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Volumn 9, Issue 10, 1998, Pages 2917-2931

A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL DNA; GREEN FLUORESCENT PROTEIN; MITOCHONDRIAL DNA; PROTEASOME;

EID: 0031709394     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.10.2917     Document Type: Article
Times cited : (67)

References (58)
  • 1
    • 0027518334 scopus 로고
    • Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control
    • Amsterdam, A., Pitzer, F., and Baumeister, W. (1993). Changes in intracellular localization of proteasomes in immortalized ovarian granulosa cells during mitosis associated with a role in cell cycle control. Proc. Natl. Acad. Sci. USA 90, 99-103.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 99-103
    • Amsterdam, A.1    Pitzer, F.2    Baumeister, W.3
  • 2
    • 0023061489 scopus 로고
    • A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1 beta in Saccharomyces cerevisiae
    • Baldari, C., Murray, J.A., Ghiara, P., Cesareni, G., and Galeotti, C.L. (1987). A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1 beta in Saccharomyces cerevisiae. EMBO J. 6, 229-234.
    • (1987) EMBO J. , vol.6 , pp. 229-234
    • Baldari, C.1    Murray, J.A.2    Ghiara, P.3    Cesareni, G.4    Galeotti, C.L.5
  • 3
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess, S.M., Delannoy, M., and Jensen, R.E. (1994). MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J. Cell Biol. 126, 1375-1391.
    • (1994) J. Cell Biol. , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 4
    • 0027979074 scopus 로고
    • Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue
    • Campbell, C.L., Tanaka, N., White, K.H., and Thorsness, P.E. (1994). Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue. Mol. Biol. Cell 5, 899-905.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 899-905
    • Campbell, C.L.1    Tanaka, N.2    White, K.H.3    Thorsness, P.E.4
  • 5
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W., and Prasher, D.C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 7
    • 0030833816 scopus 로고    scopus 로고
    • Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance
    • Fisk, H.A., and Yaffe, M.P. (1997). Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance. J. Cell Biol. 138, 485-494.
    • (1997) J. Cell Biol. , vol.138 , pp. 485-494
    • Fisk, H.A.1    Yaffe, M.P.2
  • 8
    • 1842405431 scopus 로고    scopus 로고
    • Yeast cycloheximide-resistant crl mutants defective in protein degradation
    • Gerlinger, U.M., Guckel, R., Hoffmann, M., Wolf, D.H., and Hilt, W. (1997). Yeast cycloheximide-resistant crl mutants defective in protein degradation. Mol. Biol. Cell 8, 2487-2477.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2487-12477
    • Gerlinger, U.M.1    Guckel, R.2    Hoffmann, M.3    Wolf, D.H.4    Hilt, W.5
  • 9
    • 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
  • 10
    • 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. (1988). New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 11
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman, M.H., Rubin, D.M., Fried, V.A., and Finley, D. (1998). The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18, 3149-3162.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 12
    • 0027379925 scopus 로고
    • Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit
    • Gordon, C., McGurk, G., Dillon, P., Rosen, C., and Hastie, D. (1993). Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit. Nature 366, 355-357.
    • (1993) Nature , vol.366 , pp. 355-357
    • Gordon, C.1    McGurk, G.2    Dillon, P.3    Rosen, C.4    Hastie, D.5
  • 13
  • 14
    • 0029917506 scopus 로고    scopus 로고
    • The yeast CDC16 and CDC27 genes restrict DNA replication to once per cell cycle
    • Heichman, K.A., and Roberts, J.M. (1996). The yeast CDC16 and CDC27 genes restrict DNA replication to once per cell cycle. Cell 85, 39-48.
    • (1996) Cell , vol.85 , pp. 39-48
    • Heichman, K.A.1    Roberts, J.M.2
  • 15
    • 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
  • 16
    • 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. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 17
    • 0032104227 scopus 로고    scopus 로고
    • The PCI domain: A common theme in three multiprotein complexes
    • Hofmann, K., and Bucher, P. (1998). The PCI domain: a common theme in three multiprotein complexes. Trends Biochem. Sci. 23, 204-205.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 204-205
    • Hofmann, K.1    Bucher, P.2
  • 18
    • 0020529962 scopus 로고
    • Trasformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Trasformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 19
    • 0029036735 scopus 로고
    • Determinants of half-site spacing preferences that distinguish AP-1 and ATF/CREB bZIP domains
    • Kim, J., and Struhl, K. (1995). Determinants of half-site spacing preferences that distinguish AP-1 and ATF/CREB bZIP domains. Nucleic Acids Res. 23, 2531-2537.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2531-2537
    • Kim, J.1    Struhl, K.2
  • 21
    • 0029024819 scopus 로고
    • Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae
    • Kominami, K., et al. (1995). Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO J. 14, 3105-3115.
    • (1995) EMBO J. , vol.14 , pp. 3105-3115
    • Kominami, K.1
  • 22
    • 17044444591 scopus 로고    scopus 로고
    • Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multi-copy suppressors of nin1-1
    • Kominami, K., et al. (1997). Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multi-copy suppressors of nin1-1. Mol. Biol. Cell 8, 171-187.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 171-187
    • Kominami, K.1
  • 23
    • 0028229295 scopus 로고
    • Characterization of the function of the NIN1 gene product of Saccharomyces cerevisiae
    • Kominami, K., and Toh-e, A. (1994). Characterization of the function of the NIN1 gene product of Saccharomyces cerevisiae. Exp. Cell Res. 211, 203-211.
    • (1994) Exp. Cell Res. , vol.211 , pp. 203-211
    • Kominami, K.1    Toh-e, A.2
  • 24
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. (1996). Coiled coils: new structures and new functions. Trends Biochem. Sci. 21, 375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 25
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., VanDyke, M., and Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    VanDyke, M.2    Stock, J.3
  • 26
    • 0030997922 scopus 로고    scopus 로고
    • A proteasome cap subunit required for spindle pole body duplication in yeast
    • McDonald, H.B., and Byers, B. (1997). A proteasome cap subunit required for spindle pole body duplication in yeast. J. Cell Biol. 137, 539-553.
    • (1997) J. Cell Biol. , vol.137 , pp. 539-553
    • McDonald, H.B.1    Byers, B.2
  • 27
    • 0028044610 scopus 로고
    • Regulation of progression through the G1 phase of the cell cycle by the rum1+ gene
    • Moreno, S., and Nurse, P. (1994). Regulation of progression through the G1 phase of the cell cycle by the rum1+ gene. Nature 367, 236-242.
    • (1994) Nature , vol.367 , pp. 236-242
    • Moreno, S.1    Nurse, P.2
  • 28
    • 0029016299 scopus 로고
    • Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae
    • Murakami, Y., et al. (1995). Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae. Nat. Genet. 10, 261-268.
    • (1995) Nat. Genet. , vol.10 , pp. 261-268
    • Murakami, Y.1
  • 29
    • 0029051233 scopus 로고
    • Cyclin ubiquitination: The destructive end of mitosis
    • Murray, A. (1995). Cyclin ubiquitination: the destructive end of mitosis. Cell 81, 149-152.
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.1
  • 30
    • 0027230956 scopus 로고
    • Extragenic suppressor of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
    • Nelson, M.K., Kurihara, T., and Silver, P.A. (1993). Extragenic suppressor of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae. Genetics 134, 159-173.
    • (1993) Genetics , vol.134 , pp. 159-173
    • Nelson, M.K.1    Kurihara, T.2    Silver, P.A.3
  • 31
    • 0029953712 scopus 로고    scopus 로고
    • Green fluorescent protein as marker for gene expression and subcellular localization in budding yeast
    • Niedenthal, R.K., Riles, L., Johnston, M., and Hegemann, J.H. (1996). Green fluorescent protein as marker for gene expression and subcellular localization in budding yeast. Yeast 12, 773-786.
    • (1996) Yeast , vol.12 , pp. 773-786
    • Niedenthal, R.K.1    Riles, L.2    Johnston, M.3    Hegemann, J.H.4
  • 32
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari, J., Marshall, W.F., Straight, A., Murray, A., Sedat, J.W., and Walter, P. (1997). Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8, 1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 33
    • 0025246110 scopus 로고
    • Universal control mechanism regulation onset of M-phase
    • Nurse, P. (1990). Universal control mechanism regulation onset of M-phase. Nature 344, 503-508.
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 34
    • 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 Hochstrasser, M. (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
  • 35
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters, J.M. (1994). Proteasomes: protein degradation machines of the cell. Trends Biochem. Sci. 19, 377-382.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 377-382
    • Peters, J.M.1
  • 36
    • 0028234770 scopus 로고
    • Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters, J.M., Franke, W.W., and Kleinschmidt, J.A. (1994). Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm. J. Biol. Chem. 269, 7709-7718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7709-7718
    • Peters, J.M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 37
    • 0028291932 scopus 로고
    • Proposed roles in protein-protein association and presentation of peptides by MHC Class I receptor
    • Realini, C., Rogers, S.W., and Rechsteiner, M. (1994). Proposed roles in protein-protein association and presentation of peptides by MHC Class I receptor. FEBS Lett. 348, 109-113.
    • (1994) FEBS Lett. , vol.348 , pp. 109-113
    • Realini, C.1    Rogers, S.W.2    Rechsteiner, M.3
  • 38
    • 0027414074 scopus 로고
    • The multicatalytic and 26S proteases
    • Rechsteiner, M., Hoffman, L., and Dubiel, W. (1993). The multicatalytic 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
  • 39
    • 0029803808 scopus 로고    scopus 로고
    • The role of protein degradation in mitochondrial function and biogenesis
    • Rep, M., and Grivell, L.A. (1996). The role of protein degradation in mitochondrial function and biogenesis. Curr. Genet. 30, 367-380.
    • (1996) Curr. Genet. , vol.30 , pp. 367-380
    • Rep, M.1    Grivell, L.A.2
  • 40
    • 0029053890 scopus 로고
    • A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution
    • Rinaldi, T., Bolotin-Fukuhara, M., and Frontali, L. (1995). A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution. Gene 160, 135-136.
    • (1995) Gene , vol.160 , pp. 135-136
    • Rinaldi, T.1    Bolotin-Fukuhara, M.2    Frontali, L.3
  • 41
    • 0028349952 scopus 로고
    • Suppression of a mitochondrial point mutation in a tRNA gene can cast light on the mechanisms of 3′ end-processing
    • Rinaldi, T., Francisci, S., Zennaro, E., Frontali, L., and Bolotin-Fukuhara, M. (1994). Suppression of a mitochondrial point mutation in a tRNA gene can cast light on the mechanisms of 3′ end-processing. Curr. Genet. 25, 451-455.
    • (1994) Curr. Genet. , vol.25 , pp. 451-455
    • Rinaldi, T.1    Francisci, S.2    Zennaro, E.3    Frontali, L.4    Bolotin-Fukuhara, M.5
  • 42
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett, A.J. (1993). Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291, 1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 43
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
    • Rose, M.D., Novick, P., Thomas, J.H., Botstein, D., and Fink, G.R. (1987). A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60, 237-243.
    • (1987) Gene , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 44
    • 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
  • 46
    • 0028898060 scopus 로고
    • +-dependent transcription and is implicated in the maintenance of chromosome structure
    • +-dependent transcription and is implicated in the maintenance of chromosome structure. J. Cell Sci. 108, 569-579.
    • (1995) J. Cell Sci. , vol.108 , pp. 569-579
    • Shimanuki, M.1    Saka, Y.2    Yanagida, M.3    Toda, T.4
  • 47
    • 0029926295 scopus 로고    scopus 로고
    • Coordinating DNA replication to produce one copy of the genome requires genes that act in ubiquitin metabolism
    • Singer, J.D., Manning, B.M., and Formosa, T. (1996). Coordinating DNA replication to produce one copy of the genome requires genes that act in ubiquitin metabolism. Mol. Cell. Biol. 16, 1356-1366.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1356-1366
    • Singer, J.D.1    Manning, B.M.2    Formosa, T.3
  • 48
    • 0028799104 scopus 로고
    • Organelle-cytoskeletal interactions: Actin mutations inhibit meiosis-dependent mitochondrial rearrangements in the budding yeast
    • Smith, M.G., Simon, V.R., O'Sullivan, H., and Pon, L.A. (1995). Organelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangements in the budding yeast. Mol. Biol. Cell 6, 1381-1396.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1381-1396
    • Smith, M.G.1    Simon, V.R.2    O'Sullivan, H.3    Pon, L.A.4
  • 49
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of mitochondrial outer membrane
    • Sogo, L.F., and Yaffe, M.P. (1994). Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of mitochondrial outer membrane. J. Cell Biol. 126, 1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 50
    • 0030728770 scopus 로고    scopus 로고
    • Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26S proteasome subunit
    • Spataro, V., Toda, T., Craig, R., Seeger, M., Dubiel, W., Harris, A.L., and Norbury, C. (1997). Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26S proteasome subunit. J. Biol. Chem. 272, 30470-30475.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30470-30475
    • Spataro, V.1    Toda, T.2    Craig, R.3    Seeger, M.4    Dubiel, W.5    Harris, A.L.6    Norbury, C.7
  • 51
    • 0027477526 scopus 로고
    • Structural analysis based on state-space modeling
    • Stultz, C.M., White, J.V., and Smith, T.F. (1993). Structural analysis based on state-space modeling. Protein Sci. 2, 305-314.
    • (1993) Protein Sci. , vol.2 , pp. 305-314
    • Stultz, C.M.1    White, J.V.2    Smith, T.F.3
  • 53
    • 0027304446 scopus 로고
    • Inactivation of YME1, a member of the ftsH-sec18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae
    • Thorsness, P.E., White, K.H., and Fox, T.D. (1993). Inactivation of YME1, a member of the ftsH-sec18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 5418-5426.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5418-5426
    • Thorsness, P.E.1    White, K.H.2    Fox, T.D.3
  • 55
    • 0028181528 scopus 로고
    • Protein classification by stochastic modeling on optimal filtering of amino-acid sequences
    • White, J.V., Stultz, C.M., and Smith, T.F. (1994). Protein classification by stochastic modeling on optimal filtering of amino-acid sequences. Math. Biosci. 119, 35-75.
    • (1994) Math. Biosci. , vol.119 , pp. 35-75
    • White, J.V.1    Stultz, C.M.2    Smith, T.F.3
  • 56
    • 0028794516 scopus 로고
    • Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C
    • Winston, F., Dollard, C., and Ricupero-Hovasse, S.L. (1995). Construction of a set of convenient Saccharomyces cerevisiae strains that are isogenic to S288C. Yeast 11, 53-55.
    • (1995) Yeast , vol.11 , pp. 53-55
    • Winston, F.1    Dollard, C.2    Ricupero-Hovasse, S.L.3
  • 57
    • 8944250216 scopus 로고    scopus 로고
    • cDNA cloning of p112, the largest regulatory subunit of the human 26S proteasome, and functional analysis of its yeast homologue, Sen3p
    • Yokota, K., et al. (1996). cDNA cloning of p112, the largest regulatory subunit of the human 26S proteasome, and functional analysis of its yeast homologue, Sen3p. Mol. Biol. Cell 7, 853-870.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 853-870
    • Yokota, K.1


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