메뉴 건너뛰기




Volumn 205, Issue 2, 1999, Pages 322-331

A role for Rho-like GTPases in the polarisation of mouse eight-cell blastomeres

Author keywords

Adhesion; Compaction; Cytoskeleton; GTPase; Micro filaments; Polarity; Preimplantation mouse conceptus; Rho

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE RIBOSE; CYTOCHALASIN D; GUANOSINE TRIPHOSPHATASE; RHO FACTOR; UVOMORULIN;

EID: 0033555897     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1006/dbio.1998.9117     Document Type: Article
Times cited : (87)

References (57)
  • 1
    • 0029680639 scopus 로고    scopus 로고
    • Two GTPases, cdc42 and rac, bind directly to a protein implicated in the immunodeficiency syndrome Wiscott-Aldrich syndrome
    • Aspenstrom, P., Lindberg, U., and Hall, A. (1996). Two GTPases, cdc42 and rac, bind directly to a protein implicated in the immunodeficiency syndrome Wiscott-Aldrich syndrome. Curr. Biol. 6, 70-75.
    • (1996) Curr. Biol. , vol.6 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 2
    • 0024406406 scopus 로고
    • The effects of phorbol esters on the mouse blastomeres: A role for protein kinase C in compaction?
    • Bloom, T. L. (1989). The effects of phorbol esters on the mouse blastomeres: A role for protein kinase C in compaction? Development 106, 159-171.
    • (1989) Development , vol.106 , pp. 159-171
    • Bloom, T.L.1
  • 3
    • 0025339971 scopus 로고
    • Changes in protein phosphorylation associated with compaction of the mouse preimplantation embryo
    • Bloom, T. L., and McConnell, J. M. (1990). Changes in protein phosphorylation associated with compaction of the mouse preimplantation embryo. Mol. Reprod. Dev. 26, 199-210.
    • (1990) Mol. Reprod. Dev. , vol.26 , pp. 199-210
    • Bloom, T.L.1    McConnell, J.M.2
  • 4
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga, V. M. M., Machesky, L. M., Hall, A., and Hotchkin, N. A. (1997). The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137, 1421-1431.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.M.1    Machesky, L.M.2    Hall, A.3    Hotchkin, N.A.4
  • 5
    • 0026232880 scopus 로고
    • Budding and cell polarity in Saccharomyces cerevisiae
    • Chant, J., and Pringle, J. R. (1991). Budding and cell polarity in Saccharomyces cerevisiae. Curr. Opin. Genet. Dev. 1, 342-350.
    • (1991) Curr. Opin. Genet. Dev. , vol.1 , pp. 342-350
    • Chant, J.1    Pringle, J.R.2
  • 6
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Closridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P., Boquet, P., Madaule, P., Popoff, M. R., Rubin, E. J., and Gill, D. M. (1989). The mammalian G protein rhoC is ADP-ribosylated by Closridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8, 1087-1092.
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 7
    • 0032004877 scopus 로고    scopus 로고
    • Tropomyosin in preimplantation mouse development: Identification, expression and organisation during cell division and polarisation
    • Clayton, L., and Johnson, M. H. (1998). Tropomyosin in preimplantation mouse development: Identification, expression and organisation during cell division and polarisation. Exp. Cell Res. 238, 450-464.
    • (1998) Exp. Cell Res. , vol.238 , pp. 450-464
    • Clayton, L.1    Johnson, M.H.2
  • 8
    • 0027691241 scopus 로고
    • Cell surface localisation and stability of uvomorulin during early mouse development
    • Clayton, L., Stinchcombe, S. V., and Johnson, M. H. (1993). Cell surface localisation and stability of uvomorulin during early mouse development. Zygote 1, 333-344.
    • (1993) Zygote , vol.1 , pp. 333-344
    • Clayton, L.1    Stinchcombe, S.V.2    Johnson, M.H.3
  • 9
    • 0025899137 scopus 로고
    • Development of cell polarity in budding yeast
    • Drubin, D. G. (1991). Development of cell polarity in budding yeast. Cell 65, 1093-1096.
    • (1991) Cell , vol.65 , pp. 1093-1096
    • Drubin, D.G.1
  • 10
    • 0030045345 scopus 로고    scopus 로고
    • Origins of polarity
    • Drubin, D. G., and Nelson, W. J. (1996). Origins of polarity. Cell 84, 335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 12
    • 0022930862 scopus 로고
    • The generation of cell surface polarity in mouse 8-cell blastomeres: The role of cortical microfilaments analysed using cytochalasin D
    • Fleming, T. P., Pickering, S. J., Qasim, F., and Maro, B. (1986). The generation of cell surface polarity in mouse 8-cell blastomeres: The role of cortical microfilaments analysed using cytochalasin D. J. Embryol. Exp. Morphol. 95, 169-191.
    • (1986) J. Embryol. Exp. Morphol. , vol.95 , pp. 169-191
    • Fleming, T.P.1    Pickering, S.J.2    Qasim, F.3    Maro, B.4
  • 13
    • 0021289449 scopus 로고
    • The nature of intercellular coupling within the preimplantation mouse embryo
    • Goodall, H., and Johnson, M. H. (1984). The nature of intercellular coupling within the preimplantation mouse embryo. J. Embryol. Exp. Morphol. 79, 53-76.
    • (1984) J. Embryol. Exp. Morphol. , vol.79 , pp. 53-76
    • Goodall, H.1    Johnson, M.H.2
  • 14
    • 0022580445 scopus 로고
    • Major loss of junctional coupling during mitosis in early mouse embryos
    • Goodall, H., and Maro, B. (1986). Major loss of junctional coupling during mitosis in early mouse embryos. J. Cell Biol. 102, 568-575.
    • (1986) J. Cell Biol. , vol.102 , pp. 568-575
    • Goodall, H.1    Maro, B.2
  • 15
    • 0023217750 scopus 로고
    • Redistribution of microtubules and pericentriolar material during the development of polarity in mouse blastomeres
    • Houliston, E., Pickering, S. J., and Maro, B. (1987). Redistribution of microtubules and pericentriolar material during the development of polarity in mouse blastomeres. J. Cell Biol. 104, 1299-1308.
    • (1987) J. Cell Biol. , vol.104 , pp. 1299-1308
    • Houliston, E.1    Pickering, S.J.2    Maro, B.3
  • 16
    • 0024314723 scopus 로고
    • Alternative routes for the establishment of surface polarity during compaction in the mouse embryo
    • Houliston, E., Pickering, S. J., and Maro, B. (1989). Alternative routes for the establishment of surface polarity during compaction in the mouse embryo. Dev. Biol. 134, 342-350.
    • (1989) Dev. Biol. , vol.134 , pp. 342-350
    • Houliston, E.1    Pickering, S.J.2    Maro, B.3
  • 17
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42, a Saccaromyces cerevisiae gene involved in the development of cell polarity
    • Johnson, D. I., and Pringle, J. R. (1990). Molecular characterization of CDC42, a Saccaromyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111, 143-152.
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.I.1    Pringle, J.R.2
  • 18
    • 0029827205 scopus 로고    scopus 로고
    • The origins of pluriblast and trophoblast in the eutherian conceptus
    • Johnson, M. H. (1996). The origins of pluriblast and trophoblast in the eutherian conceptus. Reprod. Fertil. Dev. 8, 699-709.
    • (1996) Reprod. Fertil. Dev. , vol.8 , pp. 699-709
    • Johnson, M.H.1
  • 19
    • 0021285228 scopus 로고
    • The distribution of cytoplasmic actin in mouse 8-cell blastomeres
    • Johnson, M. H., and Maro, B. (1984). The distribution of cytoplasmic actin in mouse 8-cell blastomeres. J. Embryol. Exp. Morphol. 82, 97-117.
    • (1984) J. Embryol. Exp. Morphol. , vol.82 , pp. 97-117
    • Johnson, M.H.1    Maro, B.2
  • 20
    • 0022273286 scopus 로고
    • A dissection of the mechanisms generating and stabilising polarity in mouse 8- and 16-cell blastomeres: The role of cytoskeletal elements
    • Johnson, M. H., and Maro, B. (1985). A dissection of the mechanisms generating and stabilising polarity in mouse 8- and 16-cell blastomeres: The role of cytoskeletal elements. J. Embryol. Exp. Morphol. 90, 311-334.
    • (1985) J. Embryol. Exp. Morphol. , vol.90 , pp. 311-334
    • Johnson, M.H.1    Maro, B.2
  • 21
    • 0002468665 scopus 로고
    • Time and space in the early mouse embryo: A cell biological approach to cell diversification
    • Cambridge Univ. Press, Cambridge, UK
    • Johnson, M. H., and Maro, B. (1986). Time and space in the early mouse embryo: A cell biological approach to cell diversification. In "Experimental Approaches to Mammalian Embryonic Development," pp. 35-65. Cambridge Univ. Press, Cambridge, UK.
    • (1986) Experimental Approaches to Mammalian Embryonic Development , pp. 35-65
    • Johnson, M.H.1    Maro, B.2
  • 22
    • 0022556510 scopus 로고
    • The role of cell adhesion in the synchronisation and orientation of polarisation in 8-cell mouse blastomeres
    • Johnson, M. H., Maro, B., and Takeichi, M. (1986). The role of cell adhesion in the synchronisation and orientation of polarisation in 8-cell mouse blastomeres. J. Embryol. Exp. Morphol. 93, 239-255.
    • (1986) J. Embryol. Exp. Morphol. , vol.93 , pp. 239-255
    • Johnson, M.H.1    Maro, B.2    Takeichi, M.3
  • 23
    • 0029822521 scopus 로고    scopus 로고
    • The nomenclature of early development in mammals
    • Johnson, M. H., and Selwood, L. (1996). The nomenclature of early development in mammals. Reprod. Fertil. Dev. 8, 759-764.
    • (1996) Reprod. Fertil. Dev. , vol.8 , pp. 759-764
    • Johnson, M.H.1    Selwood, L.2
  • 24
    • 0019801567 scopus 로고
    • Induction of polarity in mouse 8-cell blastomeres: Specificity, geometry and stability
    • Johnson, M. H., and Ziomek, C. A. (1981). Induction of polarity in mouse 8-cell blastomeres: Specificity, geometry and stability. J. Cell Biol. 91, 303-308.
    • (1981) J. Cell Biol. , vol.91 , pp. 303-308
    • Johnson, M.H.1    Ziomek, C.A.2
  • 26
    • 0027496730 scopus 로고
    • ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein-tyrosine phosphorylation and phosphati-dylinositol 3-kinase activation in cultured swiss 3T3 cells
    • Kumagi, N., Morii, N., Fujisawa, K., Nemoto, Y., and Narumiya, S. (1993). ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein-tyrosine phosphorylation and phosphati-dylinositol 3-kinase activation in cultured swiss 3T3 cells. J. Biol. Chem. 268, 24535-24538.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24535-24538
    • Kumagi, N.1    Morii, N.2    Fujisawa, K.3    Nemoto, Y.4    Narumiya, S.5
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (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
  • 28
    • 0022930861 scopus 로고
    • The timing of compaction: Control of a major developmental transition in mouse early embryogenesis
    • Levy, J., Johnson, M. H., Goodall, H., and Maro, B. (1986). The timing of compaction: Control of a major developmental transition in mouse early embryogenesis. J. Em bryol. Exp. Morphol. 95, 213-237.
    • (1986) J. Em Bryol. Exp. Morphol. , vol.95 , pp. 213-237
    • Levy, J.1    Johnson, M.H.2    Goodall, H.3    Maro, B.4
  • 29
    • 0027235324 scopus 로고
    • A non-receptor tyrosine kinase that inhibits the GTPase activity of p21 (CDC42)
    • Manser, E., Leung, T., Salihuddin, H., Tan, L., and Lim, L. (1993). A non-receptor tyrosine kinase that inhibits the GTPase activity of p21 (CDC42). Nature 363, 364-367.
    • (1993) Nature , vol.363 , pp. 364-367
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Tan, L.4    Lim, L.5
  • 30
    • 0028078824 scopus 로고
    • A brain serine-threonine protein kinase activated by CDC42 and rac1
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z. S., and Lim, L. (1994). A brain serine-threonine protein kinase activated by CDC42 and rac1. Nature 367, 40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 31
    • 0021285488 scopus 로고
    • Changes in actin distribution during fertilization of the mouse egg
    • Maro, B., Johnson, M. H., Pickering, S. J., and Flach, G. (1984). Changes in actin distribution during fertilization of the mouse egg. J. Embryol. Exp. Morphol. 81, 211-237.
    • (1984) J. Embryol. Exp. Morphol. , vol.81 , pp. 211-237
    • Maro, B.1    Johnson, M.H.2    Pickering, S.J.3    Flach, G.4
  • 32
    • 0021647885 scopus 로고
    • Microtubules influence compaction in preimplantation mouse embryos
    • Maro, B., and Pickering, S. (1984). Microtubules influence compaction in preimplantation mouse embryos. J. Embryol. Exp. Morphol. 84, 217-232.
    • (1984) J. Embryol. Exp. Morphol. , vol.84 , pp. 217-232
    • Maro, B.1    Pickering, S.2
  • 33
    • 0025877228 scopus 로고
    • Purification of a 92 kDa cytoplasmic protein tightly associated with the cell-cell adhesion molecule E-cadherin
    • McCrea, P. D., Turck, C. W., and Gumbiner, B. (1991). Purification of a 92 kDa cytoplasmic protein tightly associated with the cell-cell adhesion molecule E-cadherin. J. Biol. Chem. 266, 4514-4520.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4514-4520
    • McCrea, P.D.1    Turck, C.W.2    Gumbiner, B.3
  • 34
    • 0026700090 scopus 로고
    • A rho gene product in human blood platelets II effects of the ADP-ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation
    • Morii, N., Teru-uchi, T., Tominaga, T., Kumagi, N., Kozaki, S., Ushikubi, F., and Narumiya, S. (1992). A rho gene product in human blood platelets II effects of the ADP-ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation. J. Biol. Chem. 267, 20921-20926.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20921-20926
    • Morii, N.1    Teru-uchi, T.2    Tominaga, T.3    Kumagi, N.4    Kozaki, S.5    Ushikubi, F.6    Narumiya, S.7
  • 35
    • 0024755646 scopus 로고
    • Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin
    • Nagafuchi, A., and Takeichi, M. (1989). Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin. Cell Regul. 1, 37-44.
    • (1989) Cell Regul. , vol.1 , pp. 37-44
    • Nagafuchi, A.1    Takeichi, M.2
  • 36
    • 0025604563 scopus 로고
    • The effect of iron and iron chelators on the in vitro block to development of the mouse preimplantation embryo: BAT6 a new medium for improved culture of mouse embryos in vitro
    • Nasr-Esfahani, M., Johnson, M. H., and Aitken, R. J. (1991). The effect of iron and iron chelators on the in vitro block to development of the mouse preimplantation embryo: BAT6 a new medium for improved culture of mouse embryos in vitro. Hum. Reprod. 5, 997-1003.
    • (1991) Hum. Reprod. , vol.5 , pp. 997-1003
    • Nasr-Esfahani, M.1    Johnson, M.H.2    Aitken, R.J.3
  • 37
    • 0016538915 scopus 로고
    • Ultrastructural localization of lectin-binding sites on the zonae pellucidae and plasma membranes of mammalian eggs
    • Nicolson, G. L., Yanagimachi, R., and Yanagimachi, H. (1975). Ultrastructural localization of lectin-binding sites on the zonae pellucidae and plasma membranes of mammalian eggs. J. Cell Biol. 66, 263-274.
    • (1975) J. Cell Biol. , vol.66 , pp. 263-274
    • Nicolson, G.L.1    Yanagimachi, R.2    Yanagimachi, H.3
  • 38
    • 0028961293 scopus 로고
    • Rho, rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with the actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and Hall, A. (1995). Rho, rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with the actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 39
    • 0027596407 scopus 로고
    • Staurosporine advances interblastomeric flattening of the mouse embryo
    • O'Sullivan, D. M., Johnson, M. H., and McConnell, J. M. (1993). Staurosporine advances interblastomeric flattening of the mouse embryo. Zygote 1, 103-112.
    • (1993) Zygote , vol.1 , pp. 103-112
    • O'Sullivan, D.M.1    Johnson, M.H.2    McConnell, J.M.3
  • 40
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa, M., Baribault, H., and Kemler, R. (1989). The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO J. 8, 1711-1717.
    • (1989) EMBO J. , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 41
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21rho induces rapid changes in cell morphology
    • Paterson, H. F., Self, A. J., Garrett, M. D., Just, I., Aktories, K., and Hall, A. (1990). Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007.
    • (1990) J. Cell Biol. , vol.111 , pp. 1001-1007
    • Paterson, H.F.1    Self, A.J.2    Garrett, M.D.3    Just, I.4    Aktories, K.5    Hall, A.6
  • 42
    • 0027944638 scopus 로고
    • Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125 (FAK) and paxillin induced by bombesin and endothelin
    • Rankin, S., Morii, N., Narumiya, S., and Rozengurt, E. (1994). Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125 (FAK) and paxillin induced by bombesin and endothelin. FEBS Lett. 354, 315-319.
    • (1994) FEBS Lett. , vol.354 , pp. 315-319
    • Rankin, S.1    Morii, N.2    Narumiya, S.3    Rozengurt, E.4
  • 43
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibres in response to growth factors
    • Ridley, A. J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibres in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 44
    • 0023779031 scopus 로고
    • Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin, E. J., Gill, D. M., Boquet, P., and Popoff, M. R. (1988). Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell. Biol. 8, 418-426.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 45
    • 0026735251 scopus 로고
    • Synthesis and phosphorylation of uvomorulin during mouse early development
    • Sefton, M., Johnson, M. H., and Clayton, L. (1992). Synthesis and phosphorylation of uvomorulin during mouse early development. Development 115, 313-318.
    • (1992) Development , vol.115 , pp. 313-318
    • Sefton, M.1    Johnson, M.H.2    Clayton, L.3
  • 46
    • 0029877981 scopus 로고    scopus 로고
    • Experimental manipulations of compaction and their effects on the phosphorylation of uvomorulin
    • Sefton, M., Johnson, M. H., Clayton, L., and McConnell, J. M. L. (1996). Experimental manipulations of compaction and their effects on the phosphorylation of uvomorulin. Mol. Reprod. Dev. 44, 77-87.
    • (1996) Mol. Reprod. Dev. , vol.44 , pp. 77-87
    • Sefton, M.1    Johnson, M.H.2    Clayton, L.3    McConnell, J.M.L.4
  • 47
    • 0022891682 scopus 로고
    • N-linked oligosaccharides are not involved in the function of a cell-cell binding glycoprotein
    • Shirayoshi, Y., Nose, A., Iwasaki, K., and Takeichi, M. (1986). N-linked oligosaccharides are not involved in the function of a cell-cell binding glycoprotein. Cell Struct. Funct. 11, 245-252.
    • (1986) Cell Struct. Funct. , vol.11 , pp. 245-252
    • Shirayoshi, Y.1    Nose, A.2    Iwasaki, K.3    Takeichi, M.4
  • 48
    • 0021015747 scopus 로고
    • The calcium dependent cell-cell adhesion system regulated inner cell mass formation and cell surface polarisation in early mouse development
    • Shirayoshi, Y., Okada, T. S., and Takeichi, M. (1983). The calcium dependent cell-cell adhesion system regulated inner cell mass formation and cell surface polarisation in early mouse development. Cell 35, 631-638.
    • (1983) Cell , vol.35 , pp. 631-638
    • Shirayoshi, Y.1    Okada, T.S.2    Takeichi, M.3
  • 49
    • 0029008280 scopus 로고
    • Regulation of the polarisation of T cells toward antigen-presenting cells by ras-related GTPase CDC42
    • Stowers, L., Yelon, D., Berg, L. J., and Chant, J. (1995). Regulation of the polarisation of T cells toward antigen-presenting cells by ras-related GTPase CDC42. Proc. Natl. Acad. Sci. USA 92, 5027-5031.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5027-5031
    • Stowers, L.1    Yelon, D.2    Berg, L.J.3    Chant, J.4
  • 50
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerisation
    • Symons, M., Derry, J. M. J., Karlak, B., Jiang, S., Lemahieu, V., McCormick, F., Francke, U., and Abo, A. (1996). Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerisation. Cell 84, 723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.J.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 51
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi, K., Sasaki, T., Kotani, H., Nishioka, H., and Takai, Y. (1997). Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J. Cell Biol. 139, 1047-1059.
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 52
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi, M. (1991). Cadherin cell adhesion receptors as a morphogenetic regulator. Science 251, 1451-1455.
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 53
    • 0030904698 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion by the small GTP-binding protein Rho in small cell lung carcinoma cells
    • Tokman, M. G., Porter, R. A., and Williams, C. L. (1997). Regulation of cadherin-mediated adhesion by the small GTP-binding protein Rho in small cell lung carcinoma cells. Cancer Res. 57, 1785-1793.
    • (1997) Cancer Res. , vol.57 , pp. 1785-1793
    • Tokman, M.G.1    Porter, R.A.2    Williams, C.L.3
  • 54
    • 0027471215 scopus 로고
    • Inhibition of PMA-induced, LFA-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho
    • Tominaga, T., Sugie, K., Hirata, M., Morii, N., Fukata, J., Uchida, A., Imura, H., and Narumiya, S. (1993). Inhibition of PMA-induced, LFA-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J. Cell Biol. 120, 1529-1537.
    • (1993) J. Cell Biol. , vol.120 , pp. 1529-1537
    • Tominaga, T.1    Sugie, K.2    Hirata, M.3    Morii, N.4    Fukata, J.5    Uchida, A.6    Imura, H.7    Narumiya, S.8
  • 55
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schory, C. (1997). Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schory, C.2
  • 56
    • 0025261141 scopus 로고
    • Activation of protein kinase C triggers premature compaction in the four-cell stage mouse embryo
    • Winkel, G. K., Ferguson, J. E., Takeichi, M., and Nuccitelli, R. (1990). Activation of protein kinase C triggers premature compaction in the four-cell stage mouse embryo. Dev. Biol. 138, 1-15.
    • (1990) Dev. Biol. , vol.138 , pp. 1-15
    • Winkel, G.K.1    Ferguson, J.E.2    Takeichi, M.3    Nuccitelli, R.4
  • 57
    • 0018963282 scopus 로고
    • Cell surface interactions induces polarisation of early mouse 8-cell blastomeres at compaction
    • Ziomek, C., and Johnson, M. H. (1980). Cell surface interactions induces polarisation of early mouse 8-cell blastomeres at compaction. Cell 21, 935-942.
    • (1980) Cell , vol.21 , pp. 935-942
    • Ziomek, C.1    Johnson, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.