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Volumn 11, Issue , 1995, Pages 633-675

Unconventional myosins

Author keywords

actin based motors; cytoskeleton; motility; motor proteins; myosin I

Indexed keywords

ACTIN; MYOSIN;

EID: 0029616658     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cb.11.110195.003221     Document Type: Review
Times cited : (391)

References (158)
  • 1
    • 0026666397 scopus 로고
    • An active motor model for adaptation by vertebrate hair cells
    • Assad JA, Corey DP. 1992. An active motor model for adaptation by vertebrate hair cells. J. Neurosci. 12:3291-309
    • (1992) J. Neurosci. , vol.12 , pp. 3291-3309
    • Assad, J.A.1    Corey, D.P.2
  • 2
    • 0028306902 scopus 로고
    • Rat myr 4 defines a novel subclass of myosin I: Identification, distribution, localization and mapping of calmodulin binding sites wilh differential calcium sensitivity
    • Bähler M, Kroschewski R, Stofller H-E, Behrmann T. 1994. Rat myr 4 defines a novel subclass of myosin I: identification, distribution, localization and mapping of calmodulin binding sites wilh differential calcium sensitivity. J. Cell Biol. 126:375-49
    • (1994) J. Cell Biol. , vol.126 , pp. 375-449
    • Bähler, M.1    Kroschewski, R.2    Stofller, H.-E.3    Behrmann, T.4
  • 3
    • 0025155340 scopus 로고
    • Localization of myosin IC and myosin II in Acanthainoeba castellanii by indirect immunofluorescence and immunogold electron microscopy
    • Baines IC, Korn ED. 1990. Localization of myosin IC and myosin II in Acanthainoeba castellanii by indirect immunofluorescence and immunogold electron microscopy. J. Cell Biol. 111:1895-904
    • (1990) J. Cell Biol. , vol.111 , pp. 1895-1904
    • Baines, I.C.1    Korn, E.D.2
  • 7
    • 0028231886 scopus 로고
    • Identification and overlapping expression of multiple unconventional myosins in vertebrate cell types
    • Bement WM, Hasson T, Wirth JA, Cheney RE, Moosekcr MS. 1994a. Identification and overlapping expression of multiple unconventional myosins in vertebrate cell types. Proc. Natl. Acad. Sci. USA 91:6549-53
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6549-6553
    • Bement, W.M.1    Hasson, T.2    Wirth, J.A.3    Cheney, R.E.4    Moosekcr, M.S.5
  • 8
    • 0027422248 scopus 로고
    • Keeping out the rain
    • Bement WM, Mooseker MS. 1993. Keeping out the rain. Nature 365:785-86
    • (1993) Nature , vol.365 , pp. 785-786
    • Bement, W.M.1    Mooseker, M.S.2
  • 9
    • 0029006373 scopus 로고
    • TEDS Rule: A molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head
    • Bement WM, Mooseker MS. 1995. TEDS Rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head. Cell Motil. Cytoskelet. 31:87-92
    • (1995) Cell Motil. Cytoskelet. , vol.31 , pp. 87-92
    • Bement, W.M.1    Mooseker, M.S.2
  • 10
    • 0028061489 scopus 로고
    • Cloning and mRNA expression of human uncoventional niyosin-IC; a homolog of amoeboid myosins-I with a single IQ motif and an SH3 domain
    • Bement WM, Wirth JA, Mooseker MS. 1994b. Cloning and mRNA expression of human uncoventional niyosin-IC; a homolog of amoeboid myosins-I with a single IQ motif and an SH3 domain. J. Mol. Biol. 243:356-63
    • (1994) J. Mol. Biol. , vol.243 , pp. 356-363
    • Bement, W.M.1    Wirth, J.A.2    Mooseker, M.S.3
  • 11
    • 0026027618 scopus 로고
    • Limited tissue distribution of the intestinal brush border myosin I protein
    • Bikle DD, Munson S, Mancianti M-L. 1991. Limited tissue distribution of the intestinal brush border myosin I protein. Gastroenterology 100:395-402
    • (1991) Gastroenterology , vol.100 , pp. 395-402
    • Bikle, D.D.1    Munson, S.2    Mancianti, M.-L.3
  • 12
    • 0027732538 scopus 로고
    • Proteins regulating ras and its relatives
    • Boguski MS, McCormick F. 1993. Proteins regulating ras and its relatives. Nature 366:643-54
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 13
    • 0028035094 scopus 로고
    • Myosin I localizes to the midbody region during mammalian cytokinesis
    • Breckler J, Burnside B. 1994. Myosin I localizes to the midbody region during mammalian cytokinesis. Cell Motil. Cytoskelet. 29:312-20
    • (1994) Cell Motil. Cytoskelet. , vol.29 , pp. 312-320
    • Breckler, J.1    Burnside, B.2
  • 14
    • 0027954167 scopus 로고
    • The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae
    • Brockerhoff SE, Stevens RC, Davis TN. 1994. The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. J. Cell Biol. 124:315-23
    • (1994) J. Cell Biol. , vol.124 , pp. 315-323
    • Brockerhoff, S.E.1    Stevens, R.C.2    Davis, T.N.3
  • 16
    • 0025193529 scopus 로고
    • Acanthamoeba myosin I heavy chain kinase is activated by phosphatidylserine-enhanced phosphorylation
    • Brzeska H, Lynch TJ, Korn ED, 1990a. Acanthamoeba myosin I heavy chain kinase is activated by phosphatidylserine-enhanced phosphorylation. J. Biol. Chem. 265:3591-94
    • (1990) J. Biol. Chem. , vol.265 , pp. 3591-3594
    • Brzeska, H.1    Lynch, T.J.2    Korn, E.D.3
  • 17
    • 0025144587 scopus 로고
    • Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides
    • Brzeska H, Lynch TJ, Martin B, Corgliano-Murphy A, Korn ED. 1990b. Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides. J. Biol. Chem. 256:16138-44
    • (1990) J. Biol. Chem. , vol.256 , pp. 16138-16144
    • Brzeska, H.1    Lynch, T.J.2    Martin, B.3    Corgliano-Murphy, A.4    Korn, E.D.5
  • 18
    • 0028199090 scopus 로고
    • Myosin-I from mammalian smooth muscle is regulated by caldesmon-calmodulin
    • Chacko S, Jacob SS, Joriuchi K. 1994. Myosin-I from mammalian smooth muscle is regulated by caldesmon-calmodulin. J. Biol. Chem. 269:15803-807
    • (1994) J. Biol. Chem. , vol.269 , pp. 15803-15807
    • Chacko, S.1    Jacob, S.S.2    Joriuchi, K.3
  • 21
    • 0027420994 scopus 로고
    • Brain myosin-V is a two-headed unconventional myosin with motor activity
    • Cheney RE, O'Shea MK, Heuser JE, Coelho MV, Wolenski JS, et al. 1993a. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75:13-23
    • (1993) Cell , vol.75 , pp. 13-23
    • Cheney, R.E.1    O'Shea, M.K.2    Heuser, J.E.3    Coelho, M.V.4    Wolenski, J.S.5
  • 23
    • 0025935246 scopus 로고
    • Differential regulation of vertebrate myosins I and II
    • Collins K, Matsudaira FT. 1991. Differential regulation of vertebrate myosins I and II. J. Cell Sci. Suppl. 14:11-16
    • (1991) J. Cell Sci. Suppl. , vol.14 , pp. 11-16
    • Collins, K.1    Matsudaira, F.T.2
  • 24
    • 0025264994 scopus 로고
    • Calmodulin dissociation regulates brush border myosin-1 (110 K-calmodulin) activity in vitro
    • Collins K, Sellers JR, Matsudaira PT. 1990. Calmodulin dissociation regulates brush border myosin-1 (110 K-calmodulin) activity in vitro. J. Cell Biol. 110:1137-47
    • (1990) J. Cell Biol. , vol.110 , pp. 1137-1147
    • Collins, K.1    Sellers, J.R.2    Matsudaira, P.T.3
  • 25
    • 0027932202 scopus 로고
    • Differential calmodulin binding to three myosin-1 isoforms from liver
    • Coluccio LM. 1994. Differential calmodulin binding to three myosin-1 isoforms from liver. J. Cell Sci. 107:2279-84
    • (1994) J. Cell Sci. , vol.107 , pp. 2279-2284
    • Coluccio, L.M.1
  • 26
    • 0023871582 scopus 로고
    • Mapping of the microvillar 110K-calmodulin complex: Calmodulin-associaied or calmodulin-free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activity
    • Coluccio LM, Bretscher A. 1988. Mapping of the microvillar 110K-calmodulin complex: calmodulin-associaied or calmodulin-free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activity. J. Cell Biol. 106:367-73
    • (1988) J. Cell Biol. , vol.106 , pp. 367-373
    • Coluccio, L.M.1    Bretscher, A.2
  • 28
    • 0028106091 scopus 로고
    • Identification of coelomocyte unconventional myosin and its associations with in vivo particles
    • D'Andrea LM, Danon A, Sgourdas GP, Bonder ER. 1994. Identification of coelomocyte unconventional myosin and its associations with in vivo particles. J. Cell Sci. 107:2081-94
    • (1994) J. Cell Sci. , vol.107 , pp. 2081-2094
    • D'Andrea, L.M.1    Danon, A.2    Sgourdas, G.P.3    Bonder, E.R.4
  • 29
    • 0027452047 scopus 로고
    • Inhibition of contractile vacuole function in vivo by antibodies against myosin-I
    • Doberstein SK, Baines IC, Wiegand G, Korn ED, Pollard TD. 1993. Inhibition of contractile vacuole function in vivo by antibodies against myosin-I. Nature 356:841-43
    • (1993) Nature , vol.356 , pp. 841-843
    • Doberstein, S.K.1    Baines, I.C.2    Wiegand, G.3    Korn, E.D.4    Pollard, T.D.5
  • 30
    • 0026721410 scopus 로고
    • Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthainoeba myosin IC
    • Doberstein SK, Pollard, TD. 1992. Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthainoeba myosin IC. J. Cell Biol. 117:1241-49
    • (1992) J. Cell Biol. , vol.117 , pp. 1241-1249
    • Doberstein, S.K.1    Pollard, T.D.2
  • 31
    • 0028219183 scopus 로고
    • Cloning, analysis and chromosomal localization of myoxin (MYH12), the human homolog to the mouse dilute gene
    • Engle U, Kennett RH. 1994. Cloning, analysis and chromosomal localization of myoxin (MYH12), the human homolog to the mouse dilute gene. Genomics 19:407-16
    • (1994) Genomics , vol.19 , pp. 407-416
    • Engle, U.1    Kennett, R.H.2
  • 32
    • 0026642525 scopus 로고
    • Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: A novel calmodulin binding myosin
    • Espindola FS, Espreafico E, Coelbo M, Martins A, Costa F, et al. 1992. Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin binding myosin. J. Cell Biol. 118:359-68
    • (1992) J. Cell Biol. , vol.118 , pp. 359-368
    • Espindola, F.S.1    Espreafico, E.2    Coelbo, M.3    Martins, A.4    Costa, F.5
  • 33
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains
    • Espreafico EM, Cheney RE, Matteoli M, Nascimento AAC, De Camilli PV, et al. 1992, Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J. Cell Biol. 119:1541-58
    • (1992) J. Cell Biol. , vol.119 , pp. 1541-1558
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.C.4    De Camilli, P.V.5
  • 34
    • 0027933182 scopus 로고
    • Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
    • Fanning AS, Wolenski JS, Mooseker MS, Izant JG. 1994. Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cell Motil. Cytoskelet. 29:29-45
    • (1994) Cell Motil. Cytoskelet. , vol.29 , pp. 29-45
    • Fanning, A.S.1    Wolenski, J.S.2    Mooseker, M.S.3    Izant, J.G.4
  • 35
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Fath KR, Burgess DR. 1993. Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein. J. Cell Biol. 120:117-28
    • (1993) J. Cell Biol. , vol.120 , pp. 117-128
    • Fath, K.R.1    Burgess, D.R.2
  • 36
    • 0028049387 scopus 로고
    • Unconventional myosm-mediated membrane motility
    • Fath KR, Burgess DR. 1994. Unconventional myosm-mediated membrane motility. Curr. Opin. Cell Biol. 6:131-36
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 131-136
    • Fath, K.R.1    Burgess, D.R.2
  • 37
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath KR, Trimbur CM, Burgess DR. 1994. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol. 126:661-75
    • (1994) J. Cell Biol. , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, C.M.2    Burgess, D.R.3
  • 38
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng S, Chen JK, Hongtao Y, Simon JA, Schreiber SL. 1994. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266:1241-47
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Hongtao, Y.3    Simon, J.A.4    Schreiber, S.L.5
  • 39
    • 0028239967 scopus 로고
    • Brush border myosin-I microinjected into cultured cells is targeted to aetin-containing surface structures
    • Footer M, Bretscher A. 1904. Brush border myosin-I microinjected into cultured cells is targeted to aetin-containing surface structures. J. Cell Sci. 107:1623-31
    • (1904) J. Cell Sci. , vol.107 , pp. 1623-1631
    • Footer, M.1    Bretscher, A.2
  • 40
    • 0027240352 scopus 로고
    • Toward a new concept of cell motility: Cytoskeletal dynamics in amoeboid movement and cell division
    • Fukui Y. 1993a. Toward a new concept of cell motility: cytoskeletal dynamics in amoeboid movement and cell division. Int. Rev. Cytol. 144:85-127
    • (1993) Int. Rev. Cytol. , vol.144 , pp. 85-127
    • Fukui, Y.1
  • 41
    • 0027130298 scopus 로고
    • Composition, organization and function of the motor systems of free-living Dictyostelium amoeba
    • Fukui Y. 1993b. Composition, organization and function of the motor systems of free-living Dictyostelium amoeba. Acta Protozool. 32:201-10
    • (1993) Acta Protozool. , vol.32 , pp. 201-210
    • Fukui, Y.1
  • 42
    • 0028860302 scopus 로고
    • A type VII myosin encoded by the mouse deafness gene shaker-1
    • Gibson F, Walsh J, Mburu P, Varela A, Brown KA, et al. 1995. A type VII myosin encoded by the mouse deafness gene shaker-1. Nature 374:62-64
    • (1995) Nature , vol.374 , pp. 62-64
    • Gibson, F.1    Walsh, J.2    Mburu, P.3    Varela, A.4    Brown, K.A.5
  • 44
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed componenet of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill SR, SchroerT A, Szilak I, Steur ER, Sheetz MP. 1991. Dynactin, a conserved, ubiquitously expressed componenet of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 115:1639-50
    • (1991) J. Cell Biol. , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steur, E.R.4    Sheetz, M.P.5
  • 45
    • 0027439124 scopus 로고
    • Identifiction of a 120 kd hair-bundle myosin located near stereociliary tips
    • Gillespie PG, Wagner MC, Hudspeth AJ. 1993. Identifiction of a 120 kd hair-bundle myosin located near stereociliary tips. Neuron 11:581-94
    • (1993) Neuron , vol.11 , pp. 581-594
    • Gillespie, P.G.1    Wagner, M.C.2    Hudspeth, A.J.3
  • 47
    • 0028250631 scopus 로고
    • Molecular evolution of the myosin superfamily: Application of phylogenetic techniques to cell biological questions
    • Goodson HV. 1994. Molecular evolution of the myosin superfamily: application of phylogenetic techniques to cell biological questions. Soc. Gen. Physiol. Ser. 49:141-57
    • (1994) Soc. Gen. Physiol. Ser. , vol.49 , pp. 141-157
    • Goodson, H.V.1
  • 48
    • 0027508927 scopus 로고
    • Molecular evolution of the myosin family: Relationships derived from comparisons of amino acid sequens
    • Goodson HV, Spudich JA. 1993. Molecular evolution of the myosin family: relationships derived from comparisons of amino acid sequens. Proc. Natl. Acad. Sci. USA 90:659-63
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 659-663
    • Goodson, H.V.1    Spudich, J.A.2
  • 49
    • 13344258673 scopus 로고
    • Synthetic lethality screen identifies a new yeast myosin I
    • Abstr.
    • Goodson HV, Spudich JA. 1994. Synthetic lethality screen identifies a new yeast myosin I. Mol. Biol. Cell Suppl. 5:276a (Abstr.)
    • (1994) Mol. Biol. Cell Suppl. , vol.5
    • Goodson, H.V.1    Spudich, J.A.2
  • 50
    • 0028929478 scopus 로고
    • Identification and molecular characterization of a yeast myosin-I
    • Goodson HV, Spudich JA. 1995. Identification and molecular characterization of a yeast myosin-I. Cell Motil. Cytoskelet. 30:73-84
    • (1995) Cell Motil. Cytoskelet. , vol.30 , pp. 73-84
    • Goodson, H.V.1    Spudich, J.A.2
  • 51
    • 0028902506 scopus 로고
    • The role of MYO2, a yeast class V myosin, in vesicular transport
    • Govindan B, Bower R, Novick P. 1995. The role of MYO2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128:1055-68
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bower, R.2    Novick, P.3
  • 53
    • 0028216280 scopus 로고
    • Identification of MYO4, a second class V myosin gene in yeast
    • Haarer B K, Petzold A, Lillie SH, Brown SS. 1994. Identification of MYO4, a second class V myosin gene in yeast. J. Cell Sci. 107:1055-64
    • (1994) J. Cell Sci. , vol.107 , pp. 1055-1064
    • Haarer, B.K.1    Petzold, A.2    Lillie, S.H.3    Brown, S.S.4
  • 54
    • 0028170820 scopus 로고
    • Small GTP binding proteins and the regulation of the actin cytoskeleton
    • Hall A. 1994. Small GTP binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10:31-54
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 55
    • 0025340346 scopus 로고
    • A second isoform of chicken brush border myosin-I contains a 29-residue inserted sequence that binds calmodulin
    • Halsall DJ, Hammer JA. 1990. A second isoform of chicken brush border myosin-I contains a 29-residue inserted sequence that binds calmodulin. FEBS Lett. 267:126-30
    • (1990) FEBS Lett. , vol.267 , pp. 126-130
    • Halsall, D.J.1    Hammer, J.A.2
  • 56
    • 0028280744 scopus 로고
    • The structure and function of unconventional myosins: A review
    • Hammer JA. 1994. The structure and function of unconventional myosins: a review. J. Muscle Res. Cell Motil. 15:1-10
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 1-10
    • Hammer, J.A.1
  • 58
    • 0027993176 scopus 로고
    • Porcine myosin-VI: Characterization of a new mammalian unconventional myosin
    • Hasson T, Mooseker MS. 1994. Porcine myosin-VI: characterization of a new mammalian unconventional myosin. J. Cell Biol. 127:425-40
    • (1994) J. Cell Biol. , vol.127 , pp. 425-440
    • Hasson, T.1    Mooseker, M.S.2
  • 59
    • 0029163054 scopus 로고
    • Molecular motors, membrane movements and physiology: Emerging roles for myosins
    • Hasson T, Mooseker MS. 1995. Molecular motors, membrane movements and physiology: emerging roles for myosins. Curr. Opin. Cell Biol. 7:587-94
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 587-594
    • Hasson, T.1    Mooseker, M.S.2
  • 60
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-biphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Feslik SW. 1994. Pleckstrin homology domains bind to phosphatidylinositol-4,5-biphosphate. Nature 371:168-70
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Feslik, S.W.4
  • 61
    • 0025365190 scopus 로고
    • Binding of brush border myosin-I to phospholipid vesicles
    • Hayden SM, Wolenski JS, Mooseker MS. 1990. Binding of brush border myosin-I to phospholipid vesicles. J. Cell Biol. 111:443-51
    • (1990) J. Cell Biol. , vol.111 , pp. 443-451
    • Hayden, S.M.1    Wolenski, J.S.2    Mooseker, M.S.3
  • 62
    • 0028569487 scopus 로고
    • Multiple unconventional myosin domains of the intestinal brush border cytoskeleton
    • Heintzelman MB, Hasson T, Mooseker MS. 1994, Multiple unconventional myosin domains of the intestinal brush border cytoskeleton. J. Cell Sci. 107:3535-43
    • (1994) J. Cell Sci. , vol.107 , pp. 3535-3543
    • Heintzelman, M.B.1    Hasson, T.2    Mooseker, M.S.3
  • 63
    • 0026515395 scopus 로고
    • Distribution of the myosin-I-like ninaC proteins in the Drosophila retina and ultrastructural analysis of mutant phenotypes
    • Hicks JL, Williams DS. 1992. Distribution of the myosin-I-like ninaC proteins in the Drosophila retina and ultrastructural analysis of mutant phenotypes. J. Cell Sci. 101: 247-54
    • (1992) J. Cell Sci. , vol.101 , pp. 247-254
    • Hicks, J.L.1    Williams, D.S.2
  • 64
    • 0025223279 scopus 로고
    • A new Acanthamoeba myosin heavy chain
    • Horowitz JA, Hammer JA. 1990. A new Acanthamoeba myosin heavy chain. J. Biol. Chem. 265:20646-52
    • (1990) J. Biol. Chem. , vol.265 , pp. 20646-20652
    • Horowitz, J.A.1    Hammer, J.A.2
  • 65
    • 0023665165 scopus 로고
    • Identification of a new type of mammalian myosin heavy chain by molecular cloning
    • Hoshimaru M, Nakanishi S. 1987. Identification of a new type of mammalian myosin heavy chain by molecular cloning. J. Biol. Chem. 262:14625-32
    • (1987) J. Biol. Chem. , vol.262 , pp. 14625-14632
    • Hoshimaru, M.1    Nakanishi, S.2
  • 67
    • 0025096280 scopus 로고
    • Molecular cloning and amino acid sequence of brain L-glulamate decarboxylase
    • Huang WM, Reed-Fourquet L, Wu E, Wu JY. 1990. Molecular cloning and amino acid sequence of brain L-glulamate decarboxylase. Proc Natl. Acad Sci. USA 87:8491-95
    • (1990) Proc Natl. Acad Sci. USA , vol.87 , pp. 8491-8495
    • Huang, W.M.1    Reed-Fourquet, L.2    Wu, E.3    Wu, J.Y.4
  • 68
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston GC, Prendergast JA, Singer EA. 1991. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113:539-51
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, E.A.3
  • 69
    • 0027201087 scopus 로고
    • Sequence, expression pattern, intracellular localization and targeted disruption of the Dictyostelium myosin-ID heavy chain isoform
    • Jung G, Fukui Y, Martin B, Hammer JA. 1993. Sequence, expression pattern, intracellular localization and targeted disruption of the Dictyostelium myosin-ID heavy chain isoform. J. Biol. Chem 268:14981-90
    • (1993) J. Biol. Chem , vol.268 , pp. 14981-14990
    • Jung, G.1    Fukui, Y.2    Martin, B.3    Hammer, J.A.4
  • 70
    • 0028347643 scopus 로고
    • The actin binding site in the tail domain of Dictyostelium myosin IC (myoC) resides within the glycine- And proline-rich sequence (tail homology region 2)
    • Jung G, Hammer JA. 1994. The actin binding site in the tail domain of Dictyostelium myosin IC (myoC) resides within the glycine- and proline-rich sequence (tail homology region 2). FEBS Lett. 342:197-202
    • (1994) FEBS Lett. , vol.342 , pp. 197-202
    • Jung, G.1    Hammer, J.A.2
  • 71
    • 0028230508 scopus 로고
    • Regulation of calmodulin binding to the ATP extractable 110 kDa protein (myosin-I) from chicken duodenal brush border by 1,25-(OH)2D3
    • Kaune R, Munson S, Bikle DD. 1994. Regulation of calmodulin binding to the ATP extractable 110 kDa protein (myosin-I) from chicken duodenal brush border by 1,25-(OH)2D3. Biochim. Biophys. Acta 1190:329-36
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 329-336
    • Kaune, R.1    Munson, S.2    Bikle, D.D.3
  • 72
    • 0026576062 scopus 로고
    • Structural organization and expression of the gene for bovine myosin-I heavy chain
    • Kawakami HK, Moriyoshi K, Utsumi T, Nakanishi A. 1991. Structural organization and expression of the gene for bovine myosin-I heavy chain. J. Biochem. 111:302-9
    • (1991) J. Biochem. , vol.111 , pp. 302-309
    • Kawakami, H.K.1    Moriyoshi, K.2    Utsumi, T.3    Nakanishi, A.4
  • 73
    • 0026475396 scopus 로고
    • An unconventional myosin heavy chain gene from Drosophila melanogaster
    • Kellerman KA, Miller KG. 1992. An unconventional myosin heavy chain gene from Drosophila melanogaster. J. Cell Biol. 119:823-34
    • (1992) J. Cell Biol. , vol.119 , pp. 823-834
    • Kellerman, K.A.1    Miller, K.G.2
  • 75
    • 0028535275 scopus 로고
    • Molecular analysis of the myosin gene family in Arabidopsis thaliana
    • Kinkema M, Wang H, Schiefelbein J. 1994. Molecular analysis of the myosin gene family in Arabidopsis thaliana. Plant Mol. Biol. 26:2239-53
    • (1994) Plant Mol. Biol. , vol.26 , pp. 2239-2253
    • Kinkema, M.1    Wang, H.2    Schiefelbein, J.3
  • 76
    • 0028343414 scopus 로고
    • A myosin from a higher plant has structural similarities to class V myosins
    • Kinkema M, Schiefelbein J. 1994. A myosin from a higher plant has structural similarities to class V myosins. J. Mol. Biol. 239:591-97
    • (1994) J. Mol. Biol. , vol.239 , pp. 591-597
    • Kinkema, M.1    Schiefelbein, J.2
  • 77
    • 0027278759 scopus 로고
    • A myosin-like protein from a higher plant
    • Knight AE, Kendriek-Jones J, 1993. A myosin-like protein from a higher plant. J. Mol. Biol. 231:148-54
    • (1993) J. Mol. Biol. , vol.231 , pp. 148-154
    • Knight, A.E.1    Kendriek-Jones, J.2
  • 78
    • 8244256927 scopus 로고
    • Acanthamoeba myosin I: Past, present, and future
    • Korn ED, 1991. Acanthamoeba myosin I: past, present, and future. Curr. Topics Membr. 38:13-30
    • (1991) Curr. Topics Membr. , vol.38 , pp. 13-30
    • Korn, E.D.1
  • 81
    • 0027523295 scopus 로고
    • Molecular cloning of a mouse myosin-I expressed in brain
    • Koslovsky JS, Qian C, Jiang X, Mercer JA. 1993. Molecular cloning of a mouse myosin-I expressed in brain. FEBS Lett. 320:121-23
    • (1993) FEBS Lett. , vol.320 , pp. 121-123
    • Koslovsky, J.S.1    Qian, C.2    Jiang, X.3    Mercer, J.A.4
  • 82
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron SJ, Spudich JA. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA 83:6272-76
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 83
    • 0025347785 scopus 로고
    • Cytoplasmic streaming in plant cells
    • Kuroda K. 1990. Cytoplasmic streaming in plant cells. Int. Rev. Cytol. 121:267-307
    • (1990) Int. Rev. Cytol. , vol.121 , pp. 267-307
    • Kuroda, K.1
  • 84
    • 0026094639 scopus 로고
    • Immunolocalization of myosin I heavy chain kinase to isolated plasma membranes
    • Kulesza-Lipka D, Baines IC, Brzeska H, Korn ED. 1991. Immunolocalization of myosin I heavy chain kinase to isolated plasma membranes. J. Cell Biol. 115:109-19
    • (1991) J. Cell Biol. , vol.115 , pp. 109-119
    • Kulesza-Lipka, D.1    Baines, I.C.2    Brzeska, H.3    Korn, E.D.4
  • 85
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov SA, Langford CM, Weiss DG. 1992. Actin-dependent organelle movement in squid axoplasm. Nature 356:722-25
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, C.M.2    Weiss, D.G.3
  • 87
    • 0027984138 scopus 로고
    • GAPs for rho-related GTPases
    • Lamarche N, Hall A. 1994. GAPs for rho-related GTPases. Trends Genet. 10:436-40
    • (1994) Trends Genet. , vol.10 , pp. 436-440
    • Lamarche, N.1    Hall, A.2
  • 88
    • 0028942256 scopus 로고
    • Actin- And microtubule dependent organelle motors: Interrelationships between the two motility systems
    • Langford GM. 1995. Actin- and microtubule dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7:82-88
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 89
    • 0028093376 scopus 로고
    • Movement of axoplasmic organdies on actin filaments assembled onto aerosomal processes: Evidence for a barbed-end-directed organelle motor
    • Langford GM, Kuznetzov SA, Johnson D, Cohen DL, Weiss DG. 1994. Movement of axoplasmic organdies on actin filaments assembled onto aerosomal processes: evidence for a barbed-end-directed organelle motor. J. Cell Sci. 107:2291-98
    • (1994) J. Cell Sci. , vol.107 , pp. 2291-2298
    • Langford, G.M.1    Kuznetzov, S.A.2    Johnson, D.3    Cohen, D.L.4    Weiss, D.G.5
  • 90
    • 0025276537 scopus 로고
    • Calmodulin-binding proteins ami calcium/calmodulin-regulated enzyme activities associated with brain actomyosin
    • Larson RE, Espindola FS, Espreafico EM. 1990. Calmodulin-binding proteins ami calcium/calmodulin-regulated enzyme activities associated with brain actomyosin. J. Neurochem. 54:1288-94
    • (1990) J. Neurochem. , vol.54 , pp. 1288-1294
    • Larson, R.E.1    Espindola, F.S.2    Espreafico, E.M.3
  • 91
    • 0024251542 scopus 로고
    • A novel 190 kDa calmodulin-binding protein associated with brain actomyosin
    • Larson RE, Pitta DE, Ferro JA. 1988. A novel 190 kDa calmodulin-binding protein associated with brain actomyosin. Braz. J. Med. Biol. Res. 21:213-17
    • (1988) Braz. J. Med. Biol. Res. , vol.21 , pp. 213-217
    • Larson, R.E.1    Pitta, D.E.2    Ferro, J.A.3
  • 92
    • 0027384528 scopus 로고
    • Isolation and characterization of three Dictyostelium myosin-I isoszymes
    • Lee S-F, Coté GP. 1993. Isolation and characterization of three Dictyostelium myosin-I isoszymes. J. Biol. Chem. 268:20923-29
    • (1993) J. Biol. Chem. , vol.268 , pp. 20923-20929
    • Lee, S.-F.1    Coté, G.P.2
  • 93
    • 0026663083 scopus 로고
    • Evidence for a new member of the myosin I family from mammalian brain
    • Li D, Chantler PD. 1992. Evidence for a new member of the myosin I family from mammalian brain. J. Neurochem. 59:1344-51
    • (1992) J. Neurochem. , vol.59 , pp. 1344-1351
    • Li, D.1    Chantler, P.D.2
  • 94
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin related gene
    • Lillie S, Brown S, 1992. Suppression of a myosin defect by a kinesin related gene. Nature 356:358-61
    • (1992) Nature , vol.356 , pp. 358-361
    • Lillie, S.1    Brown, S.2
  • 95
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventinal myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie S, Brown S. 1994. Immunofluorescence localization of the unconventinal myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J. Cell Biol. 125:825-42
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.1    Brown, S.2
  • 96
    • 0027288910 scopus 로고
    • A putative modular domain present in diverse signaling proteins
    • Mayer BJ, Ren R, Clark K, Baltimore D. 1993. A putative modular domain present in diverse signaling proteins. Cell 73:629-30
    • (1993) Cell , vol.73 , pp. 629-630
    • Mayer, B.J.1    Ren, R.2    Clark, K.3    Baltimore, D.4
  • 97
    • 0028871168 scopus 로고
    • MyoA of Aspergillus nidulans encodes an essential myosin-1 required for secretion and polarized growth
    • McGoldrick CA, Graver C, May GS. 1995. myoA of Aspergillus nidulans encodes an essential myosin-1 required for secretion and polarized growth. J. Cell Biol. 128:577-87
    • (1995) J. Cell Biol. , vol.128 , pp. 577-587
    • McGoldrick, C.A.1    Graver, C.2    May, G.S.3
  • 99
    • 0028359778 scopus 로고
    • Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos
    • Mermall V, McNally JG, Miller KG. 1994. Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos. Nature 369:560-62
    • (1994) Nature , vol.369 , pp. 560-562
    • Mermall, V.1    McNally, J.G.2    Miller, K.G.3
  • 100
    • 0029048771 scopus 로고
    • The 95F unconventional myosin is required for proper organization of the Drosophila syncytial blastoderm
    • Mermall V, Miller KG. 1995. The 95F unconventional myosin is required for proper organization of the Drosophila syncytial blastoderm. J. Cell Biol. 129:1575-88
    • (1995) J. Cell Biol. , vol.129 , pp. 1575-1588
    • Mermall, V.1    Miller, K.G.2
  • 101
    • 0027960895 scopus 로고
    • Molecular cloning of a myosin 1β isozyme that may mediate adaptation by hair cells of the bullfrog's internal ear
    • Metcalf AB, Chelliah Y, Hudspeth AJ. 1994. Molecular cloning of a myosin 1β isozyme that may mediate adaptation by hair cells of the bullfrog's internal ear. Proc Natl. Acad. Sci. USA 91:11821-25
    • (1994) Proc Natl. Acad. Sci. USA , vol.91 , pp. 11821-11825
    • Metcalf, A.B.1    Chelliah, Y.2    Hudspeth, A.J.3
  • 102
    • 0029166933 scopus 로고
    • Identification and localization of three classes of myosins in pollen lubes of Liliuin longiflorum and Nicotiana alata
    • Miller DD, Scrodilis SP, Hepler PK. 1995. Identification and localization of three classes of myosins in pollen lubes of Liliuin longiflorum and Nicotiana alata. J. Cell Sci. 108:2549-53
    • (1995) J. Cell Sci. , vol.108 , pp. 2549-2553
    • Miller, D.D.1    Scrodilis, S.P.2    Hepler, P.K.3
  • 103
    • 0024744488 scopus 로고
    • Plasma membrane association of Acanthamoeba myosin I
    • Miyata H, Bowers B, Korn ED. 1989. Plasma membrane association of Acanthamoeba myosin I. J. Cell Biol. 109:1519-28
    • (1989) J. Cell Biol. , vol.109 , pp. 1519-1528
    • Miyata, H.1    Bowers, B.2    Korn, E.D.3
  • 104
    • 0027571097 scopus 로고
    • PCR-dependent amplification and sequence characterization of partial cDNAs encoding myosin-like proteins in Anemia phyllitidis (L.) Sw. and Arabidiopsis thaliana (L.) Heynh
    • Moepps B, Conrad S, Schraudolf H. 1993. PCR-dependent amplification and sequence characterization of partial cDNAs encoding myosin-like proteins in Anemia phyllitidis (L.) Sw. and Arabidiopsis thaliana (L.) Heynh. Plant Mol. Biol. 21:1077-83
    • (1993) Plant Mol. Biol. , vol.21 , pp. 1077-1083
    • Moepps, B.1    Conrad, S.2    Schraudolf, H.3
  • 105
    • 0024284065 scopus 로고
    • The Drosophila ninaC locus encodes two photoreceptor cell specific proteins with domains homologous to protein kinases and the myosin heavy chain head
    • Montell C, Rubin GM. 1988. The Drosophila ninaC locus encodes two photoreceptor cell specific proteins with domains homologous to protein kinases and the myosin heavy chain head. Cell 52:757-72
    • (1988) Cell , vol.52 , pp. 757-772
    • Montell, C.1    Rubin, G.M.2
  • 106
    • 0025303429 scopus 로고
    • Interaction of the murine dilute suppressor gene (dsu) with fourteen coat color mutations
    • Moore KJ, Swing DA, Copeland NG, Jenkins NA. 1990. Interaction of the murine dilute suppressor gene (dsu) with fourteen coat color mutations. Genetics 125:421-30
    • (1990) Genetics , vol.125 , pp. 421-430
    • Moore, K.J.1    Swing, D.A.2    Copeland, N.G.3    Jenkins, N.A.4
  • 107
    • 0344914021 scopus 로고
    • A multitude of myosins
    • Mooseker MS. 1993. A multitude of myosins. Curr. Biol. 3:245-48
    • (1993) Curr. Biol. , vol.3 , pp. 245-248
    • Mooseker, M.S.1
  • 108
    • 0024312342 scopus 로고
    • The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin-1) is a mechanoenzyme
    • Mooseker MS, Coleman TR. 1989. The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin-1) is a mechanoenzyme. J. Cell Biol. 108:2395-400
    • (1989) J. Cell Biol. , vol.108 , pp. 2395-2400
    • Mooseker, M.S.1    Coleman, T.R.2
  • 110
    • 0028824434 scopus 로고
    • Characterization of myosin-IA and myosin-IB, two unconventional myosins associated with the Drosophila brush border cytoskeleton
    • In press
    • Morgan NS, Heintzelman MB, Mooseker MS, 1995. Characterization of myosin-IA and myosin-IB, two unconventional myosins associated with the Drosophila brush border cytoskeleton. Development. In press
    • (1995) Development
    • Morgan, N.S.1    Heintzelman, M.B.2    Mooseker, M.S.3
  • 111
    • 0028309462 scopus 로고
    • The molecular cloning characterization of Drosophilla melanogaster myosin-IA and myosin-IB
    • Morgan NS, Skovronsky DM, Artavanis-Tskakonas S, Mooseker MS. 1994. The molecular cloning characterization of Drosophilla melanogaster myosin-IA and myosin-IB. J. Mol. Biol. 239:347-56
    • (1994) J. Mol. Biol. , vol.239 , pp. 347-356
    • Morgan, N.S.1    Skovronsky, D.M.2    Artavanis-Tskakonas, S.3    Mooseker, M.S.4
  • 115
    • 0015834603 scopus 로고
    • Acanthamoeba myosin: I. Isolation from Acanthamoeba costellanii of an enzyme similar to muscle myosin
    • Pollard TD, Korn ED. 1973. Acanthamoeba myosin: I. Isolation from Acanthamoeba costellanii of an enzyme similar to muscle myosin. J. Biol. Chem 248:4682-90
    • (1973) J. Biol. Chem , vol.248 , pp. 4682-4690
    • Pollard, T.D.1    Korn, E.D.2
  • 116
    • 0026604808 scopus 로고
    • Differential localizations and requirements for the two Drosophila ninaC kinase/myosins in photoreceptor cells
    • Porter JA, Hicks JL, Williams DS, Montell C. 1992. Differential localizations and requirements for the two Drosophila ninaC kinase/myosins in photoreceptor cells. J. Cell Biol. 116:683-93
    • (1992) J. Cell Biol. , vol.116 , pp. 683-693
    • Porter, J.A.1    Hicks, J.L.2    Williams, D.S.3    Montell, C.4
  • 117
    • 0027292230 scopus 로고
    • Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis
    • Porter JA, Montell C. 1993. Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis. J. Cell Biol. 122:601-12
    • (1993) J. Cell Biol. , vol.122 , pp. 601-612
    • Porter, J.A.1    Montell, C.2
  • 118
    • 0027768695 scopus 로고
    • Dependence of calmodulin localization in the retina on the NINAC unconventional myosin
    • Porter JA, Yu M, Doberstein SK, Pollard TD, Montell C, 1993. Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science 262:1038-42
    • (1993) Science , vol.262 , pp. 1038-1042
    • Porter, J.A.1    Yu, M.2    Doberstein, S.K.3    Pollard, T.D.4    Montell, C.5
  • 119
    • 0027373678 scopus 로고
    • Cloning of the ALL-1 fusion protein, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation
    • Prasad R, Gu Y, Alder T, Nakamura T, Canaani O, et al. 1993. Cloning of the ALL-1 fusion protein, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation. Cancer Res. 53:5624-28
    • (1993) Cancer Res. , vol.53 , pp. 5624-5628
    • Prasad, R.1    Gu, Y.2    Alder, T.3    Nakamura, T.4    Canaani, O.5
  • 121
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment IH, Holden M, Whittaker CB, Yohn M, Lorenz KC, et al. 1993a. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.H.1    Holden, M.2    Whittaker, C.B.3    Yohn, M.4    Lorenz, K.C.5
  • 125
    • 4243962932 scopus 로고
    • Purification and characterization of high-molecular-weight myosin-I (HMMI), an unconventional myosin from Acanthamoeba
    • Abstr.
    • Repezza M, Sellers J, Urrutia R, Hammer J. 1994. Purification and characterization of high-molecular-weight myosin-I (HMMI), an unconventional myosin from Acanthamoeba. Mol. Biol. Cell Suppl. 5:277a (Abstr.)
    • (1994) Mol. Biol. Cell Suppl. , vol.5
    • Repezza, M.1    Sellers, J.2    Urrutia, R.3    Hammer, J.4
  • 126
    • 0028231727 scopus 로고
    • The GPQ-rich Segment of Dictyostelium myosin-IB contains an actin binding site
    • Rosenfeld SS, Rener B. 1994. The GPQ-rich Segment of Dictyostelium myosin-IB contains an actin binding site. Biochemistry 33:2322-28
    • (1994) Biochemistry , vol.33 , pp. 2322-2328
    • Rosenfeld, S.S.1    Rener, B.2
  • 127
    • 0027499951 scopus 로고
    • Identification, characterization and cloning of myr 1, a mammalian myosin-I
    • Ryppert C, Kroschewski R, Bähler M. 1993. Identification, characterization and cloning of myr 1, a mammalian myosin-I. J. Cell Biol. 120:1393-403
    • (1993) J. Cell Biol. , vol.120 , pp. 1393-1403
    • Ryppert, C.1    Kroschewski, R.2    Bähler, M.3
  • 128
    • 0026658159 scopus 로고
    • CDNA encoding the chicken ortholog of the mouse dilute gene product
    • Sanders G, Lichte B, Meyer HE, Kilimann MW. 1992. cDNA encoding the chicken ortholog of the mouse dilute gene product. FEBS Lett. 311:295-98
    • (1992) FEBS Lett. , vol.311 , pp. 295-298
    • Sanders, G.1    Lichte, B.2    Meyer, H.E.3    Kilimann, M.W.4
  • 129
    • 0027220271 scopus 로고
    • Three-dimensional atomic model of f-actin decorated with Dictyostelium decorated with royosin s1
    • Schroder RR, Manstein DJ, Jahn W, Holden H, Rayment I. 1993. Three-dimensional atomic model of f-actin decorated with Dictyostelium decorated with royosin s1. Nature 364:171-74
    • (1993) Nature , vol.364 , pp. 171-174
    • Schroder, R.R.1    Manstein, D.J.2    Jahn, W.3    Holden, H.4    Rayment, I.5
  • 130
    • 84966140454 scopus 로고
    • A lethal allele of dilute in the house mouse
    • Searle AG. 1952. A lethal allele of dilute in the house mouse. Heredity 6:395-401
    • (1952) Heredity , vol.6 , pp. 395-401
    • Searle, A.G.1
  • 131
    • 0027479904 scopus 로고
    • Mammalian myosin 1α, 1β, and 1γ: New widely expressed genes of the myosin I family
    • Sherr EH, Joyce MP, Green LA. 1993. Mammalian myosin 1α, 1β, and 1γ: new widely expressed genes of the myosin I family. J. Cell Biol. 120:1405-16
    • (1993) J. Cell Biol. , vol.120 , pp. 1405-1416
    • Sherr, E.H.1    Joyce, M.P.2    Green, L.A.3
  • 132
    • 0001850991 scopus 로고
    • Dilute and Leaden, the p-locus, Ruby-Eye, and Ruby-Eye-2
    • ed. WK Silvers, New York: Springer Verlag
    • Silvers WK. 1979. Dilute and Leaden, the p-locus, Ruby-Eye, and Ruby-Eye-2. In Coat Colors of Mice: A Model for Mammalian Gene Action and Interaction, ed. WK Silvers, pp. 83-89; 104-7. New York: Springer Verlag
    • (1979) Coat Colors of Mice: A Model for Mammalian Gene Action and Interaction , pp. 83-89
    • Silvers, W.K.1
  • 134
    • 0003154314 scopus 로고
    • Molecular cloning of myosins from the bullfrog saccular macula: A candidate for the hair cell adaptation motor
    • Sole CF, Derfler RH, Duyk GM, Corey DR. 1994. Molecular cloning of myosins from the bullfrog saccular macula: a candidate for the hair cell adaptation motor. Aud. Neurosci. 1:63-75
    • (1994) Aud. Neurosci. , vol.1 , pp. 63-75
    • Sole, C.F.1    Derfler, R.H.2    Duyk, G.M.3    Corey, D.R.4
  • 135
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich JA. 1994. How molecular motors work. Nature 372:515-18
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 137
    • 0025924752 scopus 로고
    • 2+-ATPase activity of brush border myosin-1 with three or four calmodulin light chains but inhibits with less than two bound
    • 2+-ATPase activity of brush border myosin-1 with three or four calmodulin light chains but inhibits with less than two bound. J. Biol. Chem. 266:1312-19
    • (1991) J. Biol. Chem. , vol.266 , pp. 1312-1319
    • Swanljung-Collins, H.1    Collins, J.H.2
  • 138
    • 0026673876 scopus 로고
    • 2+-stimulated binding of myosin-I to phosphatidylserine concerted with calmodulin dissociation
    • 2+-stimulated binding of myosin-I to phosphatidylserine concerted with calmodulin dissociation. J. Biol. Chem. 267:3445-54
    • (1992) J. Biol. Chem. , vol.267 , pp. 3445-3454
    • Swanljung-Collins, H.1    Collins, J.H.2
  • 139
    • 85006166311 scopus 로고
    • Factors controlling the reassembly of the microvillus border of the small intestine of the salamander
    • Tilney LG, Cardell RR. 1970. Factors controlling the reassembly of the microvillus border of the small intestine of the salamander. J. Cell Biol. 47:408-22
    • (1970) J. Cell Biol. , vol.47 , pp. 408-422
    • Tilney, L.G.1    Cardell, R.R.2
  • 140
    • 0028111421 scopus 로고
    • Discovery of myosin genes by physical mapping in Dictyostelium
    • Titus MA, Kyspa A, Loomis, WF. 1994. Discovery of myosin genes by physical mapping in Dictyostelium. Proc. Natl. Acad. Sci. USA 91:9446-50
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9446-9450
    • Titus, M.A.1    Kyspa, A.2    Loomis, W.F.3
  • 141
    • 0024755654 scopus 로고
    • Multiple actin-based motor genes in Dictyostelium
    • Titus MA, Warrick HM, Spudich JA. 1989. Multiple actin-based motor genes in Dictyostelium. Cell Regul. 1:55-63
    • (1989) Cell Regul. , vol.1 , pp. 55-63
    • Titus, M.A.1    Warrick, H.M.2    Spudich, J.A.3
  • 142
    • 0027399722 scopus 로고
    • The unconventional myosin encoded by the myoA gene plays a role in Dictyostelium motility
    • Titus MA, Wessels D, Spudich JA, Soll D. 1993. The unconventional myosin encoded by the myoA gene plays a role in Dictyostelium motility. Mol. Biol. Cell 4:233-46
    • (1993) Mol. Biol. Cell , vol.4 , pp. 233-246
    • Titus, M.A.1    Wessels, D.2    Spudich, J.A.3    Soll, D.4
  • 143
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin binding face of myosin
    • Uyeda TQP, Ruppel KM, Spudich JA. 1994. Enzymatic activities correlate with chimaeric substitutions at the actin binding face of myosin. Nature 368:567-69
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 144
    • 0026779476 scopus 로고
    • Tissue distribution and subcellular localization of mammalian myosin-I
    • Wagner M, Barylko B, Albanesi JP. 1992. Tissue distribution and subcellular localization of mammalian myosin-I. J. Cell Biol. 119:163-70
    • (1992) J. Cell Biol. , vol.119 , pp. 163-170
    • Wagner, M.1    Barylko, B.2    Albanesi, J.P.3
  • 145
    • 0023484279 scopus 로고
    • Myosin structure and function in cell motility
    • Warrick HM, Spudich JA. 1987. Myosin structure and function in cell motility. Annu. Rev. Cell Biol. 3:379-421
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 379-421
    • Warrick, H.M.1    Spudich, J.A.2
  • 146
    • 9844262526 scopus 로고
    • Dilute melanocytes exhibit altered intracellular melanosome distribution
    • Abstr.
    • Wei MC, Ipe V, Mercer JA. 1994. Dilute melanocytes exhibit altered intracellular melanosome distribution. Mol. Biol. Cell Suppl. 5:381a (Abstr.)
    • (1994) Mol. Biol. Cell Suppl. , vol.5
    • Wei, M.C.1    Ipe, V.2    Mercer, J.A.3
  • 147
    • 0028815440 scopus 로고
    • Defective myosin VIIIA gene responsible for Usher syndrome type IB
    • Weil D, Blanchard S, Kaplan J, Guilford P, Gibson F, et al. 1995. Defective myosin VIIIA gene responsible for Usher syndrome type IB. Nature 374:60-61
    • (1995) Nature , vol.374 , pp. 60-61
    • Weil, D.1    Blanchard, S.2    Kaplan, J.3    Guilford, P.4    Gibson, F.5
  • 149
    • 0028157537 scopus 로고
    • A novel 130-kDa rat liver myosin-1 will translocate actin filaments
    • Williams R, Coluccio LM. 1994. A novel 130-kDa rat liver myosin-1 will translocate actin filaments. Cell Motil. Cytoskelet. 27:41-48
    • (1994) Cell Motil. Cytoskelet. , vol.27 , pp. 41-48
    • Williams, R.1    Coluccio, L.M.2
  • 150
    • 0029025172 scopus 로고
    • Regulation of calmodulin-binding myosins
    • Wolenski JS. 1995. Regulation of calmodulin-binding myosins. Trends Cell Biol 5:310-16
    • (1995) Trends Cell Biol , vol.5 , pp. 310-316
    • Wolenski, J.S.1
  • 151
    • 0027917985 scopus 로고
    • In vitro motilities of the unconventional myosins, brush border myosin-I and chick braie myosin-V exhibit assay-dependent differences in velocity
    • Wolenski JS, Cheney RE, Forscher P, Mooseker MS. 1993a. In vitro motilities of the unconventional myosins, brush border myosin-I and chick braie myosin-V exhibit assay-dependent differences in velocity. J. Exp. Zool. 267:33-39
    • (1993) J. Exp. Zool. , vol.267 , pp. 33-39
    • Wolenski, J.S.1    Cheney, R.E.2    Forscher, P.3    Mooseker, M.S.4
  • 152
    • 0028930479 scopus 로고
    • In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay
    • Wolenski JS, Cheney RE, Mooseker MS, Forscher P. 1995. In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay. J. Cell Sci. 108:1489-96
    • (1995) J. Cell Sci. , vol.108 , pp. 1489-1496
    • Wolenski, J.S.1    Cheney, R.E.2    Mooseker, M.S.3    Forscher, P.4
  • 153
    • 0027219972 scopus 로고
    • Calciuin-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry
    • Wolenski JS, Hayden SM, Forscher P, Mooseker MS. 1993b. Calciuin-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry. J. Cell Biol. 122:613-21
    • (1993) J. Cell Biol. , vol.122 , pp. 613-621
    • Wolenski, J.S.1    Hayden, S.M.2    Forscher, P.3    Mooseker, M.S.4
  • 155
    • 0026776714 scopus 로고
    • Association of calmodulin and an unconventional myosis with the contractile vacuole complex of Dictyostelium discoideum
    • Zhu Q, Clarke M. 1992. Association of calmodulin and an unconventional myosis with the contractile vacuole complex of Dictyostelium discoideum. J. Cell Biol. 118:347-58
    • (1992) J. Cell Biol. , vol.118 , pp. 347-358
    • Zhu, Q.1    Clarke, M.2
  • 156
    • 0028266266 scopus 로고
    • A novel myosin-I from bovine adrenal gland
    • Zhu T, Ikebe M. 1994. A novel myosin-I from bovine adrenal gland. FEBS Lett. 339:31-36
    • (1994) FEBS Lett. , vol.339 , pp. 31-36
    • Zhu, T.1    Ikebe, M.2
  • 157
    • 0028909736 scopus 로고
    • Phospholipid membrane-associated brush border myosin-I activity
    • Zot HG. 1995. Phospholipid membrane-associated brush border myosin-I activity. Cell Motil. Cytoskelet. 30:26-37
    • (1995) Cell Motil. Cytoskelet. , vol.30 , pp. 26-37
    • Zot, H.G.1
  • 158
    • 0026595130 scopus 로고
    • Myosin-I moves actin filaments on a phospholipid substrate: Implications for membrane targeting
    • Zot HG, Doberstein SK, Pollard TD. 1991. Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting. J. Cell Biol. 116:367-76
    • (1991) J. Cell Biol. , vol.116 , pp. 367-376
    • Zot, H.G.1    Doberstein, S.K.2    Pollard, T.D.3


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