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Volumn 239, Issue 2, 1999, Pages 301-308

Identification of the Xenopus 20S proteasome α4 subunit which is modified in the meiotic cell cycle

Author keywords

4 Subunits; Dephosphorylation; Meiotic cell cycle; Phosphorylation; Proteasomes

Indexed keywords

PROTEASOME;

EID: 0032740651     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00406-0     Document Type: Article
Times cited : (18)

References (28)
  • 1
    • 0029876795 scopus 로고    scopus 로고
    • Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis
    • Castaño J.G., Mahillo E., Arizti P., Arribas J. Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis. Biochemistry. 35:1996;3782-3789.
    • (1996) Biochemistry , vol.35 , pp. 3782-3789
    • Castaño, J.G.1    Mahillo, E.2    Arizti, P.3    Arribas, J.4
  • 2
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., Goldberg A. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:1996;801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.3
  • 3
    • 0025988339 scopus 로고
    • Deduced primary structure of a Xenopus proteasome subunit XC3 and expression of its mRNA during early development
    • Fujii G., Tashiro K., Emori Y., Saigo K., Tanaka K., Shiokawa K. Deduced primary structure of a Xenopus proteasome subunit XC3 and expression of its mRNA during early development. Biochem. Biophys. Res. Commun. 178:1991;1233-1239.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1233-1239
    • Fujii, G.1    Tashiro, K.2    Emori, Y.3    Saigo, K.4    Tanaka, K.5    Shiokawa, K.6
  • 4
    • 0029964613 scopus 로고    scopus 로고
    • Requirement for cAMP-PKA pathway activation by M phase-promoting factor in the transition from mitosis to interphase
    • Grieco D., Porcellini A., Awedimento E.V., Gottesman M. Requirement for cAMP-PKA pathway activation by M phase-promoting factor in the transition from mitosis to interphase. Science. 271:1996;1718-1722.
    • (1996) Science , vol.271 , pp. 1718-1722
    • Grieco, D.1    Porcellini, A.2    Awedimento, E.V.3    Gottesman, M.4
  • 5
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M., Murray A.W., Kirshner M.W. Cyclin is degraded by the ubiquitin pathway. Nature. 349:1991;132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirshner, M.W.3
  • 7
    • 0024497473 scopus 로고
    • The Drosophila proteasome undergoes changes in its subunit pattern during development
    • Haass C., Kloetzel P.M. The Drosophila proteasome undergoes changes in its subunit pattern during development. Exp. Cell Res. 180:1989;243-252.
    • (1989) Exp. Cell Res. , vol.180 , pp. 243-252
    • Haass, C.1    Kloetzel, P.M.2
  • 9
    • 0000796919 scopus 로고    scopus 로고
    • Molecular cloning of cDNA encoding a 20S proteasome α2 subunit from goldfish (Carassius auratus) and its expression analysis
    • Horiguchi R., Tokumoto M., Yoshiura Y., Aida K., Nagahama Y., Tokumoto T. Molecular cloning of cDNA encoding a 20S proteasome α2 subunit from goldfish (Carassius auratus) and its expression analysis. Zool. Sci. 15:1998;773-777.
    • (1998) Zool. Sci. , vol.15 , pp. 773-777
    • Horiguchi, R.1    Tokumoto, M.2    Yoshiura, Y.3    Aida, K.4    Nagahama, Y.5    Tokumoto, T.6
  • 10
    • 0029986179 scopus 로고    scopus 로고
    • Proteasome complex as a potential cellular target of hepatitis B virus X protein
    • Huang J., Kwong J., Sun E.C., Liang T.J. Proteasome complex as a potential cellular target of hepatitis B virus X protein. J. Virol. 70:1996;5582-5591.
    • (1996) J. Virol. , vol.70 , pp. 5582-5591
    • Huang, J.1    Kwong, J.2    Sun, E.C.3    Liang, T.J.4
  • 11
    • 0030906979 scopus 로고    scopus 로고
    • Differential expression of a proteasomal subunit during chick development
    • Hutson M.R., Rhodes M.R., Kirby M.L. Differential expression of a proteasomal subunit during chick development. Biochem. Biophys. Res. Commun. 234:1997;216-223.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 216-223
    • Hutson, M.R.1    Rhodes, M.R.2    Kirby, M.L.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0027519780 scopus 로고
    • Calmodulin-dependent protein kinase II mediates inactivation of MPF and CSF upon fertilization of Xenopus eggs
    • Lorca T., Cruzalegui F.H., Fesquet D., Cavadore J.M, Méry J., Means A., Dorée M. Calmodulin-dependent protein kinase II mediates inactivation of MPF and CSF upon fertilization of Xenopus eggs. Nature. 366:1993;270-273.
    • (1993) Nature , vol.366 , pp. 270-273
    • Lorca, T.1    Cruzalegui, F.H.2    Fesquet, D.3    Cavadore, J.M.4    Méry, J.5    Means, A.6    Dorée, M.7
  • 14
    • 0027267492 scopus 로고
    • Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit
    • Ludemann R., Lerea K.M., Etlinger J.D. Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit. J. Biol. Chem. 268:1993;17413-17417.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17413-17417
    • Ludemann, R.1    Lerea, K.M.2    Etlinger, J.D.3
  • 18
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell P.Z., Goodman H.M., O'Farrell P.H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 12:1977;1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 19
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M., Tam S.W., Theodoras A.M., Beer R.P., Del S.G., Chau V., Yew P.R., Draetta G.F., Rolfe M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science. 269:1995;682-685.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3    Beer, R.P.4    Del, S.G.5    Chau, V.6    Yew, P.R.7    Draetta, G.F.8    Rolfe, M.9
  • 20
    • 0025012292 scopus 로고
    • Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase
    • Pereria M.E., Wilk S. Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase. Arch. Biochem. Biophys. 283:1990;68-74.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 68-74
    • Pereria, M.E.1    Wilk, S.2
  • 21
    • 0023952119 scopus 로고
    • Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae
    • Remacha M., Saenz-Robles M.T., Vilella M.D., Ballesta J.P.G. Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae. J. Biol. Chem. 263:1988;9094-9101.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9094-9101
    • Remacha, M.1    Saenz-Robles, M.T.2    Vilella, M.D.3    Ballesta, J.P.G.4
  • 22
    • 0031755478 scopus 로고    scopus 로고
    • Nature and role of proteasomes in maturation of fish oocytes
    • Tokumoto T. Nature and role of proteasomes in maturation of fish oocytes. Int. Rev. Cytol. 186:1999;261-294.
    • (1999) Int. Rev. Cytol. , vol.186 , pp. 261-294
    • Tokumoto, T.1
  • 23
    • 0027771146 scopus 로고
    • 20S latent proteasomes isolated from the cytosol of Xenopus oocytes: Purification and partial characterization
    • Tokumoto T., Ishikawa K. 20S latent proteasomes isolated from the cytosol of Xenopus oocytes: purification and partial characterization. Biomed. Res. 14:1993;391-401.
    • (1993) Biomed. Res. , vol.14 , pp. 391-401
    • Tokumoto, T.1    Ishikawa, K.2
  • 24
    • 0027203388 scopus 로고
    • A novel "active" form of proteasomes from Xenopus laevis ovary cytosol
    • Tokumoto T., Ishikawa K. A novel "active" form of proteasomes from Xenopus laevis ovary cytosol. Biochem. Biophys. Res. Commun. 192:1993;1106-1114.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 1106-1114
    • Tokumoto, T.1    Ishikawa, K.2
  • 25
    • 0028832295 scopus 로고
    • Characterization of active proteasome (26S proteasome) from Xenopus laevis
    • Tokumoto T., Ishikawa K. Characterization of active proteasome (26S proteasome) from Xenopus laevis. Biomed. Res. 16:1995;295-302.
    • (1995) Biomed. Res. , vol.16 , pp. 295-302
    • Tokumoto, T.1    Ishikawa, K.2
  • 28
    • 0029066783 scopus 로고
    • Purification of latent proteasome (20S proteasome) and demonstration of active proteasome in goldfish (Carassius auratus) oocyte cytosol
    • Tokumoto T., Yamashita M., Yoshikuni M., Kajiura H., Nagahama Y. Purification of latent proteasome (20S proteasome) and demonstration of active proteasome in goldfish (Carassius auratus) oocyte cytosol. Biomed. Res. 16:1995;173-186.
    • (1995) Biomed. Res. , vol.16 , pp. 173-186
    • Tokumoto, T.1    Yamashita, M.2    Yoshikuni, M.3    Kajiura, H.4    Nagahama, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.