-695.
    • (1995) J Cell Biol , vol.129 , pp. 683-695
    • Gregorio, C.C.1    Fowler, V.M.2
  • 50
    • 0029888857 scopus 로고    scopus 로고
    • Tropomodulin function and thin filament assembly in cardiac myocytes
    • in press
    • Gregorio CC, Fowler VM: Tropomodulin function and thin filament assembly in cardiac myocytes. Trends Cardiovasc Med 1996, in press.
    • (1996) Trends Cardiovasc Med
    • Gregorio, C.C.1    Fowler, V.M.2
  • 51
    • 0028091960 scopus 로고
    • Titin and nebulin; protein rulers in muscle?
    • Trinick J: Titin and nebulin; protein rulers In muscle? Trends Biochem Sci 1994, 19:405-409.
    • (1994) Trends Biochem Sci , vol.19 , pp. 405-409
    • Trinick, J.1
  • 52
    • 0028955760 scopus 로고
    • Structure and function of titin and nebulin
    • Keller TCS III: Structure and function of titin and nebulin. Curr Opin Cell Biol 1995, 7:32-38.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 32-38
    • Keller T.C.S. III1
  • 53
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit S, Kolmerer B: The complete primary structure of human nebulin and its correlation to muscle structure. J Mol Biol 1995, 248:308-315.
    • (1995) J Mol Biol , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 54
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M, Winder SJ, Pastore A: Nebulin, a helical actin binding protein. EMBO J 1994, 13:1782-1789.
    • (1994) EMBO J , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 55
    • 0026555549 scopus 로고
    • Spatial relationship of nebulin relative to other myofibrillar proteins during myogenesis in embryonic chick skeletal muscle in vitro
    • Komiyama M, Zhou Z-H, Maruyama K, Shimada Y: Spatial relationship of nebulin relative to other myofibrillar proteins during myogenesis in embryonic chick skeletal muscle in vitro. J Muscle Res Cell Motil 1992, 13:48-54.
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 48-54
    • Komiyama, M.1    Zhou, Z.-H.2    Maruyama, K.3    Shimada, Y.4
  • 56
    • 0028101984 scopus 로고
    • Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: Evidence for a conserved myoblast differentiation program in skeletal muscle
    • Lin Z, Lu M-H, Schultheiss T, Choi J, Holtzer S, Dilullo D, Fischman DA, Holtzer H: Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: evidence for a conserved myoblast differentiation program in skeletal muscle. Cell Motil Cytoskel 1994, 29:1-19.
    • (1994) Cell Motil Cytoskel , vol.29 , pp. 1-19
    • Lin, Z.1    Lu, M.-H.2    Schultheiss, T.3    Choi, J.4    Holtzer, S.5    Dilullo, D.6    Fischman, D.A.7    Holtzer, H.8
  • 57
    • 0028080839 scopus 로고
    • Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin
    • Root DD, Wang K: Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin. Biochemistry 1994, 33:12581-12591.
    • (1994) Biochemistry , vol.33 , pp. 12581-12591
    • Root, D.D.1    Wang, K.2
  • 58
    • 0018333449 scopus 로고
    • The measurement and dynamic implications of thin filament lengths in heart muscle
    • Robinson TF, Winegrad S: The measurement and dynamic implications of thin filament lengths in heart muscle. J Physiol (Lond) 1979, 286:607-619.
    • (1979) J Physiol (Lond) , vol.286 , pp. 607-619
    • Robinson, T.F.1    Winegrad, S.2
  • 59
    • 0028784365 scopus 로고
    • Nebulette: A 107 kD nebulin-like protein in cardiac muscle
    • Moncman CL, Wang K: Nebulette: a 107 kD nebulin-like protein in cardiac muscle. Cell Motil Cytoskel 1995, 32:205-225.
    • (1995) Cell Motil Cytoskel , vol.32 , pp. 205-225
    • Moncman, C.L.1    Wang, K.2
  • 60
    • 0015530296 scopus 로고
    • Regulation of skeletal muscle contraction II. Structural studies of the interaction of the tropomyosin-troponin complex with actin
    • Spudich JA, Huxley HE, Finch JT: Regulation of skeletal muscle contraction II. Structural studies of the interaction of the tropomyosin-troponin complex with actin. J Mol Biol 1972, 72:619-632.
    • (1972) J Mol Biol , vol.72 , pp. 619-632
    • Spudich, J.A.1    Huxley, H.E.2    Finch, J.T.3
  • 61
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by x-ray fiber diffraction on oriented actin-tropomyosin gels
    • Lorenz M, Poole, KJV, Popp D, Rosenbaum G, Holmes KC: An atomic model of the unregulated thin filament obtained by x-ray fiber diffraction on oriented actin-tropomyosin gels. J Mol Biol 1995, 246:108-119.
    • (1995) J Mol Biol , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.V.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 62
    • 0028000396 scopus 로고
    • Structural requirements of tropomyosin for binding to filamentous actin
    • Hitchcock-Degregori SE: Structural requirements of tropomyosin for binding to filamentous actin. Adv Exp Med Biol 1994, 358:85-96.
    • (1994) Adv Exp Med Biol , vol.358 , pp. 85-96
    • Hitchcock-Degregori, S.E.1
  • 63
    • 0027970529 scopus 로고
    • Tropomyosin length and two-stranded F-actin flexibility in the thin filament
    • Censullo R, Cheung HC: Tropomyosin length and two-stranded F-actin flexibility in the thin filament. J Mol Biol 1994, 243:520-529.
    • (1994) J Mol Biol , vol.243 , pp. 520-529
    • Censullo, R.1    Cheung, H.C.2
  • 64
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips GN Jr, Fillers JP, Cohen C: Tropomyosin crystal structure and muscle regulation. J Mol Biol 1986, 192:111-131.
    • (1986) J Mol Biol , vol.192 , pp. 111-131
    • Phillips G.N., Jr.1    Fillers, J.P.2    Cohen, C.3
  • 65
    • 0028006335 scopus 로고
    • Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane
    • Der Terrossian E, Deprette C, Lebbar I, Cassoly R: Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane. Eur J Biochem 1994, 219:503-511.
    • (1994) Eur J Biochem , vol.219 , pp. 503-511
    • Der Terrossian, E.1    Deprette, C.2    Lebbar, I.3    Cassoly, R.4
  • 66
    • 0029101194 scopus 로고
    • Characterization of the binary interaction between human erythrocyte protein 4.1 and actln
    • Morris MB, Lux SE: Characterization of the binary interaction between human erythrocyte protein 4.1 and actln. Eur J Biochem 1995, 231:644-650.
    • (1995) Eur J Biochem , vol.231 , pp. 644-650
    • Morris, M.B.1    Lux, S.E.2
  • 67
    • 0029084382 scopus 로고
    • Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily
    • Azim AC, Knoll JHM, Beggs AH, Chishti AH: Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily. J Biol Chem 1995, 270:17407-17413.
    • (1995) J Biol Chem , vol.270 , pp. 17407-17413
    • Azim, A.C.1    Knoll, J.H.M.2    Beggs, A.H.3    Chishti, A.H.4
  • 68
    • 0021341994 scopus 로고
    • Spectrin and protein 4.1 as an actin filament capping complex
    • Pinder JC, Ohanian V, Gratzer W: Spectrin and protein 4.1 as an actin filament capping complex. FEBS Lett 1984, 169:161-164.
    • (1984) FEBS Lett , vol.169 , pp. 161-164
    • Pinder, J.C.1    Ohanian, V.2    Gratzer, W.3
  • 69
    • 0018898706 scopus 로고
    • Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation
    • Brenner SL, Korn ED: Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. J Biol Chem 1980, 255:1670-1676.
    • (1980) J Biol Chem , vol.255 , pp. 1670-1676
    • Brenner, S.L.1    Korn, E.D.2
  • 70
    • 0021136869 scopus 로고
    • Modulation of actin polymerization by the spectrin-band 4.1 complex
    • Elbaum D, Mimms LT, Branton D: Modulation of actin polymerization by the spectrin-band 4.1 complex. Biochemistry 1984, 23:4813-4816.
    • (1984) Biochemistry , vol.23 , pp. 4813-4816
    • Elbaum, D.1    Mimms, L.T.2    Branton, D.3
  • 71
    • 0015786195 scopus 로고
    • Molecular control mechanisms in muscle contraction
    • Weber A, Murray JM: Molecular control mechanisms in muscle contraction. Physiol Rev 1973, 53:612-673.
    • (1973) Physiol Rev , vol.53 , pp. 612-673
    • Weber, A.1    Murray, J.M.2
  • 72
    • 0030005249 scopus 로고    scopus 로고
    • A new function for adducin: Calcium/calmodulin regulated capping of the barbed ends of actin filaments
    • in press
    • Kuhlman PA, Hughes CA, Bennett V, Fowler VM: A new function for adducin: calcium/calmodulin regulated capping of the barbed ends of actin filaments. J Biol Chem 1996, in press.
    • (1996) J Biol Chem
    • Kuhlman, P.A.1    Hughes, C.A.2    Bennett, V.3    Fowler, V.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.