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Volumn 399, Issue , 2005, Pages 799-822

Heat-inducible degron and the making of conditional mutants

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ARGININE;

EID: 28844506010     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)99052-6     Document Type: Review
Times cited : (42)

References (91)
  • 1
    • 0028082215 scopus 로고
    • Formamide sensitivity: A novel conditional phenotype in yeast
    • Aguilera A. Formamide sensitivity: A novel conditional phenotype in yeast Genetics 136 1994 87 91
    • (1994) Genetics , vol.136 , pp. 87-91
    • Aguilera, A.1
  • 2
    • 0031691307 scopus 로고    scopus 로고
    • Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast
    • Aiba H., Kawaura R., Yamamoto E., Yamada H., Takegawa K., and Mizuno T. Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast J. Bact. 180 1998 5038 5043
    • (1998) J. Bact. , vol.180 , pp. 5038-5043
    • Aiba, H.1    Kawaura, R.2    Yamamoto, E.3    Yamada, H.4    Takegawa, K.5    Mizuno, T.6
  • 3
    • 0031011234 scopus 로고    scopus 로고
    • Regulation of B-type cyclin proteolysis by Cdc28-associated kinases in budding yeast
    • Amon A. Regulation of B-type cyclin proteolysis by Cdc28-associated kinases in budding yeast EMBO J. 16 1997 2693 2702
    • (1997) EMBO J. , vol.16 , pp. 2693-2702
    • Amon, A.1
  • 4
    • 0242331647 scopus 로고    scopus 로고
    • Tackling an essential problem in functional proteomics of Saccharomyces cerevisiae
    • Aparicio O.M. Tackling an essential problem in functional proteomics of Saccharomyces cerevisiae Genome Biol. 4 2003 230
    • (2003) Genome Biol. , vol.4 , pp. 230
    • Aparicio, O.M.1
  • 5
    • 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. In vivo half-life of a protein is a function of its amino-terminal residue Science 234 1986 179 186
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 6
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair A., and Varshavsky A. The degradation signal in a short-lived protein Cell 56 1989 1019 1032
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 7
    • 0029016564 scopus 로고
    • Yeast N-terminal amidase. a new enzyme and component of the N-end rule pathway
    • Baker R.T., and Varshavsky A. Yeast N-terminal amidase. A new enzyme and component of the N-end rule pathway J. Biol. Chem. 270 1995 12065 12074
    • (1995) J. Biol. Chem. , vol.270 , pp. 12065-12074
    • Baker, R.T.1    Varshavsky, A.2
  • 8
    • 0024296519 scopus 로고
    • Hypersensitivity to heavy water: A new conditional phenotype
    • Bartel B., and Varshavsky A. Hypersensitivity to heavy water: A new conditional phenotype Cell 52 1988 935 941
    • (1988) Cell , vol.52 , pp. 935-941
    • Bartel, B.1    Varshavsky, A.2
  • 9
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel B., Wünning I., and Varshavsky A. The recognition component of the N-end rule pathway EMBO J. 9 1990 3179 3189
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wünning, I.2    Varshavsky, A.3
  • 10
  • 11
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke J.D., Trueheart J., Natsoulis G., and Fink G.R. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics Meth. Enzymol. 154 1987 164 175
    • (1987) Meth. Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 12
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: The methionine aminopeptidase and N alpha-acetyl transferase families
    • Bradshaw R.A., Brickey W.W., and Walker K.W. N-terminal processing: The methionine aminopeptidase and N alpha-acetyl transferase families Trends Biochem. Sci. 23 1998 263 267
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 13
    • 0032472322 scopus 로고    scopus 로고
    • The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor
    • Byrd C., Turner G.C., and Varshavsky A. The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor EMBO J. 17 1998 269 277
    • (1998) EMBO J. , vol.17 , pp. 269-277
    • Byrd, C.1    Turner, G.C.2    Varshavsky, A.3
  • 14
    • 0028809873 scopus 로고
    • Multiple functions for the polyA-binding protein in mRNA decapping and deadenylation in yeast
    • Caponigro G., and Parker R. Multiple functions for the polyA-binding protein in mRNA decapping and deadenylation in yeast Genes Dev. 9 1995 2421 2432
    • (1995) Genes Dev. , vol.9 , pp. 2421-2432
    • Caponigro, G.1    Parker, R.2
  • 15
    • 0017639364 scopus 로고
    • A pH-conditional mutant of Escherichia coli
    • Colb M., and Shapiro L. A pH-conditional mutant of Escherichia coli Proc. Natl. Acad. Sci. USA 74 1977 5637 5641
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5637-5641
    • Colb, M.1    Shapiro, L.2
  • 16
    • 0142199959 scopus 로고    scopus 로고
    • Feeding the machine: Mechanisms of proteasome-catalyzed degradation of ubiquitinated proteins
    • Crews C.M. Feeding the machine: Mechanisms of proteasome-catalyzed degradation of ubiquitinated proteins Curr. Op. Chem. Biol. 7 2003 534 539
    • (2003) Curr. Op. Chem. Biol. , vol.7 , pp. 534-539
    • Crews, C.M.1
  • 17
    • 0034725661 scopus 로고    scopus 로고
    • RGS4 is arginylated and degraded by the N-end rule pathway in vitro
    • Davydov I.V., and Varshavsky A. RGS4 is arginylated and degraded by the N-end rule pathway in vitro J. Biol. Chem. 275 2000 22931 22941
    • (2000) J. Biol. Chem. , vol.275 , pp. 22931-22941
    • Davydov, I.V.1    Varshavsky, A.2
  • 19
    • 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. The N-end rule is mediated by the UBC2 (RAD6) ubiquitin-conjugating enzyme Proc. Natl. Acad. Sci. USA 88 1991 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
  • 20
    • 0025941361 scopus 로고
    • An efficient transformation procedure enabling long-term storage of competent cells of various yeast genera
    • Dohmen R.J., Strasser A.W.M., Höner C.B., and Hollenberg C.P. An efficient transformation procedure enabling long-term storage of competent cells of various yeast genera Yeast 7 1991 691 692
    • (1991) Yeast , vol.7 , pp. 691-692
    • Dohmen, R.J.1    Strasser, A.W.M.2    Höner, C.B.3    Hollenberg, C.P.4
  • 21
    • 0028213449 scopus 로고
    • Heat-inducible degron: A method for constructing temperature-sensitive mutants
    • Dohmen R.J., Wu P., and Varshavsky A. Heat-inducible degron: A method for constructing temperature-sensitive mutants Science 263 1994 1273 1276
    • (1994) Science , vol.263 , pp. 1273-1276
    • Dohmen, R.J.1    Wu, P.2    Varshavsky, A.3
  • 22
    • 0037195103 scopus 로고    scopus 로고
    • Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain
    • Du F., Navarro-Garcia F., Xia Z., Tasaki T., and Varshavsky A. Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain Proc. Natl. Acad. Sci. USA 99 2002 14110 14115
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14110-14115
    • Du, F.1    Navarro-garcia, F.2    Xia, Z.3    Tasaki, T.4    Varshavsky, A.5
  • 23
    • 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. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis Nature 338 1989 394 401
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 24
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley D., Özkaynak E., and Varshavsky A. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses Cell 48 1987 1035 1046
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Özkaynak, E.2    Varshavsky, A.3
  • 25
    • 0142250763 scopus 로고    scopus 로고
    • Proteasome degradation: Enter the substrate
    • Förster A., and Hill C.P. Proteasome degradation: Enter the substrate Trends Cell. Biol. 13 2003 550 553
    • (2003) Trends Cell. Biol. , vol.13 , pp. 550-553
    • Förster, A.1    Hill, C.P.2
  • 26
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain M., Dohmen R.J., Levy F., and Varshavsky A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae EMBO J. 15 1996 4884 4899
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 27
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz R.D., and Sugino A. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites Gene 74 1988 527 534
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 28
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz R.D., and Woods R.A. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method Meth. Enzymol. 350 2002 87 96
    • (2002) Meth. Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 29
    • 0031463942 scopus 로고    scopus 로고
    • A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond
    • Gilchrist C.A., Gray D.A., and Baker R.T. A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond J. Biol. Chem. 272 1997 32280 32285
    • (1997) J. Biol. Chem. , vol.272 , pp. 32280-32285
    • Gilchrist, C.A.1    Gray, D.A.2    Baker, R.T.3
  • 30
    • 0029075876 scopus 로고
    • Redirecting the specificity of ubiquitination by modifying ubiquitin-conjugating enzymes
    • Gosink M.M., and Vierstra R.D. Redirecting the specificity of ubiquitination by modifying ubiquitin-conjugating enzymes Proc. Natl. Acad. Sci. USA 92 1995 9117 9121
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9117-9121
    • Gosink, M.M.1    Vierstra, R.D.2
  • 31
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton R.Y. ER-associated degradation in protein quality control and cellular regulation Curr. Op. Cell Biol. 14 2002 476 482
    • (2002) Curr. Op. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 32
    • 0025949923 scopus 로고
    • The signal recognition particle in S. cerevisiae
    • Hann B.C., and Walter P. The signal recognition particle in S. cerevisiae Cell 67 1991 131 144
    • (1991) Cell , vol.67 , pp. 131-144
    • Hann, B.C.1    Walter, P.2
  • 33
    • 0029928690 scopus 로고    scopus 로고
    • Characterization of an essential Orc2p-associated factor that plays a role in DNA replication
    • Hardy C.F. Characterization of an essential Orc2p-associated factor that plays a role in DNA replication Mol. Cell. Biol. 16 1996 1832 1841
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1832-1841
    • Hardy, C.F.1
  • 34
    • 0025963054 scopus 로고
    • Putting the HO gene to work: Practical uses for mating-type switching
    • Herskowitz I., and Jensen R.E. Putting the HO gene to work: Practical uses for mating-type switching Meth. Enzymol. 194 1991 132 146
    • (1991) Meth. Enzymol. , vol.194 , pp. 132-146
    • Herskowitz, I.1    Jensen, R.E.2
  • 35
    • 0023368541 scopus 로고
    • Genetic manipulation of centromere function
    • Hill A., and Bloom K. Genetic manipulation of centromere function Mol. Cell. Biol. 7 1987 2397 2405
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2397-2405
    • Hill, A.1    Bloom, K.2
  • 36
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation Annu. Rev. Genet. 30 1996 405 439
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 37
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems Nature Cell Biol. 2 2000 153 157
    • (2000) Nature Cell Biol. , vol.2 , pp. 153-157
    • Hochstrasser, M.1
  • 38
    • 0003098547 scopus 로고
    • Biochemical genetics of Neurospora
    • Horowitz N.H. Biochemical genetics of Neurospora Adv. Genet. 3 1950 33 71
    • (1950) Adv. Genet. , vol.3 , pp. 33-71
    • Horowitz, N.H.1
  • 39
    • 0023666091 scopus 로고
    • The inducible lac operator-repressor system is functional in mammalian cells
    • Hu M.C., and Davidson N. The inducible lac operator-repressor system is functional in mammalian cells Cell 48 1987 555 566
    • (1987) Cell , vol.48 , pp. 555-566
    • Hu, M.C.1    Davidson, N.2
  • 41
    • 0038680253 scopus 로고    scopus 로고
    • Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo
    • Kanemaki M., Sanchez-Diaz A., Gambus A., and Labib K. Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo Nature 423 2003 720 724
    • (2003) Nature , vol.423 , pp. 720-724
    • Kanemaki, M.1    Sanchez-diaz, A.2    Gambus, A.3    Labib, K.4
  • 42
    • 1842689859 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase
    • Kesti T., McDonald W.H., Yates J.R. Jr., and Wittenberg C. Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase J. Biol. Chem. 279 2004 14245 14255
    • (2004) J. Biol. Chem. , vol.279 , pp. 14245-14255
    • Kesti, T.1    McDonald, W.H.2    Yates Jr., J.R.3    Wittenberg, C.4
  • 43
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova Z., and Wolf D.H. For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection EMBO J. 22 2003 2309 2317
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 46
    • 0035166684 scopus 로고    scopus 로고
    • Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3α) of the N-end rule pathway
    • Kwon Y.T., Xia Z., Davydov I.V., Lecker S.H., and Varshavsky A. Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3α) of the N-end rule pathway Mol. Cell Biol. 21 2001 8007 8021
    • (2001) Mol. Cell Biol. , vol.21 , pp. 8007-8021
    • Kwon, Y.T.1    Xia, Z.2    Davydov, I.V.3    Lecker, S.H.4    Varshavsky, A.5
  • 47
    • 0242664014 scopus 로고    scopus 로고
    • Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway
    • Kwon Y.T., Xia Z.X., An J.Y., Davydov I.V., Seo J.W., Xie Y., and Varshavsky A. Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway Mol. Cell Biol. 23 2003 8255 8271
    • (2003) Mol. Cell Biol. , vol.23 , pp. 8255-8271
    • Kwon, Y.T.1    Xia, Z.X.2    An, J.Y.3    Davydov, I.V.4    Seo, J.W.5    Xie, Y.6    Varshavsky, A.7
  • 48
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • Labib K., Tercero J.A., and Diffley J.F. Uninterrupted MCM2-7 function required for DNA replication fork progression Science 288 2000 1643 1647 (erratum in:
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffley, J.F.3
  • 49
    • 28944447190 scopus 로고    scopus 로고
    • Science 1289 2000 2052 ).
    • (2000) Science , vol.1289 , pp. 2052
  • 50
    • 0026043846 scopus 로고
    • Isolation and characterization of osmosensitive vacuolar mutants of Saccharomyces cerevisiae
    • Latterich M., and Watson M.D. Isolation and characterization of osmosensitive vacuolar mutants of Saccharomyces cerevisiae Mol. Microbiol. 5 1991 2417 2426
    • (1991) Mol. Microbiol. , vol.5 , pp. 2417-2426
    • Latterich, M.1    Watson, M.D.2
  • 51
    • 0033555642 scopus 로고    scopus 로고
    • Analysis of a conditional degradation signal in yeast and mammalian cells
    • Lévy F., Johnston J.A., and Varshavsky A. Analysis of a conditional degradation signal in yeast and mammalian cells Eur. J. Biochem. 259 1999 244 252
    • (1999) Eur. J. Biochem. , vol.259 , pp. 244-252
    • Lévy, F.1    Johnston, J.A.2    Varshavsky, A.3
  • 52
  • 53
    • 0029120399 scopus 로고
    • Micro-homology mediated PCR targeting in Saccharomyces cerevisiae
    • Manivasakam P., Weber S.C., McElver J., and Schiestl R.H. Micro-homology mediated PCR targeting in Saccharomyces cerevisiae Nucl. Acids Res. 23 1995 2799 2800
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2799-2800
    • Manivasakam, P.1    Weber, S.C.2    McElver, J.3    Schiestl, R.H.4
  • 54
    • 0025319081 scopus 로고
    • Temperature-sensitive synthesis of transfer RNAs in vivo in Saccharomyces cerevisiae
    • Marschalek R., Kalpaxis D., and Dingermann T. Temperature-sensitive synthesis of transfer RNAs in vivo in Saccharomyces cerevisiae EMBO J. 9 1990 1253 1258
    • (1990) EMBO J. , vol.9 , pp. 1253-1258
    • Marschalek, R.1    Kalpaxis, D.2    Dingermann, T.3
  • 56
    • 0020120095 scopus 로고
    • Cold-sensitive cell division-cycle mutants of yeast: Isolation, properties, and pseudoreversion studies
    • Moir D., Stewart S.E., Osmond B.C., and Botstein D. Cold-sensitive cell division-cycle mutants of yeast: Isolation, properties, and pseudoreversion studies Genetics 100 1982 547 563
    • (1982) Genetics , vol.100 , pp. 547-563
    • Moir, D.1    Stewart, S.E.2    Osmond, B.C.3    Botstein, D.4
  • 57
    • 0029811986 scopus 로고    scopus 로고
    • TBP-associated factors are not generally required for transcriptional activation in yeast
    • Moqtaderi Z., Bai Y., Poon D., Weil P.A., and Struhl K. TBP-associated factors are not generally required for transcriptional activation in yeast Nature 383 1996 188 191
    • (1996) Nature , vol.383 , pp. 188-191
    • Moqtaderi, Z.1    Bai, Y.2    Poon, D.3    Weil, P.A.4    Struhl, K.5
  • 59
    • 0026558592 scopus 로고
    • A strategy for the generation of conditional mutations by protein destabilization
    • Park E.C., Finley D., and Szostak J.W. A strategy for the generation of conditional mutations by protein destabilization Proc. Natl. Acad. Sci. USA 89 1992 1249 1252
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1249-1252
    • Park, E.C.1    Finley, D.2    Szostak, J.W.3
  • 60
    • 0036276995 scopus 로고    scopus 로고
    • PCR-based engineering of yeast genome
    • Petracek M.E., and Longtine M.S. PCR-based engineering of yeast genome Meth. Enzymol. 350 2002 445 469
    • (2002) Meth. Enzymol. , vol.350 , pp. 445-469
    • Petracek, M.E.1    Longtine, M.S.2
  • 61
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart C. Back to the future with ubiquitin Cell 116 2004 181 190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.1
  • 62
    • 0016588183 scopus 로고
    • Induction, selection, and experimental uses of temperature-sensitive and other conditional mutants in yeast
    • Pringle J.R. Induction, selection, and experimental uses of temperature-sensitive and other conditional mutants in yeast Methods Cell Biol. 12 1975 233 272
    • (1975) Methods Cell Biol. , vol.12 , pp. 233-272
    • Pringle, J.R.1
  • 63
    • 2442575658 scopus 로고    scopus 로고
    • The N-degron approach to create temperature-sensitive mutants in Schizosaccharomyces pombe
    • Rajagopalan S., Liling Z., Liu J., and Balasubramanian M. The N-degron approach to create temperature-sensitive mutants in Schizosaccharomyces pombe Methods Cell Biol. 33 2004 206 212
    • (2004) Methods Cell Biol. , vol.33 , pp. 206-212
    • Rajagopalan, S.1    Liling, Z.2    Liu, J.3    Balasubramanian, M.4
  • 64
    • 0035912183 scopus 로고    scopus 로고
    • Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability
    • Rao H., Uhlmann F., Nasmyth K., and Varshavsky A. Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability Nature 410 2001 955 960
    • (2001) Nature , vol.410 , pp. 955-960
    • Rao, H.1    Uhlmann, F.2    Nasmyth, K.3    Varshavsky, A.4
  • 65
    • 0001730460 scopus 로고    scopus 로고
    • The 26S proteasome
    • J.M. Peters J.R. Harris D. Finley Plenum Press New York
    • Rechsteiner M. The 26S proteasome J.M. Peters J.R. Harris D. Finley "Ubiquitin and the Biology of the Cell" 1998 Plenum Press New York 147 189
    • (1998) "ubiquitin and the Biology of the Cell" , pp. 147-189
    • Rechsteiner, M.1
  • 67
    • 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. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S. cerevisiae Genetics 122 1989 19 27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 68
    • 0021064550 scopus 로고
    • Temperature-inducible amber suppressor: Construction of plasmids containing the Escherichia coli serU- (supD-) gene under control of the bacteriophage lambda pL promoter
    • Steege D.A., and Horabin J.I. Temperature-inducible amber suppressor: Construction of plasmids containing the Escherichia coli serU- (supD-) gene under control of the bacteriophage lambda pL promoter J. Bact. 155 1983 1417 1425
    • (1983) J. Bact. , vol.155 , pp. 1417-1425
    • Steege, D.A.1    Horabin, J.I.2
  • 69
    • 0033231281 scopus 로고    scopus 로고
    • Degradation signals in the lysine-asparagine sequence space
    • Suzuki T., and Varshavsky A. Degradation signals in the lysine-asparagine sequence space EMBO J. 18 1999 6017 6026
    • (1999) EMBO J. , vol.18 , pp. 6017-6026
    • Suzuki, T.1    Varshavsky, A.2
  • 70
    • 0033180153 scopus 로고    scopus 로고
    • Characterization of a temperature-sensitive mutant of a ubiquitin-conjugating enzyme and its use as a heat-inducible degradation signal
    • Tongaonkar P., Beck K., Shinde U.P., and Madura K. Characterization of a temperature-sensitive mutant of a ubiquitin-conjugating enzyme and its use as a heat-inducible degradation signal Anal. Biochem. 272 1999 263 269
    • (1999) Anal. Biochem. , vol.272 , pp. 263-269
    • Tongaonkar, P.1    Beck, K.2    Shinde, U.P.3    Madura, K.4
  • 71
    • 0034213352 scopus 로고    scopus 로고
    • Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway
    • Turner G.C., Du F., and Varshavsky A. Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway Nature 405 2000 579 583
    • (2000) Nature , vol.405 , pp. 579-583
    • Turner, G.C.1    Du, F.2    Varshavsky, A.3
  • 72
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • Turner G.C., and Varshavsky A. Detecting and measuring cotranslational protein degradation in vivo Science 289 2000 2117 2120
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 73
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
    • Valasek L., Mathew A.A., Shin B.S., Nielsen K.H., Szamecz B., and Hinnebusch A.G. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo Genes Dev. 17 2003 786 799
    • (2003) Genes Dev. , vol.17 , pp. 786-799
    • Valasek, L.1    Mathew, A.A.2    Shin, B.S.3    Nielsen, K.H.4    Szamecz, B.5    Hinnebusch, A.G.6
  • 74
    • 0026068805 scopus 로고
    • Naming a targeting signal
    • Varshavsky A. Naming a targeting signal Cell 64 1991 13 15
    • (1991) Cell , vol.64 , pp. 13-15
    • Varshavsky, A.1
  • 75
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky A. The N-end rule: Functions, mysteries, uses Proc. Natl. Acad. Sci. USA 93 1996 12142 12149
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 77
    • 0034581529 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and its descendants
    • Varshavsky A. Ubiquitin fusion technique and its descendants Meth. Enzymol. 327 2000 578 593
    • (2000) Meth. Enzymol. , vol.327 , pp. 578-593
    • Varshavsky, A.1
  • 78
    • 0037719729 scopus 로고    scopus 로고
    • The N-end rule and regulation of apoptosis
    • Varshavsky A. The N-end rule and regulation of apoptosis Nature Cell Biol. 5 2003 373 376
    • (2003) Nature Cell Biol. , vol.5 , pp. 373-376
    • Varshavsky, A.1
  • 79
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R., Oania R., Graumann J., and Deshaies R.J. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system Cell 118 2003 99 110
    • (2003) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 80
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach A., Brachat A., Pohlmann R., and Philippsen P. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae Yeast 10 1994 1793 1808
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 81
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • Wach A.Y. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae Yeast 12 1996 259 265
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.Y.1
  • 82
    • 3543045545 scopus 로고    scopus 로고
    • Role of DNA replication proteins in double-strand break-induced recombination in Saccharomyces cerevisiae
    • Wang X., Ira G., Tercero J.A., Holmes A.M., Diffley J.F., and Haber J.E. Role of DNA replication proteins in double-strand break-induced recombination in Saccharomyces cerevisiae Mol. Cell. Biol. 24 2004 6891 6899
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6891-6899
    • Wang, X.1    Ira, G.2    Tercero, J.A.3    Holmes, A.M.4    Diffley, J.F.5    Haber, J.E.6
  • 83
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson K.D. Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome Semin. Cell Dev. Biol. 11 2000 141 148
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 84
    • 0032481291 scopus 로고    scopus 로고
    • An N-end rule destabilization mutant reveals pre-Golgi requirements for Sec7p in yeast membrane traffic
    • Wolf J., Nicks M., Deitz S., van Tuinen E., and Franzusoff A. An N-end rule destabilization mutant reveals pre-Golgi requirements for Sec7p in yeast membrane traffic Biochem. Biophys. Res. Commun. 243 1998 191 198
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 191-198
    • Wolf, J.1    Nicks, M.2    Deitz, S.3    Van Tuinen, E.4    Franzusoff, A.5
  • 85
    • 0033485869 scopus 로고    scopus 로고
    • The E2-E3 interaction in the N-end rule pathway: The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    • Xie Y., and Varshavsky A. The E2-E3 interaction in the N-end rule pathway: The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain EMBO J. 18 1999 6832 6844
    • (1999) EMBO J. , vol.18 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 86
    • 19544366597 scopus 로고    scopus 로고
    • RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway
    • Yin J., Kwon Y.T., Varshavsky A., and Wang W. RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway Human Mol. Genet. 13 2004 2421 2430
    • (2004) Human Mol. Genet. , vol.13 , pp. 2421-2430
    • Yin, J.1    Kwon, Y.T.2    Varshavsky, A.3    Wang, W.4
  • 87
    • 0024403294 scopus 로고
    • Control of gene expression by artificial introns in Saccharomyces cerevisiae
    • Yoshimatsu T., and Nagawa F. Control of gene expression by artificial introns in Saccharomyces cerevisiae Science 244 1989 1346 1348
    • (1989) Science , vol.244 , pp. 1346-1348
    • Yoshimatsu, T.1    Nagawa, F.2
  • 89
    • 0026034801 scopus 로고
    • Inducer-dependent conditional-lethal mutant animal viruses
    • Zhang Y.F., and Moss B. Inducer-dependent conditional-lethal mutant animal viruses Proc. Natl. Acad. Sci. USA 88 1991 1511 1515
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1511-1515
    • Zhang, Y.F.1    Moss, B.2
  • 90
    • 0033638333 scopus 로고    scopus 로고
    • Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins
    • Zhou P., Bogacki R., McReynolds L., and Howley P.M. Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins Mol. Cell 6 2000 751 756
    • (2000) Mol. Cell , vol.6 , pp. 751-756
    • Zhou, P.1    Bogacki, R.2    McReynolds, L.3    Howley, P.M.4
  • 91
    • 0034076210 scopus 로고    scopus 로고
    • Dis-assembly lines: The proteasome and related ATP-assisted proteases
    • Zwickl P., Baumeister W., and Steven A. Dis-assembly lines: The proteasome and related ATP-assisted proteases Curr. Opin. Struct. Biol. 10 2000 242 250
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 242-250
    • Zwickl, P.1    Baumeister, W.2    Steven, A.3


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