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Volumn 255, Issue 2, 2003, Pages 383-398

XGef is a CPEB-interacting protein involved in Xenopus oocyte maturation

Author keywords

G protein; GEF; Guanine nucleotide exchange factor; Polyadenylation; Translation

Indexed keywords

ANTIBODY; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; PROGESTERONE; PROTEIN C MOS; PROTEIN CDC42; PROTEIN MOS; PROTEIN XGEF; RECOMBINANT PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0037443877     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0012-1606(02)00089-1     Document Type: Article
Times cited : (17)

References (56)
  • 2
    • 0343917044 scopus 로고    scopus 로고
    • The kinase Eg2 is a component of the Xenopus oocyte progesterone-activated signaling pathway
    • Andresson T., Ruderman J.V. The kinase Eg2 is a component of the Xenopus oocyte progesterone-activated signaling pathway. EMBO J. 17:1998;5627-5637.
    • (1998) EMBO J. , vol.17 , pp. 5627-5637
    • Andresson, T.1    Ruderman, J.V.2
  • 3
    • 0030962832 scopus 로고    scopus 로고
    • A dependent pathway of cytoplasmic polyadenylation reactions linked to cell cycle control by c-mos and CDK1 activation
    • Ballantyne S., Daniel D.L. Jr., Wickens M. A dependent pathway of cytoplasmic polyadenylation reactions linked to cell cycle control by c-mos and CDK1 activation. Mol. Biol. Cell. 8:1997;1633-1648.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1633-1648
    • Ballantyne, S.1    Daniel D.L., Jr.2    Wickens, M.3
  • 4
    • 0032101696 scopus 로고    scopus 로고
    • Meiotic maturation in Xenopus requires polyadenylation of multiple mRNAs
    • Barkoff A., Ballantyne S., Wickens M. Meiotic maturation in Xenopus requires polyadenylation of multiple mRNAs. EMBO J. 17:1998;3168-3175.
    • (1998) EMBO J. , vol.17 , pp. 3168-3175
    • Barkoff, A.1    Ballantyne, S.2    Wickens, M.3
  • 5
    • 0033731791 scopus 로고    scopus 로고
    • The classical progesterone receptor mediates Xenopus oocyte maturation through a nongenomic mechanism
    • Bayaa M., Booth R.A., Sheng Y., Liu X.J. The classical progesterone receptor mediates Xenopus oocyte maturation through a nongenomic mechanism. Proc. Natl. Acad. Sci. USA. 97:2000;12607-12612.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12607-12612
    • Bayaa, M.1    Booth, R.A.2    Sheng, Y.3    Liu, X.J.4
  • 6
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop A.L., Hall A. Rho GTPases and their effector proteins. Biochem. J. 348:2000;241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 7
    • 0037099704 scopus 로고    scopus 로고
    • Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation
    • Cao Q., Richter J.D. Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J. 21:2002;3852-3862.
    • (2002) EMBO J. , vol.21 , pp. 3852-3862
    • Cao, Q.1    Richter, J.D.2
  • 8
    • 0034723369 scopus 로고    scopus 로고
    • Regulation of Xenopus p21-activated kinase (X-PAK2) by Cdc42 and maturation-promoting factor controls Xenopus oocyte maturation
    • Cau J., Faure S., Vigneron S., Labbe J.C., Delsert C., Morin N. Regulation of Xenopus p21-activated kinase (X-PAK2) by Cdc42 and maturation-promoting factor controls Xenopus oocyte maturation. J. Biol. Chem. 275:2000;2367-2375.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2367-2375
    • Cau, J.1    Faure, S.2    Vigneron, S.3    Labbe, J.C.4    Delsert, C.5    Morin, N.6
  • 9
    • 0034669086 scopus 로고    scopus 로고
    • The temporal control of wee1 mRNA translation during Xenopus oocyte maturation is regulated by cytoplasmic polyadenylation elements within the 3′-untranslated region
    • Charlesworth A., Welk J., MacNicol A.M. The temporal control of wee1 mRNA translation during Xenopus oocyte maturation is regulated by cytoplasmic polyadenylation elements within the 3′-untranslated region. Dev. Biol. 227:2000;706-719.
    • (2000) Dev. Biol. , vol.227 , pp. 706-719
    • Charlesworth, A.1    Welk, J.2    MacNicol, A.M.3
  • 11
    • 0030869091 scopus 로고    scopus 로고
    • The Mos pathway regulates cytoplasmic polyadenylation in Xenopus oocytes
    • de Moor C.H., Richter J.D. The Mos pathway regulates cytoplasmic polyadenylation in Xenopus oocytes. Mol. Cell. Biol. 17:1997;6419-6426.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6419-6426
    • De Moor, C.H.1    Richter, J.D.2
  • 12
    • 0036683056 scopus 로고    scopus 로고
    • Mos is not required for the initiation of meiotic maturation in Xenopus oocytes
    • Dupre A., Jessus C., Ozon R., Haccard O. Mos is not required for the initiation of meiotic maturation in Xenopus oocytes. EMBO J. 21:2002;4026-4036.
    • (2002) EMBO J. , vol.21 , pp. 4026-4036
    • Dupre, A.1    Jessus, C.2    Ozon, R.3    Haccard, O.4
  • 13
    • 0033567143 scopus 로고    scopus 로고
    • A novel p34(cdc2)-binding and activating protein that is necessary and sufficient to trigger G(2)/M progression in Xenopus oocytes
    • Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R. A novel p34(cdc2)-binding and activating protein that is necessary and sufficient to trigger G(2)/M progression in Xenopus oocytes. Genes Dev. 13:1999;2177-2189.
    • (1999) Genes Dev. , vol.13 , pp. 2177-2189
    • Ferby, I.1    Blazquez, M.2    Palmer, A.3    Eritja, R.4    Nebreda, A.R.5
  • 14
    • 0032718122 scopus 로고    scopus 로고
    • Dissociation of MAP kinase activation and MPF activation in hormone-stimulated maturation of Xenopus oocytes
    • Fisher D.L., Brassac T., Galas S., Doree M. Dissociation of MAP kinase activation and MPF activation in hormone-stimulated maturation of Xenopus oocytes. Development. 126:1999;4537-4546.
    • (1999) Development , vol.126 , pp. 4537-4546
    • Fisher, D.L.1    Brassac, T.2    Galas, S.3    Doree, M.4
  • 15
    • 0033558963 scopus 로고    scopus 로고
    • Confocal microscopy and 3-D reconstruction of the cytoskeleton of Xenopus oocytes
    • Gard D.L. Confocal microscopy and 3-D reconstruction of the cytoskeleton of Xenopus oocytes. Microsc. Res. Tech. 44:1999;388-414.
    • (1999) Microsc. Res. Tech. , vol.44 , pp. 388-414
    • Gard, D.L.1
  • 16
    • 0034176617 scopus 로고    scopus 로고
    • The critical role of the MAP kinase pathway in meiosis II in Xenopus oocytes is mediated by p90(Rsk)
    • Gross S.D., Schwab M.S., Taieb F.E., Lewellyn A.L., Qian Y.W., Maller J.L. The critical role of the MAP kinase pathway in meiosis II in Xenopus oocytes is mediated by p90(Rsk). Curr. Biol. 10:2000;430-438.
    • (2000) Curr. Biol. , vol.10 , pp. 430-438
    • Gross, S.D.1    Schwab, M.S.2    Taieb, F.E.3    Lewellyn, A.L.4    Qian, Y.W.5    Maller, J.L.6
  • 17
    • 0035118704 scopus 로고    scopus 로고
    • Temporal and spatial regulation of Rho-type guanine-nucleotide exchange factors: The yeast perspective
    • Gulli M.P., Peter M. Temporal and spatial regulation of Rho-type guanine-nucleotide exchange factors the yeast perspective . Genes Dev. 15:2001;365-379.
    • (2001) Genes Dev. , vol.15 , pp. 365-379
    • Gulli, M.P.1    Peter, M.2
  • 18
    • 0024998680 scopus 로고
    • Changes in mRNA length accompany translational regulation of the somatic and testis-specific cytochrome c genes during spermatogenesis in the mouse
    • Hake L.E., Alcivar A.A., Hecht N.B. Changes in mRNA length accompany translational regulation of the somatic and testis-specific cytochrome c genes during spermatogenesis in the mouse. Development. 110:1990;249-257.
    • (1990) Development , vol.110 , pp. 249-257
    • Hake, L.E.1    Alcivar, A.A.2    Hecht, N.B.3
  • 19
    • 0031883566 scopus 로고    scopus 로고
    • Specificity of RNA Binding by CPEB: Requirement for RNA recognition motifs and a novel zinc finger
    • Hake L.E., Mendez R., Richter J.D. Specificity of RNA Binding by CPEB Requirement for RNA recognition motifs and a novel zinc finger . Mol. Cell. Biol. 18:1998;685-693.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 685-693
    • Hake, L.E.1    Mendez, R.2    Richter, J.D.3
  • 20
    • 0028029983 scopus 로고
    • CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation
    • Hake L.E., Richter J.D. CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell. 79:1994;617-627.
    • (1994) Cell , vol.79 , pp. 617-627
    • Hake, L.E.1    Richter, J.D.2
  • 22
    • 0037063166 scopus 로고    scopus 로고
    • P38 MAPK-mediated activation of NF-kappaB by the RhoGEF domain of Bcr
    • Korus M., Mahon G.M., Cheng L., Whitehead I.P. p38 MAPK-mediated activation of NF-kappaB by the RhoGEF domain of Bcr. Oncogene. 21:2002;4601-4612.
    • (2002) Oncogene , vol.21 , pp. 4601-4612
    • Korus, M.1    Mahon, G.M.2    Cheng, L.3    Whitehead, I.P.4
  • 23
    • 0021770860 scopus 로고
    • Functional messenger RNAs are produced by SP6 in vitro transcription of cloned cDNAs
    • Krieg P.A., Melton D.A. Functional messenger RNAs are produced by SP6 in vitro transcription of cloned cDNAs. Nucleic Acids Res. 12:1984;7057-7070.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7057-7070
    • Krieg, P.A.1    Melton, D.A.2
  • 24
    • 0030791405 scopus 로고    scopus 로고
    • Xp54, the Xenopus homologue of human RNA helicase p54, is an integral component of stored mRNP particles in oocytes
    • Ladomery M., Wade E., Sommerville J. Xp54, the Xenopus homologue of human RNA helicase p54, is an integral component of stored mRNP particles in oocytes. Nucleic Acids Res. 25:1997;965-973.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 965-973
    • Ladomery, M.1    Wade, E.2    Sommerville, J.3
  • 25
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., Van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science. 252:1991;1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 26
    • 0035793036 scopus 로고    scopus 로고
    • The elusive progesterone receptor in Xenopus oocytes
    • Maller J.L. The elusive progesterone receptor in Xenopus oocytes. Proc. Natl. Acad. Sci. USA. 98:2001;8-10.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8-10
    • Maller, J.L.1
  • 27
    • 0031724595 scopus 로고    scopus 로고
    • Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation
    • Mangus D.A., Amrani N., Jacobson A. Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mol. Cell. Biol. 18:1998;7383-7396.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7383-7396
    • Mangus, D.A.1    Amrani, N.2    Jacobson, A.3
  • 28
    • 0037007233 scopus 로고    scopus 로고
    • Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction
    • Mendez R., Barnard D., Richter J.D. Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction. EMBO J. 21:2002;1833-1844.
    • (2002) EMBO J. , vol.21 , pp. 1833-1844
    • Mendez, R.1    Barnard, D.2    Richter, J.D.3
  • 30
    • 0033634850 scopus 로고    scopus 로고
    • Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex
    • Mendez R., Murthy K.G., Ryan K., Manley J.L., Richter J.D. Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex. Mol. Cell. 6:2000;1253-1259.
    • (2000) Mol. Cell , vol.6 , pp. 1253-1259
    • Mendez, R.1    Murthy, K.G.2    Ryan, K.3    Manley, J.L.4    Richter, J.D.5
  • 31
    • 0035404265 scopus 로고    scopus 로고
    • Translational control by CPEB: A means to the end
    • Mendez R., Richter J.D. Translational control by CPEB a means to the end . Nat. Rev. Mol. Cell Biol. 2:2001;521-529.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 521-529
    • Mendez, R.1    Richter, J.D.2
  • 32
    • 0028889749 scopus 로고
    • Newly synthesized protein(s) must associate with p34cdc2 to activate MAP kinase and MPF during progesterone-induced maturation of Xenopus oocytes
    • Nebreda A.R., Gannon J.V., Hunt T. Newly synthesized protein(s) must associate with p34cdc2 to activate MAP kinase and MPF during progesterone-induced maturation of Xenopus oocytes. EMBO J. 14:1995;5597-5607.
    • (1995) EMBO J. , vol.14 , pp. 5597-5607
    • Nebreda, A.R.1    Gannon, J.V.2    Hunt, T.3
  • 34
    • 0032866302 scopus 로고    scopus 로고
    • RHO-associated protein kinase alpha potentiates insulin-induced MAP kinase activation in Xenopus oocytes
    • Ohan N., Agazie Y., Cummings C., Booth R., Bayaa M., Liu X.J. RHO-associated protein kinase alpha potentiates insulin-induced MAP kinase activation in Xenopus oocytes. J. Cell Sci. 112:1999;2177-2184.
    • (1999) J. Cell Sci. , vol.112 , pp. 2177-2184
    • Ohan, N.1    Agazie, Y.2    Cummings, C.3    Booth, R.4    Bayaa, M.5    Liu, X.J.6
  • 36
    • 0033628521 scopus 로고    scopus 로고
    • The activation of MAP kinase and p34cdc2/cyclin B during the meiotic maturation of Xenopus oocytes
    • Palmer A., Nebreda A.R. The activation of MAP kinase and p34cdc2/cyclin B during the meiotic maturation of Xenopus oocytes. Prog. Cell Cycle Res. 4:2000;131-143.
    • (2000) Prog. Cell Cycle Res. , vol.4 , pp. 131-143
    • Palmer, A.1    Nebreda, A.R.2
  • 37
    • 0035869581 scopus 로고    scopus 로고
    • CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome
    • Reverte C.G., Ahearn M.D., Hake L.E. CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome. Dev. Biol. 231:2001;447-458.
    • (2001) Dev. Biol. , vol.231 , pp. 447-458
    • Reverte, C.G.1    Ahearn, M.D.2    Hake, L.E.3
  • 38
    • 0032535359 scopus 로고    scopus 로고
    • Inhibition of small G proteins by clostridium sordellii lethal toxin activates cdc2 and MAP kinase in Xenopus oocytes
    • Rime H., Talbi N., Popoff M.R., Suziedelis K., Jessus C., Ozon R. Inhibition of small G proteins by clostridium sordellii lethal toxin activates cdc2 and MAP kinase in Xenopus oocytes. Dev. Biol. 204:1998;592-602.
    • (1998) Dev. Biol. , vol.204 , pp. 592-602
    • Rime, H.1    Talbi, N.2    Popoff, M.R.3    Suziedelis, K.4    Jessus, C.5    Ozon, R.6
  • 39
    • 0031015299 scopus 로고    scopus 로고
    • What does Mos do in oocytes and somatic cells?
    • Sagata N. What does Mos do in oocytes and somatic cells? Bioessays. 19:1997;13-21.
    • (1997) Bioessays , vol.19 , pp. 13-21
    • Sagata, N.1
  • 40
    • 0024280269 scopus 로고
    • Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes
    • Sagata N., Oskarsson M., Copeland T., Brumbaugh J., Vande Woude G.F. Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature. 335:1988;519-525.
    • (1988) Nature , vol.335 , pp. 519-525
    • Sagata, N.1    Oskarsson, M.2    Copeland, T.3    Brumbaugh, J.4    Vande Woude, G.F.5
  • 41
    • 0027076554 scopus 로고
    • Protein prenylation: Genes, enzymes, targets, and functions
    • Schafer W.R., Rine J. Protein prenylation genes, enzymes, targets, and functions . Annu. Rev. Genet. 26:1992;209-237.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 209-237
    • Schafer, W.R.1    Rine, J.2
  • 42
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A., Hall A. Guanine nucleotide exchange factors for Rho GTPases turning on the switch . Genes Dev. 16:2002;1587-1609.
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 43
    • 0031970317 scopus 로고    scopus 로고
    • Membrane association and targeting of prenylated Ras-like GTPases
    • Seabra M.C. Membrane association and targeting of prenylated Ras-like GTPases. Cell. Signalling. 10:1998;167-172.
    • (1998) Cell. Signalling , vol.10 , pp. 167-172
    • Seabra, M.C.1
  • 44
    • 0028226530 scopus 로고
    • The 3′-untranslated regions of c-mos and cyclin mRNAs stimulate translation by regulating cytoplasmic polyadenylation
    • Sheets M.D., Fox C.A., Hunt T., Vande Woude G., Wickens M. The 3′-untranslated regions of c-mos and cyclin mRNAs stimulate translation by regulating cytoplasmic polyadenylation. Genes Dev. 8:1994;926-938.
    • (1994) Genes Dev. , vol.8 , pp. 926-938
    • Sheets, M.D.1    Fox, C.A.2    Hunt, T.3    Vande Woude, G.4    Wickens, M.5
  • 45
    • 0028950858 scopus 로고
    • Polyadenylation of c-mos mRNA as a control point in Xenopus meiotic maturation
    • Sheets M.D., Wu M., Wickens M. Polyadenylation of c-mos mRNA as a control point in Xenopus meiotic maturation. Nature. 374:1995;511-516.
    • (1995) Nature , vol.374 , pp. 511-516
    • Sheets, M.D.1    Wu, M.2    Wickens, M.3
  • 46
    • 0030723206 scopus 로고    scopus 로고
    • Targeting of Tiam1 to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain
    • Stam J.C., Sander E.E., Michiels F., van Leeuwen F.N., Kain H.E., van der Kammen R.A., Collard J.G. Targeting of Tiam1 to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain. J. Biol. Chem. 272:1997;28447-28454.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28447-28454
    • Stam, J.C.1    Sander, E.E.2    Michiels, F.3    Van Leeuwen, F.N.4    Kain, H.E.5    Van der Kammen, R.A.6    Collard, J.G.7
  • 47
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with elF-4E
    • Stebbins-Boaz B., Cao Q., de Moor C.H., Mendez R., Richter J.D. Maskin is a CPEB-associated factor that transiently interacts with elF-4E. Mol. Cell. 4:1999;1017-1027.
    • (1999) Mol. Cell , vol.4 , pp. 1017-1027
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.H.3    Mendez, R.4    Richter, J.D.5
  • 48
    • 0029998640 scopus 로고    scopus 로고
    • CPEB controls the cytoplasmic polyadenylation of cyclin, Cdk2 and c-mos mRNAs and is necessary for oocyte maturation in Xenopus
    • Stebbins-Boaz B., Hake L.E., Richter J.D. CPEB controls the cytoplasmic polyadenylation of cyclin, Cdk2 and c-mos mRNAs and is necessary for oocyte maturation in Xenopus. EMBO J. 15:1996;2582-2592.
    • (1996) EMBO J. , vol.15 , pp. 2582-2592
    • Stebbins-Boaz, B.1    Hake, L.E.2    Richter, J.D.3
  • 49
    • 0034308228 scopus 로고    scopus 로고
    • Rho family GTPases: More than simple switches
    • Symons M., Settleman J. Rho family GTPases more than simple switches . Trends Cell Biol. 10:2000;415-419.
    • (2000) Trends Cell Biol. , vol.10 , pp. 415-419
    • Symons, M.1    Settleman, J.2
  • 50
    • 0034687770 scopus 로고    scopus 로고
    • Identification of XPR-1, a progesterone receptor required for Xenopus oocyte activation
    • Tian J., Kim S., Heilig E., Ruderman J.V. Identification of XPR-1, a progesterone receptor required for Xenopus oocyte activation. Proc. Natl. Acad. Sci. USA. 97:2000;14358-14363.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14358-14363
    • Tian, J.1    Kim, S.2    Heilig, E.3    Ruderman, J.V.4
  • 51
    • 0002375072 scopus 로고    scopus 로고
    • Searching for interacting proteins with the two-hybrid system II
    • P.L. Bartel, & S. Fields. Oxford: Oxford Univ. Press
    • Vojtek A.B., Cooper J.A., Hollenberg S.M. Searching for interacting proteins with the two-hybrid system II. Bartel P.L., Fields S. The Yeast Two-Hybrid System. 1997;29-42 Oxford Univ. Press, Oxford.
    • (1997) The Yeast Two-Hybrid System , pp. 29-42
    • Vojtek, A.B.1    Cooper, J.A.2    Hollenberg, S.M.3
  • 52
    • 0029155976 scopus 로고
    • Expression cloning of lfc, a novel oncogene with structural similarities to guanine nucleotide exchange factors and to the regulatory region of protein kinase C
    • Whitehead I., Kirk H., Tognon C., Trigo-Gonzalez G., Kay R. Expression cloning of lfc, a novel oncogene with structural similarities to guanine nucleotide exchange factors and to the regulatory region of protein kinase C. J. Biol. Chem. 270:1995;18388-18395.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18388-18395
    • Whitehead, I.1    Kirk, H.2    Tognon, C.3    Trigo-Gonzalez, G.4    Kay, R.5
  • 54
    • 0002068909 scopus 로고    scopus 로고
    • Translational control of developmental decisions
    • N. Sonenberg, J.W.B. Hershey, & M.B. Mathews. Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Wickens M., Goodwin E.B., Kimble J., Strickland S., Hentze M. Translational control of developmental decisions. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;295-370 Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 295-370
    • Wickens, M.1    Goodwin, E.B.2    Kimble, J.3    Strickland, S.4    Hentze, M.5
  • 55
    • 0033858595 scopus 로고    scopus 로고
    • Importance of spatial activation of Cdc42 and rac small G Proteins by frabin for microspike formation in MDCK cells
    • Yasuda T., Ohtsuka T., Inoue E., Yokoyama S., Sakisaka T., Kodama A., Takaishi K., Takai Y. Importance of spatial activation of Cdc42 and rac small G Proteins by frabin for microspike formation in MDCK cells. Genes Cells. 5:2000;583-591.
    • (2000) Genes Cells , vol.5 , pp. 583-591
    • Yasuda, T.1    Ohtsuka, T.2    Inoue, E.3    Yokoyama, S.4    Sakisaka, T.5    Kodama, A.6    Takaishi, K.7    Takai, Y.8
  • 56
    • 0026580143 scopus 로고
    • Meiotic initiation by the mos protein in Xenopus
    • Yew N., Mellini M.L., Vande Woude G.F. Meiotic initiation by the mos protein in Xenopus. Nature. 355:1992;649-652.
    • (1992) Nature , vol.355 , pp. 649-652
    • Yew, N.1    Mellini, M.L.2    Vande Woude, G.F.3


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