메뉴 건너뛰기




Volumn 2, Issue 8, 2000, Pages

Evolution and function of ubiquitin-like protein-conjugation systems

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; UBIQUITIN;

EID: 0034253588     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35019643     Document Type: Review
Times cited : (380)

References (30)
  • 1
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A. L. & Siepmann, T. J. Pathways of ubiquitin conjugation. FASEB J. 11, 1257-1268 (1997).
    • (1997) FASEB J. , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 2
    • 0032053883 scopus 로고    scopus 로고
    • There's the rub: A novel ubiquitin-like modification involved in cell cycle regulation
    • Hochstrasser, M. There's the Rub: a novel ubiquitin-like modification involved in cell cycle regulation. Genes Dev. 12, 901-907 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 901-907
    • Hochstrasser, M.1
  • 3
    • 0033231542 scopus 로고    scopus 로고
    • Polypeptide tags, ubiquitous modifiers for plant protein regulation
    • Vierstra, R. D. & Callis, J. Polypeptide tags, ubiquitous modifiers for plant protein regulation. Plant Mol. Biol. 41, 435-442 (1999).
    • (1999) Plant Mol. Biol. , vol.41 , pp. 435-442
    • Vierstra, R.D.1    Callis, J.2
  • 4
  • 5
    • 0032738332 scopus 로고    scopus 로고
    • SUMO/sentrin: Protein modifiers regulating important cellular functions
    • Kretz-Remy, C. & Tanguay, R.M. SUMO/sentrin: protein modifiers regulating important cellular functions. Biochem. Cell Biol. 77, 299-309 (1999).
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 299-309
    • Kretz-Remy, C.1    Tanguay, R.M.2
  • 6
    • 0032547959 scopus 로고    scopus 로고
    • The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis
    • Epps, J. L. & Tanda, S. The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis. Curr. Biol. 8, 1277-1280 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1277-1280
    • Epps, J.L.1    Tanda, S.2
  • 7
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-B activation
    • Desterro, J. M. P., Rodriguez, M. S. & Hay, R. T. SUMO-1 modification of IκBα inhibits NF-B activation. Mol. Cell 2, 233-239 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 8
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • Comer, F. I. & Hart, G. W. O-GlcNAc and the control of gene expression Biochim. Biophys. Acta 1473, 161-171 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 9
    • 0034635361 scopus 로고    scopus 로고
    • A functional interaction between dorsal and components of the Smt3 conjugation machinery
    • Bhaskar, V., Valentine, S. A. & Courey, A. J. A functional interaction between dorsal and components of the Smt3 conjugation machinery J. Biol. Chem. 275, 4033-4040 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4033-4040
    • Bhaskar, V.1    Valentine, S.A.2    Courey, A.J.3
  • 10
    • 0034607653 scopus 로고    scopus 로고
    • C-Jun and p53 activity is modulated by SUMO-1 modification
    • Muller, S. et al. c-Jun and p53 activity is modulated by SUMO-1 modification. J. Biol. Chem. 275, 13321-13329 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13321-13329
    • Muller, S.1
  • 11
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(beta(TrCP-dependent ubiquitination of IkappaBalpha
    • Read, M. A. et al. Nedd8 modification of cul-1 activates SCF(beta(TrCP-dependent ubiquitination of IkappaBalpha. Mol. Cell Biol. 20, 2326-2333 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2326-2333
    • Read, M.A.1
  • 12
    • 0032727343 scopus 로고    scopus 로고
    • The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
    • Kamura, T., Conrad, M. N., Van, Q., Conaway, R. C. & Conaway, J. W. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev. 13, 2928-2933 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2928-2933
    • Kamura, T.1    Conrad, M.N.2    Yan, Q.3    Conaway, R.C.4    Conaway, J.W.5
  • 13
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima, N. et al. A protein conjugation system essential for autophagy. Nature 395, 395-398 (1998).
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1
  • 14
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
    • Furukawa, K., Mizushima, N., Noda, T. & Ohsumi, Y. A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J. Biol. Chem. 275, 7462-7465 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 15
    • 0032504021 scopus 로고    scopus 로고
    • Structure determination of the small ubiquitin-related modifier SUMO-1
    • Bayer, P. et al. Structure determination of the small ubiquitin-related modifier SUMO-1. J. Mol. Biol. 280, 275-286 (1998).
    • (1998) J. Mol. Biol. , vol.280 , pp. 275-286
    • Bayer, P.1
  • 16
    • 0034646567 scopus 로고    scopus 로고
    • Structure of the CAD domain of caspase-activated dnase and interaction with the CAD domain of its inhibitor
    • Uegaki, K. et al. Structure of the CAD domain of caspase-activated DNase and interaction with the CAD domain of its inhibitor. J. Mol. Biol. 297, 1121-1128 (2000).
    • (2000) J. Mol. Biol. , vol.297 , pp. 1121-1128
    • Uegaki, K.1
  • 17
    • 0033280667 scopus 로고    scopus 로고
    • Vacuolar import of proteins and organelles from the cytoplasm
    • Klionsky, D. J. & Ohsumi, Y. Vacuolar import of proteins and organelles from the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 1-32 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 1-32
    • Klionsky, D.J.1    Ohsumi, Y.2
  • 18
    • 0029295816 scopus 로고
    • Mammalian splicing factor SF3 a120 represents a new member of the SURP family of proteins and is homologous to the essential splicing factor PRP21p of Saccharomyces cerevisiae
    • Kramer, A., Mulhauser, F., Wersig, C., Groning, K. & Bilbe, G. Mammalian splicing factor SF3 a120 represents a new member of the SURP family of proteins and is homologous to the essential splicing factor PRP21p of Saccharomyces cerevisiae. RNA 1, 260-272 (1995).
    • (1995) RNA , vol.1 , pp. 260-272
    • Kramer, A.1    Mulhauser, F.2    Wersig, C.3    Groning, K.4    Bilbe, G.5
  • 19
    • 0032554017 scopus 로고    scopus 로고
    • Two types of chicken 2′, 5′-oligoadenylate synthetase mRNA derived from alleles at a single locus
    • Yamamoto, A. et al. Two types of chicken 2′, 5′-oligoadenylate synthetase mRNA derived from alleles at a single locus. Biochim. Biophys. Acta 1395, 181-191 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1395 , pp. 181-191
    • Yamamoto, A.1
  • 20
    • 0030868420 scopus 로고    scopus 로고
    • Biosynthesis and processing of the molybdenum cofactors
    • Rajagopalan, K. V. Biosynthesis and processing of the molybdenum cofactors. Biochem. Soc. Trans. 25, 757-761 (1997).
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 757-761
    • Rajagopalan, K.V.1
  • 21
    • 0032568948 scopus 로고    scopus 로고
    • Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation
    • Taylor, S. V. et al. Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. J. Biol. Chem. 273, 16555-16560 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 16555-16560
    • Taylor, S.V.1
  • 22
    • 0033516582 scopus 로고    scopus 로고
    • Eukaryotic molybdopterin synthase. Biochemical and molecular studies of Aspergillus nidulans cnxG and cnxH mutants
    • Unkles, S. E., Heck, I. S., Appleyard, M. V. & Kinghorn, J. R. Eukaryotic molybdopterin synthase. Biochemical and molecular studies of Aspergillus nidulans cnxG and cnxH mutants. J. Biol. Chem. 274, 19286-19293 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 19286-19293
    • Unkles, S.E.1    Heck, I.S.2    Appleyard, M.V.3    Kinghorn, J.R.4
  • 23
    • 0028868830 scopus 로고
    • Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7
    • Gonzalez-Pastor, J. E., San Millan, J. L, Castilla, M. A. & Moreno, F. Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7. J. Bacteriol. 177, 7131-7140 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 7131-7140
    • Gonzalez-Pastor, J.E.1    San Millan, J.L.2    Castilla, M.A.3    Moreno, F.4
  • 24
    • 0025321774 scopus 로고
    • Expression, nucleotide sequence and mutational analysis of two open reading frames in the nif gene region of Anabaena sp. Strain PCC7120
    • Borthakur, D., Basche, M., Buikema, W. J., Borthakur, P. B. & Haselkorn, R. Expression, nucleotide sequence and mutational analysis of two open reading frames in the nif gene region of Anabaena sp. strain PCC7120. Mol. Gen. Genet. 221, 227-234 (1990).
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 227-234
    • Borthakur, D.1    Basche, M.2    Buikema, W.J.3    Borthakur, P.B.4    Haselkorn, R.5
  • 25
    • 0034708503 scopus 로고    scopus 로고
    • Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate
    • Palenchar, P. M., Buck, C. J., Cheng, H., Larson, T. J. & Mueller, E. G. Evidence that Thil, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J. Biol. Chem. 275, 8283-8286 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 8283-8286
    • Palenchar, P.M.1    Buck, C.J.2    Cheng, H.3    Larson, T.J.4    Mueller, E.G.5
  • 26
    • 0032508464 scopus 로고    scopus 로고
    • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain
    • Hofmann, K., Bucher, P. & Kajava, A. V. A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J. Mol. Biol. 282, 195-208 (1998).
    • (1998) J. Mol. Biol. , vol.282 , pp. 195-208
    • Hofmann, K.1    Bucher, P.2    Kajava, A.V.3
  • 27
    • 2642671959 scopus 로고    scopus 로고
    • The Aspergillus nidulans cnxF gene and its involvement in molybdopterin biosynthesis. Molecular characterization and analysis of in vivo generated mutants
    • Appleyard, M.V. et al. The Aspergillus nidulans cnxF gene and its involvement in molybdopterin biosynthesis. Molecular characterization and analysis of in vivo generated mutants. J. Biol. Chem. 273, 14869-14876 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 14869-14876
    • Appleyard, M.V.1
  • 28
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S-J. & Hochstrasser, M. A new protease required for cell-cycle progression in yeast. Nature 398, 246-251 (1999).
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 29
    • 0031958596 scopus 로고    scopus 로고
    • Insertion of a sequence encoding light chain three of microtubule-associated proteins 1A and 1B in a pestivirus genome: Connection with virus cytopathogenicity and induction of lethal disease in cattle
    • Meyers, G., Stoll, D. & Gunn, M. Insertion of a sequence encoding light chain three of microtubule-associated proteins 1A and 1B in a pestivirus genome: connection with virus cytopathogenicity and induction of lethal disease in cattle. J. Virol. 72, 4139-4148 (1998).
    • (1998) J. Virol. , vol.72 , pp. 4139-4148
    • Meyers, G.1    Stoll, D.2    Gunn, M.3
  • 30
    • 0034646676 scopus 로고    scopus 로고
    • Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati, R. & Lauhon, C. T. Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. J. Biol. Chem. 275, 10727-10730 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10727-10730
    • Kambampati, R.1    Lauhon, C.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.