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Volumn 64, Issue 1, 2007, Pages 19-48

Myosin16b: The COOH-tail region directs localization to the nucleus and overexpression delays S-phase progression

Author keywords

Actin; Brain development; Subnuclear foci; Unconventional myosin

Indexed keywords

ACTIN; ANKYRIN; BROXURIDINE; CELL MARKER; CYCLINE; ENHANCED GREEN FLUORESCENT PROTEIN; ISOPROTEIN; MYOSIN; MYOSIN 16A; MYOSIN 16B; NUCLEAR PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 1; PROFILIN;

EID: 33845529654     PISSN: 08861544     EISSN: 10970169     Source Type: Journal    
DOI: 10.1002/cm.20162     Document Type: Article
Times cited : (47)

References (115)
  • 2
    • 0032101295 scopus 로고    scopus 로고
    • Differential subcellular localization of protein phosphatase-1 α, γ1, and δ isoforms during both interphase and mitosis in mammalian cells
    • Andreassen PR, Lacroix FB, Villa-Moruzzi E, Margolis RL. 1998. Differential subcellular localization of protein phosphatase-1 α, γ1, and δ isoforms during both interphase and mitosis in mammalian cells. J Cell Biol 141:1207-1215.
    • (1998) J Cell Biol , vol.141 , pp. 1207-1215
    • Andreassen, P.R.1    Lacroix, F.B.2    Villa-Moruzzi, E.3    Margolis, R.L.4
  • 3
    • 0027479449 scopus 로고
    • Immunocytochemical analysis of the coiled body in the cell cycle and during cell proliferation
    • Antrade LEC, Tan EM, Chan EKL. 1993. Immunocytochemical analysis of the coiled body in the cell cycle and during cell proliferation. Proc Natl Acad Sci USA 90:1947-1951.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1947-1951
    • Antrade, L.E.C.1    Tan, E.M.2    Chan, E.K.L.3
  • 4
    • 0038107500 scopus 로고    scopus 로고
    • Myo6 facilitates the translocation of endocytic vesicle from cell peripheries
    • Aschenbrenner L, Lee T, Hasson T. 2003. Myo6 facilitates the translocation of endocytic vesicle from cell peripheries. Mol Cell Biol 14:2728-2743.
    • (2003) Mol Cell Biol , vol.14 , pp. 2728-2743
    • Aschenbrenner, L.1    Lee, T.2    Hasson, T.3
  • 5
    • 0003276780 scopus 로고
    • Structural and functional organization of the nuclear matrix
    • Berezney R, Jeon KW, editors 162B. San Diego, CA: Academic Press
    • Berezney R, Jeon KW, editors 1995. Structural and Functional Organization of the Nuclear Matrix (International Reviews in Cytology, Vols. 162A, 162B). San Diego, CA: Academic Press.
    • (1995) International Reviews in Cytology , vol.162 A
  • 6
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • Berg JS, Cheney RE. 2002. Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat Cell Biol 4:246-250.
    • (2002) Nat Cell Biol , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 10
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • Bohnsack MT, Stuven T, Kuhn C, Cordes VC, Gorlich D. 2006. A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nat Cell Biol 8:257-263.
    • (2006) Nat Cell Biol , vol.8 , pp. 257-263
    • Bohnsack, M.T.1    Stuven, T.2    Kuhn, C.3    Cordes, V.C.4    Gorlich, D.5
  • 11
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • Borden KLB. 2002. Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies. Mol Cell Biol 22:5259-5269.
    • (2002) Mol Cell Biol , vol.22 , pp. 5259-5269
    • Borden, K.L.B.1
  • 13
    • 2142823918 scopus 로고    scopus 로고
    • "On the move"ments of nuclear components in living cells
    • Bubulya PA, Spector DL. 2004. "On the move"ments of nuclear components in living cells. Exp Cell Res 296:4-11.
    • (2004) Exp Cell Res , vol.296 , pp. 4-11
    • Bubulya, P.A.1    Spector, D.L.2
  • 14
    • 0036901155 scopus 로고    scopus 로고
    • Myosin VI, an actin motor for membrane traffic and cell migration
    • Buss F, Luzio JP, Kendrick-Jones J. 2002. Myosin VI, an actin motor for membrane traffic and cell migration. Traffic 3:851-858.
    • (2002) Traffic , vol.3 , pp. 851-858
    • Buss, F.1    Luzio, J.P.2    Kendrick-Jones, J.3
  • 15
    • 0030722709 scopus 로고    scopus 로고
    • Developmental expression, pattern of distribution, and effect on cell aggregation implicate a neuron-glial junctional domain protein in neuronal migration
    • Cameron RS, Ruffin JW, Cho NK, Cameron PL, Rakic P. 1997. Developmental expression, pattern of distribution, and effect on cell aggregation implicate a neuron-glial junctional domain protein in neuronal migration. J Comp Neurol 387:467-488.
    • (1997) J Comp Neurol , vol.387 , pp. 467-488
    • Cameron, R.S.1    Ruffin, J.W.2    Cho, N.K.3    Cameron, P.L.4    Rakic, P.5
  • 16
    • 0027494125 scopus 로고
    • Reversal of terminal differentiation and control of DNA replication: Cyclin A and cdk2 specifically localize at subnuclear sites of DNA replication
    • Cardoso MC, Leonhardt H, Nidal-Ginard B. 1993. Reversal of terminal differentiation and control of DNA replication: Cyclin A and cdk2 specifically localize at subnuclear sites of DNA replication. Cell 74:979-992.
    • (1993) Cell , vol.74 , pp. 979-992
    • Cardoso, M.C.1    Leonhardt, H.2    Nidal-Ginard, B.3
  • 17
    • 0346728803 scopus 로고    scopus 로고
    • Functional diversity of protein phosphatase-1, a cellular economizer and reset button
    • Ceulemans H, Bollen M. 2004. Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol Rev 84:1-39.
    • (2004) Physiol Rev , vol.84 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 18
    • 0027400877 scopus 로고
    • Ultrastructural radioautographic analysis of neurogenesis in the hypothalamus in the adult frog, Rana temporaria, with special reference to physiological regeneration of the preoptic nucleus. I. Ventricular zone cell proliferation
    • Chetverukhin VK, Polenov AL. 1993. Ultrastructural radioautographic analysis of neurogenesis in the hypothalamus in the adult frog, Rana temporaria, with special reference to physiological regeneration of the preoptic nucleus. I. Ventricular zone cell proliferation. Cell Tissue Res 271:341-350.
    • (1993) Cell Tissue Res , vol.271 , pp. 341-350
    • Chetverukhin, V.K.1    Polenov, A.L.2
  • 19
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1-Targeted in many directions
    • Cohen PTW. 2002. Protein phosphatase 1-Targeted in many directions. J Cell Sci 115:241-256.
    • (2002) J Cell Sci , vol.115 , pp. 241-256
    • Cohen, P.T.W.1
  • 21
    • 0016698833 scopus 로고
    • Interaction of actin with phalloidin: Polymerization and stabilization of F-actin
    • Dancker P, Low I, Hasselbach W, Wieland T. 1975. Interaction of actin with phalloidin: Polymerization and stabilization of F-actin. Biochim Biophys Acta 400:407-414.
    • (1975) Biochim Biophys Acta , vol.400 , pp. 407-414
    • Dancker, P.1    Low, I.2    Hasselbach, W.3    Wieland, T.4
  • 24
    • 0034026194 scopus 로고    scopus 로고
    • The HP1 protein family: Getting a grip on chromatin
    • Eissenberg JC, Elgin SCR. 2000. The HP1 protein family: Getting a grip on chromatin. Curr Opin Genet Dev 10:204-210.
    • (2000) Curr Opin Genet Dev , vol.10 , pp. 204-210
    • Eissenberg, J.C.1    Elgin, S.C.R.2
  • 25
    • 33644856260 scopus 로고    scopus 로고
    • New insights into myosin evolution and classification
    • Foth BJ, Goedecke MC, Soldati D. 2006. New insights into myosin evolution and classification. Proc Natl Acad Sci USA 103:3681-3686.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3681-3686
    • Foth, B.J.1    Goedecke, M.C.2    Soldati, D.3
  • 27
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M, Ohno M, Yoshida M, Mattaj IW. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 28
  • 29
    • 0018428638 scopus 로고
    • Nuclear actin bundles in Amoeba, Dictyostelium, and human HeLa cells induced by dimethyl sulfoxide
    • Fukui Y, Katsumaru H. 1979. Nuclear actin bundles in Amoeba, Dictyostelium, and human HeLa cells induced by dimethyl sulfoxide. Exp Cell Res 120:451-455.
    • (1979) Exp Cell Res , vol.120 , pp. 451-455
    • Fukui, Y.1    Katsumaru, H.2
  • 30
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves MA, Holmes KC. 1999. Structural mechanism of muscle contraction. Annu Rev Biochem 68:687-728.
    • (1999) Annu Rev Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 33
    • 0036532235 scopus 로고    scopus 로고
    • Heterochromatin: New possibilities for the inheritance of structure
    • Grewal SIS, Elgin SCR. 2002. Heterochromatin: New possibilities for the inheritance of structure. Curr Opin Genet Dev 12:178-187.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 178-187
    • Grewal, S.I.S.1    Elgin, S.C.R.2
  • 34
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • Grozinger CM, Schreiber SL. 2000. Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc Natl Acad Sci USA 97:7835-7840.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 35
    • 33644852058 scopus 로고    scopus 로고
    • Actin and myosin as transcription factors
    • Grummt I. 2006. Actin and myosin as transcription factors. Curr Opin Genet Dev 16:191-196.
    • (2006) Curr Opin Genet Dev , vol.16 , pp. 191-196
    • Grummt, I.1
  • 36
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart GW. 1997. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu Rev Biochem 66:315-335.
    • (1997) Annu Rev Biochem , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 37
    • 0037382227 scopus 로고    scopus 로고
    • Transcription elongation by RNA polymerase II
    • Hartzog GA. 2003. Transcription elongation by RNA polymerase II. Curr Opin Genet Dev 13:119-126.
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 119-126
    • Hartzog, G.A.1
  • 38
    • 0041327729 scopus 로고    scopus 로고
    • Myosin VI: Two distinct roles in endocytosis
    • Hasson T. 2003. Myosin VI: Two distinct roles in endocytosis. J Cell Sci 116:3453-3461.
    • (2003) J Cell Sci , vol.116 , pp. 3453-3461
    • Hasson, T.1
  • 39
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He D, Nickerson JA, Penman S. 1990. Core filaments of the nuclear matrix. J Cell Biol 110:569-580.
    • (1990) J Cell Biol , vol.110 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penman, S.3
  • 40
    • 0035185978 scopus 로고    scopus 로고
    • Cell motility: Proline-rich proteins promote protrusions
    • Holt MR, Koffer A. 2001. Cell motility: Proline-rich proteins promote protrusions. Trends Cell Biol 11:38-46.
    • (2001) Trends Cell Biol , vol.11 , pp. 38-46
    • Holt, M.R.1    Koffer, A.2
  • 43
    • 33644752095 scopus 로고    scopus 로고
    • Myosin VI is a mediator of the p53-dependent cell survival pathway
    • Jung EJ, Liu G, Zhou W, Chen X. 2006. Myosin VI is a mediator of the p53-dependent cell survival pathway. Mol Cell Biol 26:2175-2186.
    • (2006) Mol Cell Biol , vol.26 , pp. 2175-2186
    • Jung, E.J.1    Liu, G.2    Zhou, W.3    Chen, X.4
  • 45
    • 0031045565 scopus 로고    scopus 로고
    • PCNA: Structure, function and interactions
    • Kelman Z. 1997. PCNA: Structure, function and interactions. Oncogene 14:629-640.
    • (1997) Oncogene , vol.14 , pp. 629-640
    • Kelman, Z.1
  • 46
    • 0033545920 scopus 로고    scopus 로고
    • Continuation of neurogenesis in the hippocampus of the adult macaque monkey
    • Kornack DR, Rakic P. 1999. Continuation of neurogenesis in the hippocampus of the adult macaque monkey. Proc Natl Acad Sci USA 96:5768-5773.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5768-5773
    • Kornack, D.R.1    Rakic, P.2
  • 47
    • 0033134794 scopus 로고    scopus 로고
    • Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25
    • Kumagai A, Dunphy WG. 1999. Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25. Genes Dev 13:1067-1072.
    • (1999) Genes Dev , vol.13 , pp. 1067-1072
    • Kumagai, A.1    Dunphy, W.G.2
  • 49
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 50
    • 0036323673 scopus 로고    scopus 로고
    • Large-scale isolation of Cajal bodies from HeLa cells
    • Lam YW, Lyon CE, Lamond AI. 2002. Large-scale isolation of Cajal bodies from HeLa cells. Mol Biol Cell 13:2461-2473.
    • (2002) Mol Biol Cell , vol.13 , pp. 2461-2473
    • Lam, Y.W.1    Lyon, C.E.2    Lamond, A.I.3
  • 51
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range transport
    • Langford GM. 2002. Myosin-V, a versatile motor for short-range transport. Traffic 3:859-865.
    • (2002) Traffic , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 52
    • 0026439115 scopus 로고
    • A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei
    • Leonhardt H, Page AW, Weier HU, Bestor TH. 1992. A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei. Cell 71:865-873.
    • (1992) Cell , vol.71 , pp. 865-873
    • Leonhardt, H.1    Page, A.W.2    Weier, H.U.3    Bestor, T.H.4
  • 54
    • 0019570066 scopus 로고
    • Monoclonal antibodies to nucleic acid-containing cellular constituents: Probes for molecular biology and autoimmune disease
    • Lerner EA, Lerner MR, Janeway CA, Steitz JA. 1981. Monoclonal antibodies to nucleic acid-containing cellular constituents: Probes for molecular biology and autoimmune disease. Proc Natl Acad Sci USA 78:2737-2741.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2737-2741
    • Lerner, E.A.1    Lerner, M.R.2    Janeway, C.A.3    Steitz, J.A.4
  • 56
    • 0028361594 scopus 로고
    • Long-distance neuronal migration in the adult mammalian brain
    • Lois C, Alvarez-Buylla A. 1994. Long-distance neuronal migration in the adult mammalian brain. Science 264:1145-1148.
    • (1994) Science , vol.264 , pp. 1145-1148
    • Lois, C.1    Alvarez-Buylla, A.2
  • 57
    • 32644451623 scopus 로고    scopus 로고
    • Nucleoplasmic b-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations
    • McDonald D, Carrero G, Andrin C, de Vries G, Hendzel, MJ. 2006. Nucleoplasmic b-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J Cell Biol 172:541-552.
    • (2006) J Cell Biol , vol.172 , pp. 541-552
    • McDonald, D.1    Carrero, G.2    Andrin, C.3    De Vries, G.4    Hendzel, M.J.5
  • 58
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • Mockrin SC, Korn ED. 1980. Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19:5359-5362.
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 59
    • 0032585352 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O. 1998. Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res 5:355-364.
    • (1998) DNA Res , vol.5 , pp. 355-364
    • Nagase, T.1    Ishikawa, K.2    Suyama, M.3    Kikuno, R.4    Hirosawa, M.5    Miyajima, N.6    Tanaka, A.7    Kotani, H.8    Nomura, N.9    Ohara, O.10
  • 60
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K, Horton P. 1999. PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24:34-36.
    • (1999) Trends Biochem Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 61
    • 0022504648 scopus 로고
    • Structural organization of replicon domains during DNA synthetic phase in the mammalian nucleus
    • Nakamura H, Morita T, Sato C. 1986. Structural organization of replicon domains during DNA synthetic phase in the mammalian nucleus. Exp Cell Res 165:291-297.
    • (1986) Exp Cell Res , vol.165 , pp. 291-297
    • Nakamura, H.1    Morita, T.2    Sato, C.3
  • 62
    • 0024526184 scopus 로고
    • Mapping replicational sites in the eucaryotic cell nucleus
    • Nakayasu H, Berezney R. 1989. Mapping replicational sites in the eucaryotic cell nucleus. J Cell Biol 108:1-11.
    • (1989) J Cell Biol , vol.108 , pp. 1-11
    • Nakayasu, H.1    Berezney, R.2
  • 64
    • 0036098469 scopus 로고    scopus 로고
    • Neuronal replacement in adult brain
    • Nottebohm F. 2002. Neuronal replacement in adult brain. Brain Res Bull 57:737-749.
    • (2002) Brain Res Bull , vol.57 , pp. 737-749
    • Nottebohm, F.1
  • 65
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • Olave IA, Reck-Peterson SL, Crabtree GR. 2002. Nuclear actin and actin-related proteins in chromatin remodeling. Annu Rev Biochem 71:755-781.
    • (2002) Annu Rev Biochem , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 66
    • 0032499768 scopus 로고    scopus 로고
    • Functional transitions in myosin: Formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan
    • Onishi H, Kojima S, Katoh K, Fujiwara K, Martinez HM, Morales MF. 1998. Functional transitions in myosin: Formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan. Proc Natl Acad Sci USA 95:6653-6658.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6653-6658
    • Onishi, H.1    Kojima, S.2    Katoh, K.3    Fujiwara, K.4    Martinez, H.M.5    Morales, M.F.6
  • 67
    • 0037180422 scopus 로고    scopus 로고
    • Early stages of energy transduction by myosin: Roles of Arg in switch I, of Glu in switch II, and of the salt-bridge between them
    • Onishi H, Ohki T, Mochizuki N, Morales MF. 2002. Early stages of energy transduction by myosin: Roles of Arg in switch I, of Glu in switch II, and of the salt-bridge between them. Proc Natl Acad Sci USA 99:15339-15344.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15339-15344
    • Onishi, H.1    Ohki, T.2    Mochizuki, N.3    Morales, M.F.4
  • 68
    • 0019200479 scopus 로고
    • Dimethylsulfoxide and the ionophore A23187 affect the arrangement of actin and induce nuclear actin paracrystals in PtK2 cells
    • Osborn M, Weber K. 1980. Dimethylsulfoxide and the ionophore A23187 affect the arrangement of actin and induce nuclear actin paracrystals in PtK2 cells. Exp Cell Res 129:103-114.
    • (1980) Exp Cell Res , vol.129 , pp. 103-114
    • Osborn, M.1    Weber, K.2
  • 70
    • 0035887589 scopus 로고    scopus 로고
    • Myr 8, a novel unconventional myosin expressed during brain development associates with the protein phosphatase catalytic subunits 1α and 1γ1
    • Patel KG, Liu C, Cameron PL, Cameron RS. 2001. Myr 8, a novel unconventional myosin expressed during brain development associates with the protein phosphatase catalytic subunits 1α and 1γ1. J Neurosci 21:7954-7968.
    • (2001) J Neurosci , vol.21 , pp. 7954-7968
    • Patel, K.G.1    Liu, C.2    Cameron, P.L.3    Cameron, R.S.4
  • 73
    • 27644506209 scopus 로고    scopus 로고
    • Nuclear actin extends, with no contraction in sight
    • Pederson T, Aebi U. 2005. Nuclear actin extends, with no contraction in sight. Mol Biol Cell 16:5055-5060.
    • (2005) Mol Biol Cell , vol.16 , pp. 5055-5060
    • Pederson, T.1    Aebi, U.2
  • 76
    • 0027400878 scopus 로고
    • Ultrastructural radioautographic analysis of neurogenesis in the hypothalamus in the adult frog, Rana temporaria, with special reference to physiological regeneration of the preoptic nucleus. II. Types of neuronal cells produced
    • Polenov AL, Chetverukhin VK. 1993. Ultrastructural radioautographic analysis of neurogenesis in the hypothalamus in the adult frog, Rana temporaria, with special reference to physiological regeneration of the preoptic nucleus. II. Types of neuronal cells produced. Cell Tissue Res 271:351-362.
    • (1993) Cell Tissue Res , vol.271 , pp. 351-362
    • Polenov, A.L.1    Chetverukhin, V.K.2
  • 79
    • 0036358203 scopus 로고    scopus 로고
    • Neurogenesis in adult primate neocortex: An evaluation of the evidence
    • Rakic P. 2002a. Neurogenesis in adult primate neocortex: An evaluation of the evidence. Nature Rev Neurosci 3:65-71.
    • (2002) Nature Rev Neurosci , vol.3 , pp. 65-71
    • Rakic, P.1
  • 80
    • 0036458427 scopus 로고    scopus 로고
    • Neurogenesis in adult primates
    • Rakic P. 2002b. Neurogenesis in adult primates. Prog Brain Res 138:3-14.
    • (2002) Prog Brain Res , vol.138 , pp. 3-14
    • Rakic, P.1
  • 81
    • 23044505521 scopus 로고    scopus 로고
    • Less is more: Progenitor death and cortical size
    • Rakic P. 2005. Less is more: Progenitor death and cortical size. Nat Neurosci 8:981-982.
    • (2005) Nat Neurosci , vol.8 , pp. 981-982
    • Rakic, P.1
  • 82
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber J, Ryder U, Lamond AI, Mann M. 2002. Large-scale proteomic analysis of the human spliceosome. Genome Res 12:1231-1245.
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 83
    • 0032915418 scopus 로고    scopus 로고
    • The tail of a yeast class V myosin, Myo2p, functions as a localization domain
    • Reck-Peterson SL, Novick PJ, Mooseker MS. 1999. The tail of a yeast class V myosin, Myo2p, functions as a localization domain. Mol Biol Cell 10:1001-1017.
    • (1999) Mol Biol Cell , vol.10 , pp. 1001-1017
    • Reck-Peterson, S.L.1    Novick, P.J.2    Mooseker, M.S.3
  • 84
    • 24144503755 scopus 로고    scopus 로고
    • Myosin domain evolution and the primary divergence of eukaryotes
    • Richards TA, Cavalier-Smith T. 2005. Myosin domain evolution and the primary divergence of eukaryotes. Nature 436:1113-1118.
    • (2005) Nature , vol.436 , pp. 1113-1118
    • Richards, T.A.1    Cavalier-Smith, T.2
  • 85
    • 0031596724 scopus 로고    scopus 로고
    • Nuclear localization of IκB α is mediated by the second ankyrin repeat: The IκB α ankyrin repeats define a novel class of cis-acting nuclear import sequences
    • Sachdev S, Hoffmann A, Hannink M. 1998. Nuclear localization of IκB α is mediated by the second ankyrin repeat: The IκB α ankyrin repeats define a novel class of cis-acting nuclear import sequences. Mol Cell Biol 18:2524-2534.
    • (1998) Mol Cell Biol , vol.18 , pp. 2524-2534
    • Sachdev, S.1    Hoffmann, A.2    Hannink, M.3
  • 88
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • Schott D, Ho J, Pruyne D, Bretscher A. 1999. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J Cell Biol 147:791-807.
    • (1999) J Cell Biol , vol.147 , pp. 791-807
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 90
    • 0020044056 scopus 로고
    • Actions of cytochalasin D on cytoskeletal networks
    • Schliwa M. 1982. Actions of cytochalasin D on cytoskeletal networks. J Cell Biol 92:79-91.
    • (1982) J Cell Biol , vol.92 , pp. 79-91
    • Schliwa, M.1
  • 91
    • 0036137684 scopus 로고    scopus 로고
    • Rab GTPases, intracellular traffic and disease
    • Seabra MC, Mules EH, Hume AN. 2002. Rab GTPases, intracellular traffic and disease. Trends Mol Med 8:23-30.
    • (2002) Trends Mol Med , vol.8 , pp. 23-30
    • Seabra, M.C.1    Mules, E.H.2    Hume, A.N.3
  • 92
    • 3142512358 scopus 로고    scopus 로고
    • 14-3-3 Suppresses the nuclear localization of threonine 157-phosphorylated p27 (Kip1)
    • Sekimoto T, Fukumoto M, Yoneda Y. 2004. 14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27 (Kip1). EMBO J 23:1934-1942.
    • (2004) EMBO J , vol.23 , pp. 1934-1942
    • Sekimoto, T.1    Fukumoto, M.2    Yoneda, Y.3
  • 93
    • 0030664537 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II
    • Shimada T, Sasaki N, Ohkura R, Sutoh K. 1997. Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II. Biochemistry 36:14037-14043.
    • (1997) Biochemistry , vol.36 , pp. 14037-14043
    • Shimada, T.1    Sasaki, N.2    Ohkura, R.3    Sutoh, K.4
  • 94
    • 0037809789 scopus 로고    scopus 로고
    • Unconventional myosins, actin dynamics and endocylosis: A ménage a trios?
    • Soldati T. 2003. Unconventional myosins, actin dynamics and endocylosis: A ménage a trios? Traffic 4:358-366.
    • (2003) Traffic , vol.4 , pp. 358-366
    • Soldati, T.1
  • 95
    • 4143131124 scopus 로고    scopus 로고
    • Dynamic targeting of the replication machinery to sites of DNA damage
    • Solomon DA, Cardoso MC, Knudsen ES. 2004. Dynamic targeting of the replication machinery to sites of DNA damage. J Cell Biol 166:455-463.
    • (2004) J Cell Biol , vol.166 , pp. 455-463
    • Solomon, D.A.1    Cardoso, M.C.2    Knudsen, E.S.3
  • 96
    • 31644448163 scopus 로고    scopus 로고
    • Myo10 in brain: Developmental regulation, identification of a headless isoform and dynamics in neurons
    • Sousa AD, Berg JS, Robertson BW, Meeker RB, Cheney RE. 2006. Myo10 in brain: Developmental regulation, identification of a headless isoform and dynamics in neurons. J Cell Sci 119:184-194.
    • (2006) J Cell Sci , vol.119 , pp. 184-194
    • Sousa, A.D.1    Berg, J.S.2    Robertson, B.W.3    Meeker, R.B.4    Cheney, R.E.5
  • 97
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector I, Braet F, Shochet NR, Bubb MR. 1999. New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc Res Tech 47:18-37.
    • (1999) Microsc Res Tech , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 98
    • 0015293356 scopus 로고
    • The synthesis of acidic chromosomal proteins during the cell cycle of HeLa S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication
    • Stein GS, Borun TW. 1972. The synthesis of acidic chromosomal proteins during the cell cycle of HeLa S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication. J Cell Biol 52:292-307.
    • (1972) J Cell Biol , vol.52 , pp. 292-307
    • Stein, G.S.1    Borun, T.W.2
  • 99
    • 18344371641 scopus 로고    scopus 로고
    • Moving messages: The intracellular localization of mRNAs
    • St Johnston D. 2005. Moving messages: The intracellular localization of mRNAs. Nat Rev Mol Cell Biol 6:363-375.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 363-375
    • St. Johnston, D.1
  • 100
    • 0035499887 scopus 로고    scopus 로고
    • The development of neural stem cells
    • Temple S. 2001. The development of neural stem cells. Nature 414:112-117.
    • (2001) Nature , vol.414 , pp. 112-117
    • Temple, S.1
  • 101
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin H, Staehlin T, Gordin J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordin, J.3
  • 102
    • 0035207924 scopus 로고    scopus 로고
    • Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells
    • Trinkle-Mulcahy L, Sleeman JE, Lamond AI. 2001. Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci 114:4219-4228.
    • (2001) J Cell Sci , vol.114 , pp. 4219-4228
    • Trinkle-Mulcahy, L.1    Sleeman, J.E.2    Lamond, A.I.3
  • 105
    • 0025299405 scopus 로고
    • Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies
    • Turner JR, Tartakoff AM, Greenspan NS. 1990. Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Proc Natl Acad Sci USA 87:5608-5618.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5608-5618
    • Turner, J.R.1    Tartakoff, A.M.2    Greenspan, N.S.3
  • 107
    • 2442560225 scopus 로고    scopus 로고
    • A role for myosin-1A in the localization of a brush border disaccharidase
    • Tyska MJ, Mooseker MS. 2004. A role for myosin-1A in the localization of a brush border disaccharidase. J Cell Biol 165:395-405.
    • (2004) J Cell Biol , vol.165 , pp. 395-405
    • Tyska, M.J.1    Mooseker, M.S.2
  • 109
    • 0032031972 scopus 로고    scopus 로고
    • PCNA binding through a conserved motif
    • Warbrick E. 1998. PCNA binding through a conserved motif. Bioessays 20:195-199.
    • (1998) Bioessays , vol.20 , pp. 195-199
    • Warbrick, E.1
  • 112
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou Z, Licklider LJ, Gygi SP, Reed R. 2002. Comprehensive proteomic analysis of the human spliceosome. Nature 419:182-185.
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 113
    • 0033137094 scopus 로고    scopus 로고
    • Neurogenesis, cell death and regeneration in the adult gymnotiform brain
    • Zupanc GKH. 1999. Neurogenesis, cell death and regeneration in the adult gymnotiform brain. J Exp Biol 202:1435-1446.
    • (1999) J Exp Biol , vol.202 , pp. 1435-1446
    • Zupanc, G.K.H.1
  • 114
    • 0035735721 scopus 로고    scopus 로고
    • Adult neurogenesis and neuronal regeneration in the central nervous system of teleost fish
    • Zupanc GKH. 2001. Adult neurogenesis and neuronal regeneration in the central nervous system of teleost fish. Brain Behav Evol 58:250-275.
    • (2001) Brain Behav Evol , vol.58 , pp. 250-275
    • Zupanc, G.K.H.1
  • 115
    • 21644445730 scopus 로고    scopus 로고
    • Proliferation, migration, neuronal differentiation, and long-term survival of new cells in the adult zebrafish brain
    • Zupanc GKH, Hinsch K, Gage FH. 2005, Proliferation, migration, neuronal differentiation, and long-term survival of new cells in the adult zebrafish brain. J Comp Neurol 488:290-319.
    • (2005) J Comp Neurol , vol.488 , pp. 290-319
    • Zupanc, G.K.H.1    Hinsch, K.2    Gage, F.H.3


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