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Volumn 15, Issue 18, 1996, Pages 4884-4899

Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae

Author keywords

Cell cycle; N end rule; Proteolysis; Ubiquitin; WD repeat

Indexed keywords

CELL CYCLE PROTEIN; PROTEIN; UBIQUITIN;

EID: 0029814693     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00869.x     Document Type: Article
Times cited : (238)

References (88)
  • 2
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair, A. and Varshavsky, A. (1989) The degradation signal in a short-lived protein. Cell, 56, 1019-1032.
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 3
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. and Varshavsky, A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 4
    • 0001236309 scopus 로고
    • Inhibition of the N-end rule pathway in living cells
    • Baker, R.T. and Varshavsky, A. (1991) Inhibition of the N-end rule pathway in living cells. Proc. Natl Acad. Sci. USA, 87, 2374-2378.
    • (1991) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2374-2378
    • Baker, R.T.1    Varshavsky, A.2
  • 5
    • 0029016564 scopus 로고
    • Yeast N-terminal amidase: A new enzyme and component of the N-end rule pathway
    • Baker, R.T. and Varshavsky, A. (1995) Yeast N-terminal amidase: a new enzyme and component of the N-end rule pathway. J. Biol. Chem., 270, 12065-12074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12065-12074
    • Baker, R.T.1    Varshavsky, A.2
  • 6
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker, R.T., Tobias, J.W. and Varshavsky, A. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J. Biol. Chem., 267, 23364-23375.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 7
    • 0028986667 scopus 로고
    • G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast
    • Barral, Y., Jentsch, S. and Mann, C. (1995) G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev., 9, 399-409.
    • (1995) Genes Dev. , vol.9 , pp. 399-409
    • Barral, Y.1    Jentsch, S.2    Mann, C.3
  • 8
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel, B., Wünning, I. and Varshavsky, A. (1990) The recognition component of the N-end rule pathway. EMBO J., 9, 3179-3189.
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wünning, I.2    Varshavsky, A.3
  • 10
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance
    • Boeke, J.D., Lacroute, F. and Fink, G.R. (1984) A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance. Mol. Gen. Genet., 197, 345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 11
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard, B.L., Chubet, R.G. and Vizard, D.L. (1994) Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. BioTechniques, 16, 730-734.
    • (1994) BioTechniques , vol.16 , pp. 730-734
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 12
    • 0018564346 scopus 로고
    • Transformation in yeast: Development of a hybrid cloning vector and isolation of the CAN1l gene
    • Broach, J.R., Strathern, J.N. and Hicks, J.B. (1979) Transformation in yeast: development of a hybrid cloning vector and isolation of the CAN1l gene. Gene, 8, 121-133.
    • (1979) Gene , vol.8 , pp. 121-133
    • Broach, J.R.1    Strathern, J.N.2    Hicks, J.B.3
  • 13
    • 0026783641 scopus 로고
    • Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase from Saccharomyces cerevisiae
    • Chang, Y.-H., Teichert, V. and Smith, J. (1992) Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase from Saccharomyces cerevisiae. J. Biol. Chem., 267, 8007-8011.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8007-8011
    • Chang, Y.-H.1    Teichert, V.2    Smith, J.3
  • 14
    • 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
  • 15
    • 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
  • 17
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. (1994) The ubiquitin-proteasome proteolytic pathway. Cell, 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 19
    • 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
  • 21
    • 0028841492 scopus 로고
    • Make it or break it: The role of ubiquitin-dependent proteolysis in cellular regulation
    • Deshaies, R.J. (1995) Make it or break it: the role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol., 5, 428-434.
    • (1995) Trends Cell Biol. , vol.5 , pp. 428-434
    • Deshaies, R.J.1
  • 22
    • 0025913944 scopus 로고
    • The N-end rule is mediated by the Ubc2 (Rad6) ubiquitin-conjugating enzyme
    • Dohmen, R.J., Madura, K., Bartel, B. and Varshavsky, A. (1991) The N-end rule is mediated by the Ubc2 (Rad6) ubiquitin-conjugating enzyme. Proc. Natl Acad. Sci. USA, 88, 7351-7355.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7351-7355
    • Dohmen, R.J.1    Madura, K.2    Bartel, B.3    Varshavsky, A.4
  • 23
    • 0028213449 scopus 로고
    • Heat-inducible degron: A method for constructing temperature-sensitive mutants
    • Dohmen, R.J., Wu, P. and Varshavsky, A. (1994) Heat-inducible degron: a method for constructing temperature-sensitive mutants. Science, 263, 1273-1276.
    • (1994) Science , vol.263 , pp. 1273-1276
    • Dohmen, R.J.1    Wu, P.2    Varshavsky, A.3
  • 25
    • 0027204580 scopus 로고
    • Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26S protease
    • Dubiel, W., Ferrell, K. and Rechsteiner, M. (1993) Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26S protease. FEBS Lett., 323, 276-278.
    • (1993) FEBS Lett. , vol.323 , pp. 276-278
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 26
    • 0028301199 scopus 로고
    • Complete DNA sequence of yeast chromosome XI
    • Dujon, B. et al. (1994) Complete DNA sequence of yeast chromosome XI. Nature, 369, 371-378.
    • (1994) Nature , vol.369 , pp. 371-378
    • Dujon, B.1
  • 27
    • 0025965277 scopus 로고
    • PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases
    • Erdmann, R., Wiebel, F.F., Flessau, A., Rytka, J., Beyer, A., Fröhlich, K.-U. and Kunau, W.-H. (1991) PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases. Cell, 64, 499-510.
    • (1991) Cell , vol.64 , pp. 499-510
    • Erdmann, R.1    Wiebel, F.F.2    Flessau, A.3    Rytka, J.4    Beyer, A.5    Fröhlich, K.-U.6    Kunau, W.-H.7
  • 28
  • 29
    • 0028805251 scopus 로고
    • The higher plant Arabidopsis thaliana encodes a functional CDC48 homologue which is highly expressed in dividing and expanding cells
    • Feiler, H.S., Desprez, T., Santoni, V., Kronenberger, J., Cahoche, M. and Traas, J. (1995) The higher plant Arabidopsis thaliana encodes a functional CDC48 homologue which is highly expressed in dividing and expanding cells. EMBO J., 14, 5626-5637.
    • (1995) EMBO J. , vol.14 , pp. 5626-5637
    • Feiler, H.S.1    Desprez, T.2    Santoni, V.3    Kronenberger, J.4    Cahoche, M.5    Traas, J.6
  • 30
    • 0028263738 scopus 로고
    • Construction of an improved host strain for two-hybrid screening
    • Feilotter, H.E., Hannon, G.J., Ruddell, C.J. and Beach, D. (1994) Construction of an improved host strain for two-hybrid screening. Nucleic Acids Res., 22, 1502-1503.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1502-1503
    • Feilotter, H.E.1    Hannon, G.J.2    Ruddell, C.J.3    Beach, D.4
  • 31
    • 0024004720 scopus 로고
    • Purification of a RAS-responsive adenylyl cyclase complex from S.cerevisiae by use of an epitope addition method
    • Field, J., Nikawa, J.I., Broek, D., MacDonald, B., Rodgers, L., Wilson, I.A., Lerner, R.A. and Wigler, M. (1988) Purification of a RAS-responsive adenylyl cyclase complex from S.cerevisiae by use of an epitope addition method. Mol. Cell. Biol., 8, 2159-2165.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2159-2165
    • Field, J.1    Nikawa, J.I.2    Broek, D.3    MacDonald, B.4    Rodgers, L.5    Wilson, I.A.6    Lerner, R.A.7    Wigler, M.8
  • 32
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. and Song, O. (1989) A novel genetic system to detect protein-protein interactions. Nature, 340, 245-247.
    • (1989) Nature , vol.340 , pp. 245-247
    • Fields, S.1    Song, O.2
  • 33
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., Bartel, B. and Varshavsky, A. (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature, 338, 394-401.
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 34
    • 4243134624 scopus 로고
    • Repetitive segmental structure of the transducin β subunit: Homology with the CDC4 gene and identification of related mRNAs
    • Fong, H.K., Hurley, J.B., Hopkins, R.S., Miake-Lye, R., Johnson, M.S., Doolittle, R.F. and Simon, M.I. (1986) Repetitive segmental structure of the transducin β subunit: homology with the CDC4 gene and identification of related mRNAs. Proc. Natl Acad. Sci. USA, 83, 2162-2166.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 2162-2166
    • Fong, H.K.1    Hurley, J.B.2    Hopkins, R.S.3    Miake-Lye, R.4    Johnson, M.S.5    Doolittle, R.F.6    Simon, M.I.7
  • 35
    • 0025913947 scopus 로고
    • Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP, and is a member of a protein family involved in secretion, peroxisome formation, and gene expression
    • Frölich, K.-U., Fries, H.-W., Rud̈iger, M., Erdmann, R., Botstein, D. and Mecke, D. (1991) Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP, and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J. Cell Biol., 114, 443-453.
    • (1991) J. Cell Biol. , vol.114 , pp. 443-453
    • Frölich, K.-U.1    Fries, H.-W.2    Rud̈iger, M.3    Erdmann, R.4    Botstein, D.5    Mecke, D.6
  • 36
    • 0027444947 scopus 로고
    • S.cerevisiae 26S protease mutants arrest cell division in G2/metaphase
    • Ghislain, M., Udvardy, A. and Mann, C. (1993) S.cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature, 366, 358-362.
    • (1993) Nature , vol.366 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 38
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 39
    • 0028023599 scopus 로고
    • The catalytic subunit of bovine brain platelet-activating factor acetylhydrolase is a novel type of serine esterase
    • Hattori, M., Adachi, H., Tsujimoto, M., Arai, H. and Inoue, K. (1994) The catalytic subunit of bovine brain platelet-activating factor acetylhydrolase is a novel type of serine esterase. Nature, 370, 216-218.
    • (1994) Nature , vol.370 , pp. 216-218
    • Hattori, M.1    Adachi, H.2    Tsujimoto, M.3    Arai, H.4    Inoue, K.5
  • 40
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. and Ciechanover, A. (1992) The ubiquitin system for protein degradation. Annu. Rev. Biochem., 61, 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 41
    • 0027251453 scopus 로고
    • Crystal structure of a ubiquitin-dependent degradation substrate: A three-disulfide form of lysozyme
    • Hill, C.P., Johnston, N.L. and Cohen, R.E. (1993) Crystal structure of a ubiquitin-dependent degradation substrate: a three-disulfide form of lysozyme. Proc. Natl Acad. Sci. USA, 90, 4136-4140.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4136-4140
    • Hill, C.P.1    Johnston, N.L.2    Cohen, R.E.3
  • 42
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W. and Wolf, D.H. (1996) Proteasomes: destruction as a programme. Trends. Biochem. Sci., 21, 96-102.
    • (1996) Trends. Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 43
    • 0026055806 scopus 로고
    • Purification of His-tagged proteins in nondenaturing conditions suggests a convenient method for protein interaction studies
    • Hoffmann, A. and Roeder, R.G. (1991) Purification of His-tagged proteins in nondenaturing conditions suggests a convenient method for protein interaction studies. Nucleic Acids Res., 19, 6337-6338.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6337-6338
    • Hoffmann, A.1    Roeder, R.G.2
  • 44
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Biol., 7, 215-223.
    • (1995) Curr. Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 45
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast Matα2 repressor
    • Hochstrasser, M. and Varshavsky, A. (1990) In vivo degradation of a transcriptional regulator: the yeast Matα2 repressor. Cell, 61, 697-708.
    • (1990) Cell , vol.61 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 46
    • 0024440559 scopus 로고
    • Galactose as a gratuitous inducer of GAL gene expression in yeasts growing on glucose
    • Hovland, P., Flick, J., Johnston, M. and Sclafani, R.A. (1989) Galactose as a gratuitous inducer of GAL gene expression in yeasts growing on glucose. Gene, 83, 57-64.
    • (1989) Gene , vol.83 , pp. 57-64
    • Hovland, P.1    Flick, J.2    Johnston, M.3    Sclafani, R.A.4
  • 47
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Huang, Y., Baker, R.T. and Fischer-Vize, J.A. (1995) Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science, 270, 1828-1831.
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, R.T.2    Fischer-Vize, J.A.3
  • 48
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S. and Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell, 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 49
    • 0025345753 scopus 로고
    • Cis-trans recognition and subunit-specific degradation of short-lived proteins
    • Johnson, E.S., Gonda, D.K. and Varshavsky, A. (1990) Cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature, 346, 287-291.
    • (1990) Nature , vol.346 , pp. 287-291
    • Johnson, E.S.1    Gonda, D.K.2    Varshavsky, A.3
  • 50
    • 0026541141 scopus 로고
    • Ubiquitin as a degradation signal
    • Johnson, E.S., Bartel, B.W. and Varshavsky, A. (1992) Ubiquitin as a degradation signal. EMBO J., 11, 497-505.
    • (1992) EMBO J. , vol.11 , pp. 497-505
    • Johnson, E.S.1    Bartel, B.W.2    Varshavsky, A.3
  • 51
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C.M., Ota, I.M. and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem., 270, 17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.M.2    Ota, I.M.3    Varshavsky, A.4
  • 52
    • 0023088363 scopus 로고
    • Many random sequences functionally replace the secretion signal sequence of yeast invertase
    • Kaiser, C.A., Preuss, D., Grisafi, P. and Botstein, D. (1987) Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science, 235, 312-317.
    • (1987) Science , vol.235 , pp. 312-317
    • Kaiser, C.A.1    Preuss, D.2    Grisafi, P.3    Botstein, D.4
  • 53
    • 0023111691 scopus 로고
    • Use of acDNA clone to identify a supposed precursor protein containing valosin
    • Koller, K.J. and Brownstein, M.J. (1987) Use of acDNA clone to identify a supposed precursor protein containing valosin. Nature, 325, 542-545.
    • (1987) Nature , vol.325 , pp. 542-545
    • Koller, K.J.1    Brownstein, M.J.2
  • 54
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Fröhlich, K.-U. and Scheckman, R. (1995) Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell, 82, 885-893.
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Fröhlich, K.-U.2    Scheckman, R.3
  • 55
    • 0026073301 scopus 로고
    • Classical mutagenesis techniques
    • Lawrence, C.W. (1991) Classical mutagenesis techniques. Methods Enzymol., 194, 273-281.
    • (1991) Methods Enzymol. , vol.194 , pp. 273-281
    • Lawrence, C.W.1
  • 57
    • 0027163762 scopus 로고
    • Identification of mutations in p53 that affects its binding to SV40 large T antigen by using the yeast two-hybrid system
    • Li, B. and Fields, S. (1993) Identification of mutations in p53 that affects its binding to SV40 large T antigen by using the yeast two-hybrid system. FASEB J., 7, 957-963.
    • (1993) FASEB J. , vol.7 , pp. 957-963
    • Li, B.1    Fields, S.2
  • 58
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li, X. and Chang, Y.-H. (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl Acad., Sci. USA, 92, 12357-12361.
    • (1995) Proc. Natl Acad., Sci. USA , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.-H.2
  • 59
    • 0028169361 scopus 로고
    • Degradation of Gα by the N-end rule pathway
    • Madura, K. and Varshavsky, A. (1994) Degradation of Gα by the N-end rule pathway. Science, 265, 1454-1458.
    • (1994) Science , vol.265 , pp. 1454-1458
    • Madura, K.1    Varshavsky, A.2
  • 60
    • 0027316341 scopus 로고
    • N-recognin/Ubc2 interactions in the N-end rule pathway
    • Madura, K., Dohmen, R.J. and Varshavsky, A. (1993) N-recognin/Ubc2 interactions in the N-end rule pathway. J. Biol. Chem., 268, 12046-12054.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12046-12054
    • Madura, K.1    Dohmen, R.J.2    Varshavsky, A.3
  • 61
    • 0029129193 scopus 로고
    • Enigma variations: Protein mediators of membrane fusion
    • Mellman, I. (1995) Enigma variations: protein mediators of membrane fusion. Cell, 82, 869-872.
    • (1995) Cell , vol.82 , pp. 869-872
    • Mellman, I.1
  • 62
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 63
    • 0025200973 scopus 로고
    • The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes created by oligonucleotide transformation
    • Moerschell, R.P., Hosokawa, Y., Tsunasawa, S. and Sherman, F. (1990) The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes created by oligonucleotide transformation. J. Biol. Chem., 265, 19638-19643.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19638-19643
    • Moerschell, R.P.1    Hosokawa, Y.2    Tsunasawa, S.3    Sherman, F.4
  • 64
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., Schmidt, C.J., Nambudripad, R. and Smith, T.F. (1994) The ancient regulatory-protein family of WD-repeat proteins. Nature, 371, 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 65
    • 0025339890 scopus 로고
    • A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator
    • Nelböck, P., Dillon, P.J., Perkins, A. and Rosen, C.A. (1990) A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator. Science, 248, 1650-1653.
    • (1990) Science , vol.248 , pp. 1650-1653
    • Nelböck, P.1    Dillon, P.J.2    Perkins, A.3    Rosen, C.A.4
  • 66
    • 0027390598 scopus 로고
    • Suppressors of clathrin deficiency: Overexpression of ubiquitin rescues lethal strains of clathrin-deficient Saccharomyces cerevisiae
    • Nelson, K.K. and Lemmon, S.K. (1993) Suppressors of clathrin deficiency: overexpression of ubiquitin rescues lethal strains of clathrin-deficient Saccharomyces cerevisiae. Mol. Cell. Biol., 13, 521-532.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 521-532
    • Nelson, K.K.1    Lemmon, S.K.2
  • 67
    • 0022479114 scopus 로고
    • Cloning of random-sequence oligodeoxynucleotides
    • Oliphant, A.R., Nussbaum, A.L. and Struhl, K. (1986) Cloning of random-sequence oligodeoxynucleotides. Gene, 44, 177-183.
    • (1986) Gene , vol.44 , pp. 177-183
    • Oliphant, A.R.1    Nussbaum, A.L.2    Struhl, K.3
  • 68
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: A family of natural gene fusions
    • Özkaynak, E., Finley, D., Solomon, M.J. and Varshavsky, A. (1987) The yeast ubiquitin genes: a family of natural gene fusions. EMBO J., 6, 1429-1440.
    • (1987) EMBO J. , vol.6 , pp. 1429-1440
    • Özkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 69
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters, J.-M., Walsh, M.J. and Franke, W.W. (1990) An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J., 9, 1757-1767.
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.-M.1    Walsh, M.J.2    Franke, W.W.3
  • 70
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky, E.M. and Fields, S. (1995) Protein-protein interactions: methods for detection and analysis. Microbiol. Rev., 59, 94-123.
    • (1995) Microbiol. Rev. , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 71
    • 0027493180 scopus 로고
    • Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein
    • Pleasure, I.T., Black, M.M. and Keen, J.H. (1993) Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. Nature, 365, 459-462.
    • (1993) Nature , vol.365 , pp. 459-462
    • Pleasure, I.T.1    Black, M.M.2    Keen, J.H.3
  • 72
    • 0028330841 scopus 로고
    • Proteasomes: Multisubunit proteases common to Thermoplasma and eukaryotes
    • Pühler, G., Pitzer, F., Zwickl, P. and Baumeister, W. (1994) Proteasomes: multisubunit proteases common to Thermoplasma and eukaryotes. Syst. Appl. Microbiol., 16, 734-741.
    • (1994) Syst. Appl. Microbiol. , vol.16 , pp. 734-741
    • Pühler, G.1    Pitzer, F.2    Zwickl, P.3    Baumeister, W.4
  • 73
    • 0027414074 scopus 로고
    • The multicatalylic and 26S proteases
    • Rechsteiner, M., Hoffman, L. and Dubiel, W. (1993) The multicatalylic and 26S proteases. J. Biol. Chem., 268, 6065-6068.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6065-6068
    • Rechsteiner, M.1    Hoffman, L.2    Dubiel, W.3
  • 74
    • 0025975312 scopus 로고
    • Cloning genes by complementation in yeast
    • Rose, M.D. and Broach, J.R. (1991) Cloning genes by complementation in yeast. Methods Enzymol., 194, 195-230.
    • (1991) Methods Enzymol. , vol.194 , pp. 195-230
    • Rose, M.D.1    Broach, J.R.2
  • 75
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. (1991) Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol., 194, 281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 76
    • 0030061512 scopus 로고    scopus 로고
    • Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome
    • Rubin, D.M., Coux, O., Wefes, I., Hengartner, C., Young, R.A., Goldberg, A.L. and Finley, D. (1996) Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature, 379, 655-657.
    • (1996) Nature , vol.379 , pp. 655-657
    • Rubin, D.M.1    Coux, O.2    Wefes, I.3    Hengartner, C.4    Young, R.A.5    Goldberg, A.L.6    Finley, D.7
  • 77
    • 0029002717 scopus 로고
    • Synthetic signals for ubiquitin-dependent proteolysis
    • Sadis, S., Atienza, C. and Finley, D. (1995) Synthetic signals for ubiquitin-dependent proteolysis. Mol. Cell. Biol., 15, 4086-4094.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4086-4094
    • Sadis, S.1    Atienza, C.2    Finley, D.3
  • 78
    • 0028071874 scopus 로고
    • Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex
    • Schnall, R., Mannhaupt, G., Stucka, R., Tauer, R., Ehnle, S., Scwarzlose, C., Vetter, I. and Feldmann, H. (1994) Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast, 10, 1141-1155.
    • (1994) Yeast , vol.10 , pp. 1141-1155
    • Schnall, R.1    Mannhaupt, G.2    Stucka, R.3    Tauer, R.4    Ehnle, S.5    Scwarzlose, C.6    Vetter, I.7    Feldmann, H.8
  • 80
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S.cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S.cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 81
    • 0018449422 scopus 로고
    • High-frequency transformation of yeast: Autonomous replication of hybrid DNA molecules
    • Struhl, K., Stinchcomb, D.T., Scherer, S. and Davis, R.W. (1979) High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules. Proc. Natl Acad. Sci. USA, 76, 1035-1039.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1035-1039
    • Struhl, K.1    Stinchcomb, D.T.2    Scherer, S.3    Davis, R.W.4
  • 84
    • 0028343084 scopus 로고
    • The sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new ORFs, including homologues of the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein
    • Tzermia, M., Horaitis, O. and Alexandraki, D. (1994) The sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new ORFs, including homologues of the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein. Yeast, 10, 663-679.
    • (1994) Yeast , vol.10 , pp. 663-679
    • Tzermia, M.1    Horaitis, O.2    Alexandraki, D.3
  • 85
    • 0026068805 scopus 로고
    • Naming a targeting signal
    • Varshavsky, A. (1991) Naming a targeting signal. Cell, 64, 13-15.
    • (1991) Cell , vol.64 , pp. 13-15
    • Varshavsky, A.1
  • 86
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky, A. (1992) The N-end rule. Cell, 69, 725-735.
    • (1992) Cell , vol.69 , pp. 725-735
    • Varshavsky, A.1


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