메뉴 건너뛰기




Volumn 96, Issue 5, 1999, Pages 645-653

Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair

Author keywords

[No Author keywords available]

Indexed keywords

UBIQUITIN;

EID: 0033525582     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80575-9     Document Type: Article
Times cited : (692)

References (55)
  • 1
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., Cao, L., and Kleckner, N. (1987). A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116, 541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 3
    • 0028314007 scopus 로고
    • Specific complex formation between yeast RAD6 and RAD18 proteins: A potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites
    • Bailly, V., Lamb, J., Sung, P., Prakash, S., and Prakash, L. (1994). Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites. Genes Dev. 8, 811-820.
    • (1994) Genes Dev. , vol.8 , pp. 811-820
    • Bailly, V.1    Lamb, J.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 4
    • 0030800865 scopus 로고    scopus 로고
    • Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities
    • Bailly, V., Lauder, S., Prakash, S., and Prakash, L. (1997). Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem. 272, 23360-23365.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23360-23365
    • Bailly, V.1    Lauder, S.2    Prakash, S.3    Prakash, L.4
  • 5
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal, R., Deveraux, Q., Xia, G., Rechsteiner, M., and Pickart, C. (1996). Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc. Natl. Acad. Sci. USA 93, 861-866.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 7
    • 0032510731 scopus 로고    scopus 로고
    • MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway
    • Broomfield, S., Chow, B.L., and Xiao, W. (1998). MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway. Proc. Natl. Acad. Sci. USA 95, 5678-5683.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5678-5683
    • Broomfield, S.1    Chow, B.L.2    Xiao, W.3
  • 8
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J.W., Bachmair, A., Marriott, D., Ecker, D.J., Gonda, D.K., and Varshavsky, A. (1989). A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 9
    • 0025644201 scopus 로고
    • A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine-48 of ubiquitin
    • Chen, Z., and Pickart, C.M. (1990). A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine-48 of ubiquitin. J. Biol. Chem. 265, 21835-21842.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21835-21842
    • Chen, Z.1    Pickart, C.M.2
  • 10
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • Chen, P., Johnson, P., Sommer, T., Jentsch, S., and Hochstrasser, M. (1993). Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 11
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway
    • Chen, Z.J., Hagler, J., Palombella, V.J., Melandri, F., Scherer, D., Ballard, D., and Maniatis, T. (1995). Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway. Genes Dev. 9, 1586-1597.
    • (1995) Genes Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.J.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 12
    • 0027788114 scopus 로고
    • Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: Crystal structure of yeast Ubc4
    • Cook, W.J., Jeffrey, L.C., Xu, Y., and Chau, V. (1993). Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4. Biochemistry 32, 13809-13817.
    • (1993) Biochemistry , vol.32 , pp. 13809-13817
    • Cook, W.J.1    Jeffrey, L.C.2    Xu, Y.3    Chau, V.4
  • 13
    • 0028316184 scopus 로고
    • Structure of tetraubiquitin shows how multiubiquitin chains can be formed
    • Cook, W.J., Jeffrey, L.C., Kasperek, E., and Pickart, C.M. (1994). Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J. Mol. Biol. 236, 601-609.
    • (1994) J. Mol. Biol. , vol.236 , pp. 601-609
    • Cook, W.J.1    Jeffrey, L.C.2    Kasperek, E.3    Pickart, C.M.4
  • 14
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman, R.M.R., Correll, C.C., Kaplan, K.B., and Deshaies, R.J. (1997). A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.R.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 15
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., Sadis, S., Monia, B.P., Boucher, P., Ecker, D.J., Crooke, S.T., and Chau, V. (1994). Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol. 14, 5501-5509.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 16
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A.L., and Siepmann, T.J. (1997). Pathways of ubiquitin conjugation. FASEB J. 11, 1257-1268.
    • (1997) FASEB J. , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 17
    • 0030772445 scopus 로고    scopus 로고
    • Structure and function of ubiquitin conjugating enzyme E2-25K: The tail is a core-dependent activity element
    • Haldeman, M.T., Xia, G., Kasperek, E.M., and Pickart, C.M. (1997). Structure and function of ubiquitin conjugating enzyme E2-25K: the tail is a core-dependent activity element. Biochemistry 36, 10526-10537.
    • (1997) Biochemistry , vol.36 , pp. 10526-10537
    • Haldeman, M.T.1    Xia, G.2    Kasperek, E.M.3    Pickart, C.M.4
  • 18
    • 0021813071 scopus 로고
    • Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates
    • Hershko, A., and Heller, H. (1985). Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates. Biochem. Biophys. Res. Commun. 128, 1079-1086.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 1079-1086
    • Hershko, A.1    Heller, H.2
  • 20
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L., and Riezman, H. (1996). Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 21
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996). Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 22
    • 0029821534 scopus 로고    scopus 로고
    • The tail of a ubiquitin-conjugating enzyme redirects multi-ubiquitin chain synthesis from the lysine 48-linked configuration to a novel nonlysine-linked form
    • Hodgins, R., Gwozd, C., Arnason, T., Cummings, M., and Ellison, M.J. (1996). The tail of a ubiquitin-conjugating enzyme redirects multi-ubiquitin chain synthesis from the lysine 48-linked configuration to a novel nonlysine-linked form. J. Biol. Chem. 271, 28766-28771.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28766-28771
    • Hodgins, R.1    Gwozd, C.2    Arnason, T.3    Cummings, M.4    Ellison, M.J.5
  • 23
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J.M., Scheffner, M., Beaudenon, S., and Howley, P.M. (1995). A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA 92, 2563-2567.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 24
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch, S., McGrath, J.P., and Varshavsky, A. (1987). The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329, 131-133.
    • (1987) Nature , vol.329 , pp. 131-133
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 25
    • 0031201741 scopus 로고    scopus 로고
    • TSG101 may be the prototype of a class of dominant negative ubiquitin regulators
    • Koonin, E.V., and Abagyan, R.A. (1997). TSG101 may be the prototype of a class of dominant negative ubiquitin regulators. Nat. Genet. 16, 330-331.
    • (1997) Nat. Genet. , vol.16 , pp. 330-331
    • Koonin, E.V.1    Abagyan, R.A.2
  • 26
    • 0030908874 scopus 로고    scopus 로고
    • Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity
    • Kumar, S., Kao, W.H., and Howley, P.M. (1997). Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J. Biol. Chem. 272, 13548-13554.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13548-13554
    • Kumar, S.1    Kao, W.H.2    Howley, P.M.3
  • 27
    • 0029904430 scopus 로고    scopus 로고
    • Tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
    • Li, L., and Cohen, S.N. (1996). tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells. Cell 85, 319-329.
    • (1996) Cell , vol.85 , pp. 319-329
    • Li, L.1    Cohen, S.N.2
  • 28
    • 0026737743 scopus 로고
    • Construction of a GAL1-regulated yeast cDNA expression library and its application to the identification of genes whose overexpression causes lethality in yeast
    • Liu, H., Krizek, J., and Bretscher, A. (1992). Construction of a GAL1-regulated yeast cDNA expression library and its application to the identification of genes whose overexpression causes lethality in yeast. Genetics 132, 665-673.
    • (1992) Genetics , vol.132 , pp. 665-673
    • Liu, H.1    Krizek, J.2    Bretscher, A.3
  • 29
    • 0032505022 scopus 로고    scopus 로고
    • Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines
    • Ma, L., Broomfield, S., Lavery, C., Lin, S.L., Xiao, W., and Bacchetti, S. (1998). Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines. Oncogene 17, 1321-1326.
    • (1998) Oncogene , vol.17 , pp. 1321-1326
    • Ma, L.1    Broomfield, S.2    Lavery, C.3    Lin, S.L.4    Xiao, W.5    Bacchetti, S.6
  • 30
    • 0027185303 scopus 로고
    • The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes
    • Muralidhar, M.G., and Thomas, J.B. (1993). The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes. Neuron 11, 253-266.
    • (1993) Neuron , vol.11 , pp. 253-266
    • Muralidhar, M.G.1    Thomas, J.B.2
  • 31
    • 0030043724 scopus 로고    scopus 로고
    • Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 and characterization of their interaction with E6-AP and RSP5
    • Nuber, U., Schwarz, S., Kaiser, P., Schneider, R., and Scheffner, M. (1996). Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 and characterization of their interaction with E6-AP and RSP5. J. Biol. Chem. 271, 2795-2800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2795-2800
    • Nuber, U.1    Schwarz, S.2    Kaiser, P.3    Schneider, R.4    Scheffner, M.5
  • 32
    • 0028271574 scopus 로고
    • Bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog
    • Oh, C.E., McMahon, R., Benzer, S., and Tanouye, M.A. (1994). bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog. J. Neurosci. 14, 3166-3179.
    • (1994) J. Neurosci. , vol.14 , pp. 3166-3179
    • Oh, C.E.1    McMahon, R.2    Benzer, S.3    Tanouye, M.A.4
  • 33
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V.J., Rando, O.J., Goldberg, A.L., and Maniatis, T. (1994). The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 34
    • 0031831274 scopus 로고    scopus 로고
    • Combinatorial control in ubiquitin-dependent proteolysis: Don't Skp the F-box hypothesis
    • Patton, E., Willems, A.R., and Tyers, M. (1998). Combinatorial control in ubiquitin-dependent proteolysis: don't Skp the F-box hypothesis. Trends Genet. 14, 236-243.
    • (1998) Trends Genet. , vol.14 , pp. 236-243
    • Patton, E.1    Willems, A.R.2    Tyers, M.3
  • 35
    • 0002081502 scopus 로고    scopus 로고
    • Cell cycle control by ubiquitin-dependent proteolysis
    • J.-M. Peters, J.R. Harris, and D. Finley, eds. (New York: Plenum Press)
    • Peters, J.-M., King, R.W., and Deshaies, R.J. (1998). Cell cycle control by ubiquitin-dependent proteolysis. In Ubiquitin and the Biology of the Cell, J.-M. Peters, J.R. Harris, and D. Finley, eds. (New York: Plenum Press), pp. 345-387.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 345-387
    • Peters, J.-M.1    King, R.W.2    Deshaies, R.J.3
  • 36
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart, C.M. (1997). Targeting of substrates to the 26S proteasome. FASEB J. 11, 1055-1066.
    • (1997) FASEB J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 37
    • 0023682264 scopus 로고
    • Levels of active ubiquitin carrier proteins decline during erythroid maturation
    • Pickart, C.M., and Vella, A.T. (1988). Levels of active ubiquitin carrier proteins decline during erythroid maturation. J. Biol. Chem. 263, 12028-12035.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12028-12035
    • Pickart, C.M.1    Vella, A.T.2
  • 38
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths
    • Piotrowski, J., Beal, R., Hoffman, L., Wilkinson, K.D., Cohen, R.E., and Pickart, C.M. (1997). Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths. J. Biol. Chem. 272, 23712-23721.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23712-23721
    • Piotrowski, J.1    Beal, R.2    Hoffman, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 39
    • 0031180564 scopus 로고    scopus 로고
    • The breast cancer gene product TSG101: A regulator of ubiquitination?
    • Ponting, C.P., Cai, Y-D., and Bork, P. (1997). The breast cancer gene product TSG101: a regulator of ubiquitination? J. Mol. Med. 75, 467-469.
    • (1997) J. Mol. Med. , vol.75 , pp. 467-469
    • Ponting, C.P.1    Cai, Y.-D.2    Bork, P.3
  • 40
    • 0017409010 scopus 로고
    • Isolation and characterization of M ms-sensitive mutants of Saccharomyces cerevisiae
    • Prakash, L., and Prakash, S. (1977). Isolation and characterization of M ms-sensitive mutants of Saccharomyces cerevisiae. Genetics 86, 33-55.
    • (1977) Genetics , vol.86 , pp. 33-55
    • Prakash, L.1    Prakash, S.2
  • 41
    • 0027146121 scopus 로고
    • DNA repair genes and proteins of Saccharomyces cerevisiae
    • Prakash, S., Sung, P., and Prakash, L. (1993). DNA repair genes and proteins of Saccharomyces cerevisiae. Annu. Rev. Genet. 27, 33-70.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 33-70
    • Prakash, S.1    Sung, P.2    Prakash, L.3
  • 42
    • 0021925909 scopus 로고
    • RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive aspartates
    • Reynolds, P., Weber, S., and Prakash, L. (1985). RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive aspartates. Proc. Natl. Acad. Sci. USA 82, 168-172.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 168-172
    • Reynolds, P.1    Weber, S.2    Prakash, L.3
  • 43
    • 0031962188 scopus 로고    scopus 로고
    • Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells
    • Sancho, E., Vilá, M.R., Sánchez-Pulido, L., Lozano, J.J., Paciucci, R., Nadal, M., Fox, M., Harvey, C., Bercovich, B., Loukili, N., et al. (1997). Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells. Mol. Cell. Biol. 18, 576-589.
    • (1997) Mol. Cell. Biol. , vol.18 , pp. 576-589
    • Sancho, E.1    Vilá, M.R.2    Sánchez-Pulido, L.3    Lozano, J.J.4    Paciucci, R.5    Nadal, M.6    Fox, M.7    Harvey, C.8    Bercovich, B.9    Loukili, N.10
  • 44
    • 0026519884 scopus 로고
    • Expression of argU, the Escherichia coli gene coding for a rare arginine tRNA
    • Saxena, P., and Walker, J.R. (1992). Expression of argU, the Escherichia coli gene coding for a rare arginine tRNA. J. Bacteriol. 174, 1956-1964.
    • (1992) J. Bacteriol. , vol.174 , pp. 1956-1964
    • Saxena, P.1    Walker, J.R.2
  • 45
    • 0038400239 scopus 로고    scopus 로고
    • The genetics and biochemistry of the repair of UV-induced DNA damage in Saccharomyces cerevisiae
    • J.A. Nickoloff and M.F. Hoekstra, eds. (Totowa, NJ: Humana Press)
    • Siede, W. (1998). The genetics and biochemistry of the repair of UV-induced DNA damage in Saccharomyces cerevisiae. In DNA Damage and Repair, J.A. Nickoloff and M.F. Hoekstra, eds. (Totowa, NJ: Humana Press), pp. 307-333.
    • (1998) DNA Damage and Repair , pp. 307-333
    • Siede, W.1
  • 46
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., Craig, K.L., Tyers, M., Elledge, S.J., and Harper, J.W. (1997). F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91, 209-219.
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 47
    • 0029805901 scopus 로고    scopus 로고
    • Role of the ubiquitin/proteasome system in regulated protein degradation in Saccharomyces cerevisiae
    • Smith, S.E., Koegl, M., and Jentsch, S. (1996). Role of the ubiquitin/proteasome system in regulated protein degradation in Saccharomyces cerevisiae. Biol. Chem. 377, 437-446.
    • (1996) Biol. Chem. , vol.377 , pp. 437-446
    • Smith, S.E.1    Koegl, M.2    Jentsch, S.3
  • 48
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis, S., Haas, A.L., and Finley, D. (1995). A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265-1273.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 49
    • 0032512632 scopus 로고    scopus 로고
    • Role of UEV-1A, a homologue of tumor suppressor protein TSG101, in protection from DNA damage
    • Thomson, T.M., Kalid, H., Lozano, J.J., Sancho, E., and Ariño, J. (1998). Role of UEV-1A, a homologue of tumor suppressor protein TSG101, in protection from DNA damage. FEBS Lett. 423, 49-52.
    • (1998) FEBS Lett. , vol.423 , pp. 49-52
    • Thomson, T.M.1    Kalid, H.2    Lozano, J.J.3    Sancho, E.4    Ariño, J.5
  • 50
    • 0029821929 scopus 로고    scopus 로고
    • Requirement of proliferating cell nuclear antigen in RAD6-dependent postreplicational DNA repair
    • Torres-Ramos, C.A., Yoder, B.L., Burgers, P.M.J., Prakash, S., and Prakash, L. (1996). Requirement of proliferating cell nuclear antigen in RAD6-dependent postreplicational DNA repair. Proc. Natl. Acad. Sci. USA 93, 9676-9681.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9676-9681
    • Torres-Ramos, C.A.1    Yoder, B.L.2    Burgers, P.M.J.3    Prakash, S.4    Prakash, L.5
  • 51
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996). The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 93, 12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 52
    • 0019877280 scopus 로고
    • Stimulation of ATP-dependent proteolysis requires ubiquitin with the COOH-terminal sequence Arg-Gly-Gly
    • Wilkinson, K.D., and Audhya, T.K. (1981 ). Stimulation of ATP-dependent proteolysis requires ubiquitin with the COOH-terminal sequence Arg-Gly-Gly. J. Biol. Chem. 256, 9235-9241.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9235-9241
    • Wilkinson, K.D.1    Audhya, T.K.2
  • 53
    • 0032169004 scopus 로고    scopus 로고
    • The products of the yeast MMS2 and two human homo logs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family
    • Xiao, W., Lin, S.L., Broomfield, S., Chow, B.L., and Wei, Y-F. (1998). The products of the yeast MMS2 and two human homo logs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family. Nucleic Acids Res. 26, 3908-3914.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3908-3914
    • Xiao, W.1    Lin, S.L.2    Broomfield, S.3    Chow, B.L.4    Wei, Y.-F.5
  • 54
    • 0032539548 scopus 로고    scopus 로고
    • Cell cycle-dependent subcellular localization of the TSG101 protein and mitotic and nuclear abnormalities associated with TSG101 deficiency
    • Xie, W., Li, L., and Cohen, S. (1998). Cell cycle-dependent subcellular localization of the TSG101 protein and mitotic and nuclear abnormalities associated with TSG101 deficiency. Proc. Natl. Acad. Sci. USA 95, 1595-1600.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1595-1600
    • Xie, W.1    Li, L.2    Cohen, S.3
  • 55
    • 0029761411 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product
    • Yamaguchi, T., Kim, N.-S., Sekine, S., Seino, H., Osaka, F., Yamao, F., and Kato, S. (1996). Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product. J. Biochem. 120, 494-497.
    • (1996) J. Biochem. , vol.120 , pp. 494-497
    • Yamaguchi, T.1    Kim, N.-S.2    Sekine, S.3    Seino, H.4    Osaka, F.5    Yamao, F.6    Kato, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.