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Volumn 17, Issue 21, 1998, Pages 6144-6154

Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast

Author keywords

ER network; GFP; NE; Yeast 26S proteasome

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEASOME; PROTEIN SUBUNIT;

EID: 0032476655     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.21.6144     Document Type: Article
Times cited : (188)

References (55)
  • 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
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast proteasome catalytic centers and subunit interactions required for active-site formation
    • Arendt, C.S. and Hochstrasser, M. (1997) Identification of the yeast proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl Acad. Sci. USA, 94, 7156-7161.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7156-7161
    • Arendt, C.S.1    Hochstrasser, M.2
  • 4
    • 0031019245 scopus 로고    scopus 로고
    • Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells
    • Belgareh, N. and Doye, V. (1997) Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. J. Cell Biol., 136, 747-759.
    • (1997) J. Cell Biol. , vol.136 , pp. 747-759
    • Belgareh, N.1    Doye, V.2
  • 5
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cuelp in ubiquitination and degradation at the ER surface
    • Biederer, T., Volkwein, C. and Sommer, T. (1997) Role of Cuelp in ubiquitination and degradation at the ER surface. Science, 278, 1806-1808.
    • (1997) Science , vol.278 , pp. 1806-1808
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 6
    • 0030793799 scopus 로고    scopus 로고
    • In vivo dynamics of nuclear pore complexes in yeast
    • Bucci, M. and Wente, S.R. (1997) In vivo dynamics of nuclear pore complexes in yeast. J. Cell Biol., 136, 1185-1199.
    • (1997) J. Cell Biol. , vol.136 , pp. 1185-1199
    • Bucci, M.1    Wente, S.R.2
  • 7
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • Chen, P. and Hochstrasser, M. (1996) Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell, 86, 961-972.
    • (1996) Cell , vol.86 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 8
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F. and Duguet, M. (1995) A 200-amino acid ATPase module in search of a basic function. BioEssays, 17, 639-650.
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 9
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. and Goldberg, A.L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem., 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 11
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα
    • Dai, R.-M., Chen, E., Longo, D.L., Gorbea, C.M. and Li, C.-C.H. (1998) Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα. J. Biol Chem., 273, 3562-3573.
    • (1998) J. Biol Chem. , vol.273 , pp. 3562-3573
    • Dai, R.-M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.-C.H.5
  • 12
    • 0028235965 scopus 로고
    • A 26S protease subunit that binds ubiquitin conjugates
    • Deveraux, Q., Ustrell, C., Pickart, C. and Rechsteiner, M. (1994) A 26S protease subunit that binds ubiquitin conjugates. J. Biol. Chem., 269, 7059-7061.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, C.2    Pickart, C.3    Rechsteiner, M.4
  • 13
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S protease
    • Dubiel, W., Ferrell, K. and Rechsteiner, M. (1995) Subunits of the regulatory complex of the 26S protease. Mol. Biol Rep., 21, 27-34.
    • (1995) Mol. Biol Rep. , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 14
    • 0028265471 scopus 로고
    • PRE3, highly homologous to the human major histo compatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity
    • Enenkel, C., Lehmann, H., Kipper, J., Guckel, R., Hilt, W. and Wolf, D.H. (1994) PRE3, highly homologous to the human major histo compatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity. FEBS Lett., 341, 193-196.
    • (1994) FEBS Lett. , vol.341 , pp. 193-196
    • Enenkel, C.1    Lehmann, H.2    Kipper, J.3    Guckel, R.4    Hilt, W.5    Wolf, D.H.6
  • 15
    • 0030948085 scopus 로고    scopus 로고
    • SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase
    • Fraser, R.A., Rossignol, M., Heard, D.J., Egly, J.M. and Chambon, P. (1997) SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase. J. Biol. Chem., 272, 7122-7126.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7122-7126
    • Fraser, R.A.1    Rossignol, M.2    Heard, D.J.3    Egly, J.M.4    Chambon, P.5
  • 16
    • 0028205144 scopus 로고
    • Mutations in PRG1, a yeast proteasome-related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin gene
    • Friedman, H. and Snyder, M. (1994) Mutations in PRG1, a yeast proteasome-related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin gene. Proc. Natl Acad. Sci. USA, 91, 2031-2035.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2031-2035
    • Friedman, H.1    Snyder, M.2
  • 18
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon, T., Chomsky, O. and Kulka, R.G. (1998) Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J., 17, 2759-2766.
    • (1998) EMBO J. , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 19
    • 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
  • 20
    • 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, N.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, N.D.5
  • 22
    • 0025994140 scopus 로고
    • Guide to Yeast Genetics and Molecular Biology
    • Academic Press Inc., San Diego, CA
    • Guthrie, C. and Fink, G.R. (1991) Guide to Yeast Genetics and Molecular Biology. Methods in Enzymology Vol 194. Academic Press Inc., San Diego, CA.
    • (1991) Methods in Enzymology , vol.194
    • Guthrie, C.1    Fink, G.R.2
  • 23
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R.Y., Gardner, R.G. and Rine, J. (1996) Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol. Cell 7, 2029-2044.
    • (1996) Mol Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 24
    • 0028109918 scopus 로고
    • PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core
    • Heinemeyer, W., Trondle, N., Albrecht, G. and Wolf, D.H. (1994) PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core. Biochemistry, 33, 12229-12237.
    • (1994) Biochemistry , vol.33 , pp. 12229-12237
    • Heinemeyer, W.1    Trondle, N.2    Albrecht, G.3    Wolf, D.H.4
  • 25
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eucaryotic 20S proteasome and their involvement in subunit precursor processing
    • Heinemeyer, W., Fischer, M., Krimmer, T., Stachon, U. and Wolf, D.H. (1997) The active sites of the eucaryotic 20S proteasome and their involvement in subunit precursor processing. J. Biol. Chem., 272, 25200-25209.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-25209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 26
    • 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
  • 27
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M. and Wolf, D.H. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science, 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 28
    • 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
  • 29
    • 0027707469 scopus 로고
    • Studies on the yeast proteasome uncover its basic structural features and multiple in vivo functions
    • Hilt, W., Heinemeyer, W. and Wolf, D.H. (1994) Studies on the yeast proteasome uncover its basic structural features and multiple in vivo functions. Enzyme Protein, 47, 189-201.
    • (1994) Enzyme Protein , vol.47 , pp. 189-201
    • Hilt, W.1    Heinemeyer, W.2    Wolf, D.H.3
  • 30
    • 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
  • 31
    • 0025483120 scopus 로고
    • Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers
    • Jones, J.S. and Prakash, L. (1990) Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers. Yeast, 6, 363-366.
    • (1990) Yeast , vol.6 , pp. 363-366
    • Jones, J.S.1    Prakash, L.2
  • 32
    • 0025633196 scopus 로고
    • Cell-specific accumulation of Drosophila proteasomes (MCP) during early development
    • Klein, U., Gernold, M. and Kloetzel, P.-M. (1990) Cell-specific accumulation of Drosophila proteasomes (MCP) during early development. J. Cell Biol., 111, 2275-2282.
    • (1990) J. Cell Biol. , vol.111 , pp. 2275-2282
    • Klein, U.1    Gernold, M.2    Kloetzel, P.-M.3
  • 33
    • 0029024819 scopus 로고
    • Nin1p, a regulatory subunit of the 26S proteasome, is necessary for the activation of Cdc28p kinase of Saccharomyces cerevisiae
    • Kominami, K. et al. (1995) Nin1p, a regulatory subunit of the 26S proteasome, is necessary for the activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO J., 14, 3105-3115.
    • (1995) EMBO J. , vol.14 , pp. 3105-3115
    • Kominami, K.1
  • 34
    • 17044444591 scopus 로고    scopus 로고
    • Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy 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 multicopy suppressors of nin1-1. Mol. Biol. Cell. 8, 171-187.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 171-187
    • Kominami, K.1
  • 35
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam, Y.A., Xu, W., DeMartino, G.N. and Cohen, R.E. (1997) Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature, 385, 737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    Demartino, G.N.3    Cohen, R.E.4
  • 36
    • 0028365624 scopus 로고
    • The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion
    • Latterich, M. and Schekman, R. (1994) The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion. Cell, 78, 87-98.
    • (1994) Cell , vol.78 , pp. 87-98
    • Latterich, M.1    Schekman, R.2
  • 37
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Fröhlich, K.-U. and Schekman, 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    Schekman, R.3
  • 38
    • 0032549815 scopus 로고    scopus 로고
    • Cotranslational biogenesis of NF-κB p50 by the 26S proteasome
    • Lin, L., DeMartino, G.N. and Greene, W.C. (1998) Cotranslational biogenesis of NF-κB p50 by the 26S proteasome. Cell, 92, 819-828.
    • (1998) Cell , vol.92 , pp. 819-828
    • Lin, L.1    DeMartino, G.N.2    Greene, W.C.3
  • 39
    • 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
  • 41
    • 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, 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, A.3
  • 42
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and Bip to retrograde protein transport for ER degradation
    • Plemper, R.K., Böhmler, S., Bordallo, J., Sommer, T. and Wolf, D.H. (1997) Mutant analysis links the translocon and Bip to retrograde protein transport for ER degradation. Nature, 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Böhmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 44
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian Bip/GRP78 gene
    • Rose, M.D., Misra, L.M. and Vogel, J.P. (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian Bip/GRP78 gene. Cell, 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 45
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout, M.P. and Blobel, G. (1993) Isolation of the yeast nuclear pore complex. J. Cell Biol., 123, 771-783.
    • (1993) J. Cell Biol. , vol.123 , pp. 771-783
    • Rout, M.P.1    Blobel, G.2
  • 46
    • 0030464067 scopus 로고    scopus 로고
    • Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26S proteasome
    • Russell, S.J., Sathyanarayana, U.G. and Johnston, S.A. (1996) Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26S proteasome. J. Biol. Chem., 271, 32810-32817.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32810-32817
    • Russell, S.J.1    Sathyanarayana, U.G.2    Johnston, S.A.3
  • 47
    • 0032571366 scopus 로고    scopus 로고
    • Cotranslational ubiquitination of cystic fibrosis transmembane regulator in vitro
    • Sato, S., Ward, C.L. and Kopito, R.R. (1998) Cotranslational ubiquitination of cystic fibrosis transmembane regulator in vitro. J. Biol. Chem., 273, 7189-7192.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7189-7192
    • Sato, S.1    Ward, C.L.2    Kopito, R.R.3
  • 48
    • 0030481129 scopus 로고    scopus 로고
    • Analysis of mammalian 20S proteasome biogenesis: The maturation of β-subunits is an ordered two-step mechanism involving autocatalysis
    • Schmidtke, G., Kraft, R., Kostka, S., Henklein, R. Frommel, C., Lowe, J., Huber, R., Kloetzel, P.M. and Schmidt, M. (1996) Analysis of mammalian 20S proteasome biogenesis: the maturation of β-subunits is an ordered two-step mechanism involving autocatalysis. EMBO J., 15, 6887-6898.
    • (1996) EMBO J. , vol.15 , pp. 6887-6898
    • Schmidtke, G.1    Kraft, R.2    Kostka, S.3    Henklein, R.4    Frommel, C.5    Lowe, J.6    Huber, R.7    Kloetzel, P.M.8    Schmidt, M.9
  • 49
    • 0030297778 scopus 로고    scopus 로고
    • Characteristics of 26S proteases from fission yeast mutants, which arrest in mitosis
    • Seeger, M., Gordon, C., Ferrell, K. and Dubiel, W. (1996) Characteristics of 26S proteases from fission yeast mutants, which arrest in mitosis. J. Mol. Biol., 263, 423-431.
    • (1996) J. Mol. Biol. , vol.263 , pp. 423-431
    • Seeger, M.1    Gordon, C.2    Ferrell, K.3    Dubiel, W.4
  • 51
    • 0029789918 scopus 로고    scopus 로고
    • Autocatalytic processing of the 20S proteasome
    • Seemueller, E., Lupas, A. and Baumeister, W. (1996) Autocatalytic processing of the 20S proteasome. Nature, 382, 468-471.
    • (1996) Nature , vol.382 , pp. 468-471
    • Seemueller, E.1    Lupas, A.2    Baumeister, W.3
  • 52
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert, W., Futcher, B. and Jentsch, S. (1995) Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature. 373, 78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 53
    • 0028887431 scopus 로고
    • Isolation and characterization of nuclear envelopes from the yeast Saccharomyces
    • Strambio-de-Castillia, C., Blobel, G. and Rout, M.P. (1995) Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. J. Cell Biol., 131, 19-31.
    • (1995) J. Cell Biol. , vol.131 , pp. 19-31
    • Strambio-de-Castillia, C.1    Blobel, G.2    Rout, M.P.3
  • 54
    • 0031105921 scopus 로고    scopus 로고
    • The 26S proteasome: Subunits and functions
    • Tanaka, K. and Tsurumi, C. (1997) The 26S proteasome: subunits and functions. Mol, Biol. Rep., 24, 3-11.
    • (1997) Mol, Biol. Rep. , vol.24 , pp. 3-11
    • Tanaka, K.1    Tsurumi, C.2
  • 55
    • 0030808452 scopus 로고    scopus 로고
    • Mts4, a non-ATPase subunit of the 26S protease in fission yeast is essential for mitosis and interacts directly with the ATPase subunit Mts2
    • Wilkinson, C.R.M., Wallace, M., Seeger, M., Dubiel, W. and Gordon, C. (1997) Mts4, a non-ATPase subunit of the 26S protease in fission yeast is essential for mitosis and interacts directly with the ATPase subunit Mts2. J. Biol. Chem., 272, 25768-25777.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25768-25777
    • Wilkinson, C.R.M.1    Wallace, M.2    Seeger, M.3    Dubiel, W.4    Gordon, C.5


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