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Volumn 162, Issue 3, 2002, Pages 1079-1089

The yeast ubiquitin protease, Ubp3p, promotes protein stability

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; MICROTUBULE ASSOCIATED PROTEIN; PROTEIN STULP; PROTEIN UBP3P; UBIQUITIN PROTEASE; UNCLASSIFIED DRUG; BENOMYL; MYOSIN HEAVY CHAIN; PROTEIN; PROTEINASE; SACCHAROMYCES CEREVISIAE PROTEIN; STU1 PROTEIN, S CEREVISIAE; STU2 PROTEIN, S CEREVISIAE; UBIQUITIN; UBP3 PROTEIN, S CEREVISIAE;

EID: 0036862055     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (22)

References (57)
  • 1
    • 17744372880 scopus 로고    scopus 로고
    • Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts
    • Akhmanova, A., C. C. Hoogenraad, K. Drabek, T. Stepanova, B. Dortland et al., 2001 Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts. Cell 104: 923-935.
    • (2001) Cell , vol.104 , pp. 923-935
    • Akhmanova, A.1    Hoogenraad, C.C.2    Drabek, K.3    Stepanova, T.4    Dortland, B.5
  • 2
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • Amerik, A. Y., S. Swaminathan, B. A. Krantz, K. D. Wilkinson and M. Hochstrasser, 1997 In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16: 4826-4838.
    • (1997) EMBO J. , vol.16 , pp. 4826-4838
    • Amerik, A.Y.1    Swaminathan, S.2    Krantz, B.A.3    Wilkinson, K.D.4    Hochstrasser, M.5
  • 3
    • 0033783007 scopus 로고    scopus 로고
    • Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae
    • Amerik, A. Y., S. J. Li and M. Hochstrasser, 2000 Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biol. Chem. 381: 981-992.
    • (2000) Biol. Chem. , vol.381 , pp. 981-992
    • Amerik, A.Y.1    Li, S.J.2    Hochstrasser, M.3
  • 4
    • 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., J. W. Tobias and A. Varshavsky, 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
  • 6
    • 0031821736 scopus 로고    scopus 로고
    • Isolation of Ubp3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae
    • Baxter, B. K., and E. A. Craig, 1998 Isolation of Ubp3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae. Curr. Genet. 33: 412-419.
    • (1998) Curr. Genet , vol.33 , pp. 412-419
    • Baxter, B.K.1    Craig, E.A.2
  • 7
    • 0025959707 scopus 로고
    • Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae
    • Bender, A., and J. R. Pringle, 1991 Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11: 1295-1305.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1295-1305
    • Bender, A.1    Pringle, J.R.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0029871812 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae
    • Caponigro, G., and R. Parker, 1996 Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae. Microbiol. Rev. 60: 233-249.
    • (1996) Microbiol. Rev. , vol.60 , pp. 233-249
    • Caponigro, G.1    Parker, R.2
  • 10
    • 0033616143 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their diversity and emerging roles
    • Chung, C. H., and S. H. Baek, 1999 Deubiquitinating enzymes: Their diversity and emerging roles. Biochem. Biophys. Res. Commun. 266: 633-640.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 633-640
    • Chung, C.H.1    Baek, S.H.2
  • 11
    • 0032511150 scopus 로고    scopus 로고
    • An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast
    • Ciosk, R., W. Zachariae, C. Michaelis, A. Shevchenko, M. Mann et al., 1998 An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast. Cell 93: 1067-1076.
    • (1998) Cell , vol.93 , pp. 1067-1076
    • Ciosk, R.1    Zachariae, W.2    Michaelis, C.3    Shevchenko, A.4    Mann, M.5
  • 12
    • 0030448251 scopus 로고    scopus 로고
    • Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p
    • Cohen-Fix, O., J. M. Peters, M. W. Kirschner and D. Koshland, 1996 Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p. Genes Dev. 10: 3081-3093.
    • (1996) Genes Dev. , vol.10 , pp. 3081-3093
    • Cohen-Fix, O.1    Peters, J.M.2    Kirschner, M.W.3    Koshland, D.4
  • 13
    • 0031916967 scopus 로고    scopus 로고
    • Mammalian cytosolic chaperonin
    • Cowan, N. J., 1998 Mammalian cytosolic chaperonin. Methods Enzymol. 290: 230-241.
    • (1998) Methods Enzymol. , vol.290 , pp. 230-241
    • Cowan, N.J.1
  • 14
    • 0031760462 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: A new class of biological regulators
    • D'Andrea, A., and D. Pellman, 1998 Deubiquitinating enzymes: A new class of biological regulators. Crit. Rev. Biochem. Mol. Biol. 33: 337-352.
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 337-352
    • D'Andrea, A.1    Pellman, D.2
  • 16
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha- and gamma-tubulin
    • Geissler, S., K. Siegers and E. Schiebel, 1998 A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J. 17: 952-966.
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 17
    • 0034515298 scopus 로고    scopus 로고
    • Getting in and out of the proteasome
    • Glickman, M. H., 2000 Getting in and out of the proteasome. Semin. Cell Dev. Biol. 11: 149-158.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 149-158
    • Glickman, M.H.1
  • 18
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan, B., R. Bowser and P. Novick, 1995 The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128: 1055-1068.
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 20
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • Hansen, W. J., N. J. Cowan and W. J. Welch, 1999 Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J. Cell Biol. 145: 265-277.
    • (1999) J. Cell Biol. , vol.145 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 21
    • 0028342849 scopus 로고
    • The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site
    • Henry, Y., H. Wood, J. P. Morrissey, E. Petfalski, S. Kearsey et al., 1994 The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site. EMBOJ. 13: 2452- 2463.
    • (1994) EMBO J. , vol.13 , pp. 2452-2463
    • Henry, Y.1    Wood, H.2    Morrissey, J.P.3    Petfalski, E.4    Kearsey, S.5
  • 23
    • 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
  • 24
    • 0027214097 scopus 로고
    • Yeast cells lacking 5′-3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure
    • Hsu, C. L., and A. Stevens, 1993 Yeast cells lacking 5′-3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure. Mol. Cell. Biol. 13: 4826-4835.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4826-4835
    • Hsu, C.L.1    Stevens, A.2
  • 25
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Huang, Y., R. T. Baker and J. A. Fischer-Vize, 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
  • 26
    • 0018222124 scopus 로고
    • Flow cytometric determinations of cellular substances in algae, bacteria, moulds and yeasts
    • Hutter, K. J., and H. E. Eipel, 1978 Flow cytometric determinations of cellular substances in algae, bacteria, moulds and yeasts. Antonie Leeuwenhoek 44: 269-282.
    • (1978) Antonie Leeuwenhoek , vol.44 , pp. 269-282
    • Hutter, K.J.1    Eipel, H.E.2
  • 27
    • 0028912794 scopus 로고
    • A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae
    • Interthal, H., C. Bellocq, J. Bahler, V. I. Bashkirov, S. Edelstein et al., 1995 A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in Saccharomyces cerevisiae. EMBO J. 14: 1057-1066.
    • (1995) EMBO J. , vol.14 , pp. 1057-1066
    • Interthal, H.1    Bellocq, C.2    Bahler, J.3    Bashkirov, V.I.4    Edelstein, S.5
  • 28
    • 0030764692 scopus 로고    scopus 로고
    • Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively
    • Johnson, A. W., 1997 Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively. Mol. Cell. Biol. 17: 6122-6130.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6122-6130
    • Johnson, A.W.1
  • 29
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones, E. W., 1991 Three proteolytic systems in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 266: 7963-7966.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 30
    • 0031055137 scopus 로고    scopus 로고
    • APC-mediated proteolysis of Asel and the morphogenesis of the mitotic spindle
    • Juang, Y. L., J. Huang, J. M. Peters, M. E. McLaughlin, C. Y. Tai et al., 1997 APC-mediated proteolysis of Asel and the morphogenesis of the mitotic spindle. Science 275: 1311-1314.
    • (1997) Science , vol.275 , pp. 1311-1314
    • Juang, Y.L.1    Huang, J.2    Peters, J.M.3    McLaughlin, M.E.4    Tai, C.Y.5
  • 31
    • 0025674401 scopus 로고
    • Kem mutations affect nuclear fusion in Saccharomyces cerevisiae
    • Kim, J., P. O. Ljungdahl and G. R. Fink, 1990 Kem mutations affect nuclear fusion in Saccharomyces cerevisiae. Genetics 126: 799-812.
    • (1990) Genetics , vol.126 , pp. 799-812
    • Kim, J.1    Ljungdahl, P.O.2    Fink, G.R.3
  • 33
    • 0035168046 scopus 로고    scopus 로고
    • Control of microtubule dynamics by stu2p is essential for spindle orientation and metaphase chromosome alignment in yeast
    • Kosco, K. A., C. G. Pearson, P. S. Maddox, P. J. Wang, I. R. Adams et al., 2001 Control of microtubule dynamics by stu2p is essential for spindle orientation and metaphase chromosome alignment in yeast. Mol. Biol. Cell 12: 2870-2880.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2870-2880
    • Kosco, K.A.1    Pearson, C.G.2    Maddox, P.S.3    Wang, P.J.4    Adams, I.R.5
  • 34
    • 0026782452 scopus 로고
    • Characterization of the XRN1 gene encoding a 5′→3′ exoribonuclease: Sequence data and analysis of disparate protein and mRNA levels of gene-disrupted yeast cells
    • Larimer, F. W., C. L. Hsu, M. K. Maupin and A. Stevens, 1992 Characterization of the XRN1 gene encoding a 5′→3′ exoribonuclease: Sequence data and analysis of disparate protein and mRNA levels of gene-disrupted yeast cells. Gene 120: 51-57.
    • (1992) Gene , vol.120 , pp. 51-57
    • Larimer, F.W.1    Hsu, C.L.2    Maupin, M.K.3    Stevens, A.4
  • 35
    • 0034679590 scopus 로고    scopus 로고
    • Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organization
    • Lemos, C. L., P. Sampaio, H. Maiato, M. Costa, L. V. Omel'yanchuk et al., 2000 Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organization. EMBO J. 19: 3668-3682.
    • (2000) EMBO J. , vol.19 , pp. 3668-3682
    • Lemos, C.L.1    Sampaio, P.2    Maiato, H.3    Costa, M.4    Omel'yanchuk, L.V.5
  • 36
    • 0001598759 scopus 로고    scopus 로고
    • Cdc20 is essential for the cyclosome-mediated proteolysis of both Pds1 and Clb2 during M phase in budding yeast
    • Lim, H. H., P. Y. Goh and U. Surana, 1998 Cdc20 is essential for the cyclosome-mediated proteolysis of both Pds1 and Clb2 during M phase in budding yeast. Curr. Biol. 8: 231-234.
    • (1998) Curr. Biol. , vol.8 , pp. 231-234
    • Lim, H.H.1    Goh, P.Y.2    Surana, U.3
  • 37
    • 0024404907 scopus 로고
    • Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays
    • Liu, C. C., H. I. Miller, W. J. Kohr and J. I. Silber, 1989 Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays. J. Biol. Chem. 264: 20331-20338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20331-20338
    • Liu, C.C.1    Miller, H.I.2    Kohr, W.J.3    Silber, J.I.4
  • 38
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. ceresisiae
    • Moazed, D., and D. Johnson, 1996 A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. ceresisiae. Cell 86: 667-677.
    • (1996) Cell , vol.86 , pp. 667-677
    • Moazed, D.1    Johnson, D.2
  • 39
    • 0028202495 scopus 로고
    • Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→-3′ digestion of the transcript
    • Muhlrad, D., C. J. Decker and R. Parker, 1994 Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→-3′ digestion of the transcript. Genes Dev. 8: 855-866.
    • (1994) Genes Dev. , vol.8 , pp. 855-866
    • Muhlrad, D.1    Decker, C.J.2    Parker, R.3
  • 40
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: A family of natural gene fusions
    • Ozkaynak, E., D. Finley, M. J. Solomon and A. Varshavsky, 1987 The yeast ubiquitin genes: A family of natural gene fusions. EMBO J. 6: 1429-1439.
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 42
    • 0027427249 scopus 로고
    • The yeast Doa4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa, F. R., and M. Hochstrasser, 1993 The yeast Doa4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 366: 313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 43
    • 0028597069 scopus 로고
    • Stu1, a suppressor of a β-tubulin mutation, encodes a novel and essential component of the yeast mitotic spindle
    • Pasqualone, D., and T. C. Huffaker, 1994 Stu1, a suppressor of a β-tubulin mutation, encodes a novel and essential component of the yeast mitotic spindle. J. Cell Biol. 127: 1973-1984.
    • (1994) J. Cell Biol. , vol.127 , pp. 1973-1984
    • Pasqualone, D.1    Huffaker, T.C.2
  • 44
    • 0031935899 scopus 로고    scopus 로고
    • Processing of the precursors to small nucleolar RNAs and rRNAs requires common components
    • Petfalski, E., T. Dandekar, Y. Henry and D. Tollervey, 1998 Processing of the precursors to small nucleolar RNAs and rRNAs requires common components. Mol. Cell. Biol. 18: 1181-1189.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1181-1189
    • Petfalski, E.1    Dandekar, T.2    Henry, Y.3    Tollervey, D.4
  • 45
    • 0021929906 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides
    • Pickart, C. M., and I. A. Rose, 1985 Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J. Biol. Chem. 260: 7903-7910.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7903-7910
    • Pickart, C.M.1    Rose, I.A.2
  • 46
    • 0020555640 scopus 로고
    • An enzyme with ubiquitin carboxyterminal esterase activity from reticulocytes
    • Rose, I. A., and J. V. Warms, 1983 An enzyme with ubiquitin carboxyterminal esterase activity from reticulocytes. Biochemistry 22: 4234-4237.
    • (1983) Biochemistry , vol.22 , pp. 4234-4237
    • Rose, I.A.1    Warms, J.V.2
  • 48
    • 0035897419 scopus 로고    scopus 로고
    • Stu2 promotes mitotic spindle elongation in anaphase
    • Severin, F., B. Habermann, T. Huffaker and T. Hyman, 2001 Stu2 promotes mitotic spindle elongation in anaphase. J. Cell Biol. 153: 435-442.
    • (2001) J. Cell Biol. , vol.153 , pp. 435-442
    • Severin, F.1    Habermann, B.2    Huffaker, T.3    Hyman, T.4
  • 49
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F., 1991 Getting started with yeast. Methods Enzymol. 194: 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 50
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers, K., T. Waldmann, M. R. Leroux, K. Grein, A. Shevchenko et al., 1999 Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18: 75-84.
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5
  • 51
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter, 1989 A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 52
    • 0032794289 scopus 로고    scopus 로고
    • Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis
    • Solinger, J. A., D. Pascolini and W. D. Heyer, 1999 Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces cerevisiae reveal a specific role in meiosis. Mol. Cell. Biol. 19: 5930-5942.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5930-5942
    • Solinger, J.A.1    Pascolini, D.2    Heyer, W.D.3
  • 53
    • 0025720230 scopus 로고
    • Fragments of the internal transcribed spacer 1 of pre-rRNA accumulate in Saccharomyces cerevisiae lacking 5′-3′ exonuclease 1
    • Stevens, A., C. L. Hsu, K. R. Isham and F. W. Larimer, 1991 Fragments of the internal transcribed spacer 1 of pre-rRNA accumulate in Saccharomyces cerevisiae lacking 5′-3′ exonuclease 1. J. Bacteriol. 173: 7024-7028.
    • (1991) J. Bacteriol. , vol.173 , pp. 7024-7028
    • Stevens, A.1    Hsu, C.L.2    Isham, K.R.3    Larimer, F.W.4
  • 54
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, C. Alberti-Segui, C. Rebischung and P. Philippsen, 1997 Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae. Yeast 13: 1065-1075.
    • (1997) Yeast , vol.13 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Alberti-Segui, C.3    Rebischung, C.4    Philippsen, P.5
  • 55
    • 0030728492 scopus 로고    scopus 로고
    • Stu2p: A microtubule-binding protein that is an essential component of the yeast spindle pole body
    • Wang, P. J., and T. C. Huffaker, 1997 Stu2p: A microtubule-binding protein that is an essential component of the yeast spindle pole body. J. Cell Biol. 139: 1271-1280.
    • (1997) J. Cell Biol. , vol.139 , pp. 1271-1280
    • Wang, P.J.1    Huffaker, T.C.2
  • 56
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T
    • Wilkinson, K. D., V. L. Tashayev, L. B. O'connor, C. N. Larsen, E. Kasperek et al., 1995 Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T. Biochemistry 34: 14535-14546.
    • (1995) Biochemistry , vol.34 , pp. 14535-14546
    • Wilkinson, K.D.1    Tashayev, V.L.2    O'connor, L.B.3    Larsen, C.N.4    Kasperek, E.5
  • 57
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin, H., D. Pruyne, T. C. Huffaker and A. Bretscher, 2000 Myosin V orientates the mitotic spindle in yeast. Nature 406: 1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.