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Volumn 5, Issue 3, 2003, Pages 151-163

Archaeal proteasomes: Potential in metabolic engineering

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEA;

EID: 0141684667     PISSN: 10967176     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-7176(03)00030-2     Document Type: Short Survey
Times cited : (4)

References (169)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian, T.N., Kisselev, A.F., Goldberg, A.L., 1997. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272, 1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 3
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
    • Arendt, C.S., Hochstrasser, M., 1997. Identification of the yeast 20S 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
    • 0033168717 scopus 로고    scopus 로고
    • Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly
    • Arendt, C.S., Hochstrasser, M., 1999. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J. 18, 3575-3585.
    • (1999) EMBO J. , vol.18 , pp. 3575-3585
    • Arendt, C.S.1    Hochstrasser, M.2
  • 5
    • 0028287522 scopus 로고
    • Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex
    • Arribas, J., Arizti, P., Castaño, J.G., 1994. Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex. J. Biol. Chem. 269, 12858-12864.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12858-12864
    • Arribas, J.1    Arizti, P.2    Castaño, J.G.3
  • 6
    • 0031038205 scopus 로고    scopus 로고
    • Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus
    • Bauer, M.W., Halio, S.B., Kelly, R.M., 1997. Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 63, 1160-1164.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1160-1164
    • Bauer, M.W.1    Halio, S.B.2    Kelly, R.M.3
  • 7
    • 0033769733 scopus 로고    scopus 로고
    • PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
    • Benaroudj, N., Goldberg, A.L., 2000. PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone. Nat. Cell Biol. 2, 833-839.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 833-839
    • Benaroudj, N.1    Goldberg, A.L.2
  • 8
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • Benaroudj, N., Zwickl, P., Seemuller, E., Baumeister, W., Goldberg, A.L., 2003. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11, 69-78.
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemuller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 9
    • 0030925223 scopus 로고    scopus 로고
    • Crystal structure of heat shock locus V (HslV) from Escherichia coli
    • Bochtler, M., Ditzel, L., Groll, M., Huber, R., 1997. Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proc. Natl. Acad. Sci. USA 94, 6070-6074.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6070-6074
    • Bochtler, M.1    Ditzel, L.2    Groll, M.3    Huber, R.4
  • 12
    • 0031609083 scopus 로고    scopus 로고
    • Function of bacterial propeptides
    • Braun, P., Tommassen, J., 1998. Function of bacterial propeptides. Trends Microbiol. 6, 6-8.
    • (1998) Trends Microbiol. , vol.6 , pp. 6-8
    • Braun, P.1    Tommassen, J.2
  • 14
    • 0027708384 scopus 로고
    • Catalytic components of the bovine pituitary multicatalytic proteinase complex (proteasome)
    • Cardozo, C., 1993. Catalytic components of the bovine pituitary multicatalytic proteinase complex (proteasome). Enzyme Protein 47, 296-305.
    • (1993) Enzyme Protein , vol.47 , pp. 296-305
    • Cardozo, C.1
  • 15
    • 0036942289 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway
    • Cardozo, C., Michaud, C., 2002. Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway. Arch. Biochem. Biophys. 408, 103-110.
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 103-110
    • Cardozo, C.1    Michaud, C.2
  • 16
    • 0033609453 scopus 로고    scopus 로고
    • Components of the bovine pituitary multicatalytic proteinase complex (proteasome) cleaving bonds after hydrophobic residues
    • Cardozo, C., Michaud, C., Orlowski, M., 1999. Components of the bovine pituitary multicatalytic proteinase complex (proteasome) cleaving bonds after hydrophobic residues. Biochemistry 38, 9768-9777.
    • (1999) Biochemistry , vol.38 , pp. 9768-9777
    • Cardozo, C.1    Michaud, C.2    Orlowski, M.3
  • 17
    • 0028999726 scopus 로고
    • Biogenesis, structure, and function of the yeast 20S proteasome
    • Chen, P., Hochstrasser, M., 1995. Biogenesis, structure, and function of the yeast 20S proteasome. EMBO J. 14, 2620-2630.
    • (1995) EMBO J. , vol.14 , pp. 2620-2630
    • Chen, P.1    Hochstrasser, M.2
  • 18
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • Chen, P., 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
  • 19
    • 0035067587 scopus 로고    scopus 로고
    • Antizyme, a mediator of ubiquitin-independent proteasomal degradation
    • Coffino, P., 2001. Antizyme, a mediator of ubiquitin-independent proteasomal degradation. Biochimie 83, 319-323.
    • (2001) Biochimie , vol.83 , pp. 319-323
    • Coffino, P.1
  • 20
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90
    • Conconi, M., Szweda, L.I., Levine, R.L., Stadtman, E.R., Friguet, B., 1996. Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90. Arch. Biochem. Biophys. 331, 232-240.
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5
  • 22
    • 0028593502 scopus 로고
    • Phylogenic relationships of the amino acid sequences of prosome (proteasome, MCP) subunits
    • Coux, O., Nothwang, H.G., Pereira, I.S., Targa, F.R., Bey, F., Scherrer, K., 1994. Phylogenic relationships of the amino acid sequences of prosome (proteasome, MCP) subunits. Mol. Gen. Genet. 245, 769-780.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 769-780
    • Coux, O.1    Nothwang, H.G.2    Pereira, I.S.3    Targa, F.R.4    Bey, F.5    Scherrer, K.6
  • 23
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., 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
  • 24
    • 0024972956 scopus 로고
    • The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria
    • Dahlmann, B., Kopp, F., Kuehn, L., Niedel, B., Pfeifer, G., Hegerl, R., Baumeister, W., 1989. The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Lett. 251, 125-131.
    • (1989) FEBS Lett. , vol.251 , pp. 125-131
    • Dahlmann, B.1    Kopp, F.2    Kuehn, L.3    Niedel, B.4    Pfeifer, G.5    Hegerl, R.6    Baumeister, W.7
  • 25
    • 0026746240 scopus 로고
    • Biochemical properties of the proteasome from Thermoplasma acidophilum
    • Dahlmann, B., Kuehn, L., Grziwa, A., Zwickl, P., Baumeister, W., 1992. Biochemical properties of the proteasome from Thermoplasma acidophilum. Eur. J. Biochem. 208, 789-797.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 789-797
    • Dahlmann, B.1    Kuehn, L.2    Grziwa, A.3    Zwickl, P.4    Baumeister, W.5
  • 26
  • 27
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai, R.M., Li, C.C., 2001. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3, 740-744.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 28
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα
    • Dai, R.M., Chen, E., Longo, D.L., Gorbea, C.M., Li, C.C.H., Li, C.C., 1998. Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S 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    Li, C.C.6
  • 30
    • 0033083967 scopus 로고    scopus 로고
    • Proteasomes and other self-compartmentalizing proteases in prokaryotes
    • De Mot, R., Nagy, I., Walz, J., Baumeister, W., 1999. Proteasomes and other self-compartmentalizing proteases in prokaryotes. Trends Microbiol. 7, 88-92.
    • (1999) Trends Microbiol. , vol.7 , pp. 88-92
    • De Mot, R.1    Nagy, I.2    Walz, J.3    Baumeister, W.4
  • 32
    • 0032569036 scopus 로고    scopus 로고
    • Conformational constraints for protein self-cleavage in the proteasome
    • Ditzel, L., Huber, R., Mann, K., Heinemeyer, W., Wolf, D.H., Groll, M., 1998. Conformational constraints for protein self-cleavage in the proteasome. J. Mol. Biol. 279, 1187-1191.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1187-1191
    • Ditzel, L.1    Huber, R.2    Mann, K.3    Heinemeyer, W.4    Wolf, D.H.5    Groll, M.6
  • 33
    • 0026660330 scopus 로고
    • VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation
    • Egerton, M., Ashe, O.R., Chen, D., Druker, B.J., Burgess, W.H., Samelson, L.E., 1992. VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO J. 11, 3533-3540.
    • (1992) EMBO J. , vol.11 , pp. 3533-3540
    • Egerton, M.1    Ashe, O.R.2    Chen, D.3    Druker, B.J.4    Burgess, W.H.5    Samelson, L.E.6
  • 34
    • 0030982044 scopus 로고    scopus 로고
    • Screening for molecules interacting with proteasomes in Thermoplasma acidophilum
    • Ehlers, C., Kopp, F., Dahlmann, B., 1997. Screening for molecules interacting with proteasomes in Thermoplasma acidophilum. Biol. Chem. 378, 249-253.
    • (1997) Biol. Chem. , vol.378 , pp. 249-253
    • Ehlers, C.1    Kopp, F.2    Dahlmann, B.3
  • 35
    • 0034647551 scopus 로고    scopus 로고
    • The human 26S and 20S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate
    • Emmerich, N.P., Nussbaum, A.K., Stevanovic, S., Priemer, M., Toes, R.E., Rammensee, H.G., Schild, H., 2000. The human 26S and 20S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate. J. Biol. Chem. 275, 21140-21148.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21140-21148
    • Emmerich, N.P.1    Nussbaum, A.K.2    Stevanovic, S.3    Priemer, M.4    Toes, R.E.5    Rammensee, H.G.6    Schild, H.7
  • 36
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., Schreiber, S.L., 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 37
    • 0033976299 scopus 로고    scopus 로고
    • Regulatory subunit interactions of the 26S proteasome, a complex problem
    • Ferrell, K., Wilkinson, C.R., Dubiel, W., Gordon, C., 2000. Regulatory subunit interactions of the 26S proteasome, a complex problem. Trends Biochem. Sci. 25, 83-88.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 83-88
    • Ferrell, K.1    Wilkinson, C.R.2    Dubiel, W.3    Gordon, C.4
  • 39
    • 0012200970 scopus 로고    scopus 로고
    • Characterization of the proteasome from the extremely halophiliic archaeon Haloarcula marismortui
    • Franzetti, B., Schoehn, G., Garcia, D., Ruigrok, R.W.H., Zaccai, G., 2002. Characterization of the proteasome from the extremely halophiliic archaeon Haloarcula marismortui. Archaea 1, 53-61.
    • (2002) Archaea , vol.1 , pp. 53-61
    • Franzetti, B.1    Schoehn, G.2    Garcia, D.3    Ruigrok, R.W.H.4    Zaccai, G.5
  • 40
    • 0028178515 scopus 로고
    • 20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins take place in 13-16 S preproteasome complexes
    • Frentzel, S., Pesold-Hurt, B., Seelig, A., Kloetzel, P.-M., Kloetzel, P.M., 1994. 20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins take place in 13-16 S preproteasome complexes. J. Mol. Biol. 236, 975-981.
    • (1994) J. Mol. Biol. , vol.236 , pp. 975-981
    • Frentzel, S.1    Pesold-Hurt, B.2    Seelig, A.3    Kloetzel, P.-M.4    Kloetzel, P.M.5
  • 41
    • 0028881024 scopus 로고
    • The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM
    • Fröhlich, K.U., Fries, H.W., Peters, J.M., Mecke, D., 1995. The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM. Biochem. Biophys. Acta 1253, 25-32.
    • (1995) Biochem. Biophys. Acta , vol.1253 , pp. 25-32
    • Fröhlich, K.U.1    Fries, H.W.2    Peters, J.M.3    Mecke, D.4
  • 42
    • 0031779610 scopus 로고    scopus 로고
    • Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana
    • Fu, H., Doelling, J.H., Arendt, C.S., Hochstrasser, M., Vierstra, R.D., 1998a. Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana. Genetics 149, 677-692.
    • (1998) Genetics , vol.149 , pp. 677-692
    • Fu, H.1    Doelling, J.H.2    Arendt, C.S.3    Hochstrasser, M.4    Vierstra, R.D.5
  • 43
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcbl
    • Fu, H., Sadis, S., Rubin, D.M., Glickman, M., van Nocker, S., Finley, D., Vierstra, R.D., 1998b. Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcbl. J. Biol. Chem. 273, 1970-1981.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1970-1981
    • Fu, H.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 45
    • 0032548779 scopus 로고    scopus 로고
    • Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae
    • Fujimuro, M., Tanaka, K., Yokosawa, H., Toh-e, A., 1998b. Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 423, 149-154.
    • (1998) FEBS Lett. , vol.423 , pp. 149-154
    • Fujimuro, M.1    Tanaka, K.2    Yokosawa, H.3    Toh-e, A.4
  • 47
    • 0030950435 scopus 로고    scopus 로고
    • The human α-type proteasomal subunit HsC8 forms a double ringlike structure but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26
    • Gerards, W.L., Enzlin, J., Haner, M., Hendriks, I.L., Aebi, U., Bloemendal, H., Boelens, W., 1997. The human α-type proteasomal subunit HsC8 forms a double ringlike structure but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26. J. Biol. Chem. 272, 10080-10086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10080-10086
    • Gerards, W.L.1    Enzlin, J.2    Haner, M.3    Hendriks, I.L.4    Aebi, U.5    Bloemendal, H.6    Boelens, W.7
  • 48
    • 0032498229 scopus 로고    scopus 로고
    • The human proteasomal subunit HsC8 induces ring formation of other α-type subunits
    • Gerards, W.L., de Jong, W.W., Bloemendal, H., Boelens, W., 1998. The human proteasomal subunit HsC8 induces ring formation of other α-type subunits. J. Mol. Biol. 275, 113-121.
    • (1998) J. Mol. Biol. , vol.275 , pp. 113-121
    • Gerards, W.L.1    De Jong, W.W.2    Bloemendal, H.3    Boelens, W.4
  • 49
    • 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., Varshavsky, A., 1996. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 15, 4884-4899.
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 51
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9- signalosome and eIF3
    • Glickman, M.H., Rubin, D.M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V.A., Finley, D., 1998. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9- signalosome and eIF3. Cell 94, 615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 52
    • 0032825282 scopus 로고    scopus 로고
    • The Janus face of the archaeal Cdc48/p97 homologue VAT: Protein folding versus unfolding
    • Golbik, R., Lupas, A.N., Koretke, K.K., Baumeister, W., Peters, J., 1999. The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding. Biol. Chem. 380, 1049-1062.
    • (1999) Biol. Chem. , vol.380 , pp. 1049-1062
    • Golbik, R.1    Lupas, A.N.2    Koretke, K.K.3    Baumeister, W.4    Peters, J.5
  • 55
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
    • Groll, M., Heinemeyer, W., Jäger, S., Ullrich, T., Bochtler, M., Wolf, D.H., Huber, R., 1999. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc. Natl. Acad. Sci. USA 96, 10976-10983.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10976-10983
    • Groll, M.1    Heinemeyer, W.2    Jäger, S.3    Ullrich, T.4    Bochtler, M.5    Wolf, D.H.6    Huber, R.7
  • 57
    • 0025886124 scopus 로고
    • Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy
    • Grziwa, A., Baumeister, W., Dahlmann, B., Kopp, F., 1991. Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy. FEBS Lett. 290, 186-190.
    • (1991) FEBS Lett. , vol.290 , pp. 186-190
    • Grziwa, A.1    Baumeister, W.2    Dahlmann, B.3    Kopp, F.4
  • 58
    • 0028260610 scopus 로고
    • 240-kDa proteasome inhibitor (CF-2) is identical to δ -aminolevulinic acid dehydratase
    • Guo, G.G., Gu, M., Etlinger, J.D., 1994. 240-kDa proteasome inhibitor (CF-2) is identical to δ-aminolevulinic acid dehydratase. J. Biol. Chem. 269, 12399-12402.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12399-12402
    • Guo, G.G.1    Gu, M.2    Etlinger, J.D.3
  • 59
    • 0024497473 scopus 로고
    • The Drosophila proteasome undergoes changes in its subunit pattern during development
    • Haass, C., Kloetzel, P.-M., 1989. The Drosophila proteasome undergoes changes in its subunit pattern during development. Exp. Cell Res. 180, 243-252.
    • (1989) Exp. Cell Res. , vol.180 , pp. 243-252
    • Haass, C.1    Kloetzel, P.-M.2
  • 60
    • 0035242489 scopus 로고    scopus 로고
    • Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking
    • Hartmann-Petersen, R., Tanaka, K., Hendil, K.B., 2001. Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. Arch. Biochem. Biophys. 386, 89-94.
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 89-94
    • Hartmann-Petersen, R.1    Tanaka, K.2    Hendil, K.B.3
  • 61
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer, W., Gruhler, A., Möhrle, V., Mahé, Y., Wolf, D.H., 1993. PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268, 5115-5120.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Möhrle, V.3    Mahé, Y.4    Wolf, D.H.5
  • 62
    • 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., 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
  • 63
    • 0032526238 scopus 로고    scopus 로고
    • Simultaneous binding of PA28 and PA700 activators to 20S proteasomes
    • Hendil, K.B., Khan, S., Tanaka, K., 1998. Simultaneous binding of PA28 and PA700 activators to 20S proteasomes. Biochem. J. 332, 749-754.
    • (1998) Biochem. J. , vol.332 , pp. 749-754
    • Hendil, K.B.1    Khan, S.2    Tanaka, K.3
  • 65
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W., 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
  • 66
    • 0034237327 scopus 로고    scopus 로고
    • Intracellular targeting of the proteasome
    • Hirsch, C., Ploegh, H.L., 2000. Intracellular targeting of the proteasome. Trends Cell Biol. 10, 268-272.
    • (2000) Trends Cell Biol. , vol.10 , pp. 268-272
    • Hirsch, C.1    Ploegh, H.L.2
  • 68
    • 0036177305 scopus 로고    scopus 로고
    • Electrophoretic analysis of phosphorylation of the yeast 20S proteasome
    • Iwafune, Y., Kawasaki, H., Hirano, H., 2002. Electrophoretic analysis of phosphorylation of the yeast 20S proteasome. Electrophoresis 23, 329-338.
    • (2002) Electrophoresis , vol.23 , pp. 329-338
    • Iwafune, Y.1    Kawasaki, H.2    Hirano, H.3
  • 69
    • 0037214430 scopus 로고    scopus 로고
    • Subunit topology of two 20S proteasomes from Haloferax volcanii
    • Kaczowka, S.J., Maupin-Furlow, J.A., 2003. Subunit topology of two 20S proteasomes from Haloferax volcanii. J. Bacteriol. 185, 165-174.
    • (2003) J. Bacteriol. , vol.185 , pp. 165-174
    • Kaczowka, S.J.1    Maupin-Furlow, J.A.2
  • 70
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata, K., Inagawa, T., Wilkinson, A.J., Tatsuta, T., Ogura, T., 1999. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274, 26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 72
  • 73
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev, A.F., Akopian, T.N., Goldberg, A.L., 1998. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273, 1982-1989.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 74
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev, A.F., Akopian, T.N., Castillo, V., Goldberg, A.L., 1999a. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell 4, 395-402.
    • (1999) Mol. Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 75
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev, A.F., Akopian, T.N., Woo, K.M., Goldberg, A.L., 1999b. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation. J. Biol. Chem. 274, 3363-3371.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 76
    • 0034685889 scopus 로고    scopus 로고
    • Why does threonine, and not serine, function as the active site nucleophile in proteasomes?
    • Kisselev, A.F., Songyang, Z., Goldberg, A.L., 2000. Why does threonine, and not serine, function as the active site nucleophile in proteasomes? J. Biol. Chem. 275, 14831-14837.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14831-14837
    • Kisselev, A.F.1    Songyang, Z.2    Goldberg, A.L.3
  • 77
    • 0037151122 scopus 로고    scopus 로고
    • Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20S proteasomes. Evidence for peptide-induced channel opening in the α-rings
    • Kisselev, A.F., Kaganovich, D., Goldberg, A.L., 2002. Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20S proteasomes. Evidence for peptide-induced channel opening in the α-rings. J. Biol. Chem. 277, 22260-22270.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22260-22270
    • Kisselev, A.F.1    Kaganovich, D.2    Goldberg, A.L.3
  • 78
    • 0033614454 scopus 로고    scopus 로고
    • Species variation in ATP-dependent protein degradation: Protease profiles differ between mycobacteria and protease functions differ between Mycobacterium smegmatis and Escherichia coli
    • Knipfer, N., Seth, A., Roudiak, S.G., Shrader, T.E., 1999. Species variation in ATP-dependent protein degradation: protease profiles differ between mycobacteria and protease functions differ between Mycobacterium smegmatis and Escherichia coli. Gene 231, 95-104.
    • (1999) Gene , vol.231 , pp. 95-104
    • Knipfer, N.1    Seth, A.2    Roudiak, S.G.3    Shrader, T.E.4
  • 80
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Kohler, A., Cascio, P., Leggett, D.S., Woo, K.M., Goldberg, A.L., Finley, D., 2001b. The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7, 1143-1152.
    • (2001) Mol. Cell , vol.7 , pp. 1143-1152
    • Kohler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 82
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam, Y.A., Lawson, T.G., Velayutham, M., Zweier, J.L., Pickart, C.M., 2002. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416, 763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 83
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M., Matouschek, A., 2001. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7, 627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 84
    • 0037144567 scopus 로고    scopus 로고
    • Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel
    • Lee, C., Prakash, S., Matouschek, A., 2002. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. J. Biol. Chem. 277, 34760-34765.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34760-34765
    • Lee, C.1    Prakash, S.2    Matouschek, A.3
  • 85
    • 0036296150 scopus 로고    scopus 로고
    • 20S proteasomes are imported as precursor complexes into the nucleus of yeast
    • Lehmann, A., Janek, K., Braun, B., Kloetzel, P.M., Enenkel, C., 2002. 20S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol. 317, 401-413.
    • (2002) J. Mol. Biol. , vol.317 , pp. 401-413
    • Lehmann, A.1    Janek, K.2    Braun, B.3    Kloetzel, P.M.4    Enenkel, C.5
  • 86
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C.U., Steinmann, D., Whiteheart, S.W., Weis, W.I., 1998. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 88
    • 0037022891 scopus 로고    scopus 로고
    • ER dislocation: Cdc48p/p97 gets into the AAAct
    • Lord, J.M., Ceriotti, A., Roberts, L.M., 2002. ER dislocation: Cdc48p/ p97 gets into the AAAct. Curr. Biol. 12, R182-R184.
    • (2002) Curr. Biol. , vol.12
    • Lord, J.M.1    Ceriotti, A.2    Roberts, L.M.3
  • 89
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., Huber, R., 1995. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268, 533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 90
    • 0028109452 scopus 로고
    • Predicted secondary structure of the 20S proteasome and model structure of the putative peptide channel
    • Lupas, A., Koster, A.J., Walz, J., Baumeister, W., 1994. Predicted secondary structure of the 20S proteasome and model structure of the putative peptide channel. FEBS Lett. 354, 45-49.
    • (1994) FEBS Lett. , vol.354 , pp. 45-49
    • Lupas, A.1    Koster, A.J.2    Walz, J.3    Baumeister, W.4
  • 91
    • 0036899899 scopus 로고    scopus 로고
    • Expression of proteasome subunit isoforms during spermatogenesis in Drosophila melanogaster
    • Ma, J., Katz, E., Belote, J.M., 2001. Expression of proteasome subunit isoforms during spermatogenesis in Drosophila melanogaster. Insect Mol. Biol. 11, 627-639.
    • (2001) Insect Mol. Biol. , vol.11 , pp. 627-639
    • Ma, J.1    Katz, E.2    Belote, J.M.3
  • 92
    • 0028810102 scopus 로고
    • A proteasome from the methanogenic archaeon Methanosarcina thermophila
    • Maupin-Furlow, J.A., Ferry, J.G., 1995. A proteasome from the methanogenic archaeon Methanosarcina thermophila. J. Biol. Chem. 270, 28617-28622.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28617-28622
    • Maupin-Furlow, J.A.1    Ferry, J.G.2
  • 93
    • 0031918337 scopus 로고    scopus 로고
    • Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila
    • Maupin-Furlow, J.A., Aldrich, H.C., Ferry, J.G., 1998. Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila. J. Bacteriol. 180, 1480-1487.
    • (1998) J. Bacteriol. , vol.180 , pp. 1480-1487
    • Maupin-Furlow, J.A.1    Aldrich, H.C.2    Ferry, J.G.3
  • 97
    • 0024600924 scopus 로고
    • The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes
    • McGuire, M.J., McCullough, M.L., Croall, D.E., DeMartino, G.N., 1989. The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes. Biochem. Biophys. Acta 995, 181-186.
    • (1989) Biochem. Biophys. Acta , vol.995 , pp. 181-186
    • McGuire, M.J.1    McCullough, M.L.2    Croall, D.E.3    DeMartino, G.N.4
  • 98
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian Ufdl and Np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer, H.H., Shorter, J.G., Seemann, J., Pappin, D., Warren, G., 2000. A complex of mammalian Ufdl and Np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19, 2181-2192.
    • (2000) EMBO J. , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 99
    • 0030462757 scopus 로고    scopus 로고
    • Identifcation and characterization of HslV and HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli
    • Missiakas, D., Schwager, F., Betton, J.-M., Georgopoulos, C., Raina, S., Betton, J.M., 1996. Identifcation and characterization of HslV and HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15, 6899-6909.
    • (1996) EMBO J. , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.-M.3    Georgopoulos, C.4    Raina, S.5    Betton, J.M.6
  • 100
    • 0030025882 scopus 로고    scopus 로고
    • Differential effects of bovine PA28 on six peptidase activities of the lobster muscle proteasome (multicatalytic proteinase)
    • Mykles, D.L., 1996. Differential effects of bovine PA28 on six peptidase activities of the lobster muscle proteasome (multicatalytic proteinase). Arch. Biochem. Biophys. 325, 77-81.
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 77-81
    • Mykles, D.L.1
  • 101
    • 0035099055 scopus 로고    scopus 로고
    • Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
    • Myung, J., Kim, K.B., Lindsten, K., Dantuma, N.P., Crews, C.M., 2001. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell 7, 411-420.
    • (2001) Mol. Cell , vol.7 , pp. 411-420
    • Myung, J.1    Kim, K.B.2    Lindsten, K.3    Dantuma, N.P.4    Crews, C.M.5
  • 103
    • 0030880547 scopus 로고    scopus 로고
    • Intermediates in the formation of mouse 20S proteasomes: Implications for the assembly of precursor β subunits
    • Nandi, D., Woodward, E., Ginsburg, D.B., Monaco, J.J., 1997. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor β subunits. EMBO J. 16, 5363-5375.
    • (1997) EMBO J. , vol.16 , pp. 5363-5375
    • Nandi, D.1    Woodward, E.2    Ginsburg, D.B.3    Monaco, J.J.4
  • 104
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 106
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure - Diverse function
    • + superfamily ATPases: common structure - diverse function. Genes Cells 6, 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 107
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two component cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • Orlowski, M., Cardozo, C., Michaud, C., 1993. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two component cleaving bonds on the carboxyl side of branched chain and small neutral amino acids. Biochemistry 32, 1563-1572.
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 108
    • 0034607871 scopus 로고    scopus 로고
    • Atomic force microscopy reveals two conformations of the 20S proteasome from fission yeast
    • Osmulski, P.A., Gaczynska, M., 2000. Atomic force microscopy reveals two conformations of the 20S proteasome from fission yeast. J. Biol. Chem. 275, 13171-13174.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13171-13174
    • Osmulski, P.A.1    Gaczynska, M.2
  • 109
    • 0037018938 scopus 로고    scopus 로고
    • Nanoenzymology of the 20S proteasome: Proteasomal actions are controlled by the allosteric transition
    • Osmulski, P.A., Gaczynska, M., 2002. Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition. Biochemistry 41, 7047-7053.
    • (2002) Biochemistry , vol.41 , pp. 7047-7053
    • Osmulski, P.A.1    Gaczynska, M.2
  • 110
    • 0024843661 scopus 로고
    • Macroxyproteinase (M.O.P.): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells
    • Pacifici, R.E., Salo, D.C., Davies, K.J., 1989. Macroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Radic. Biol. Med. 7, 521-536.
    • (1989) Free Radic. Biol. Med. , vol.7 , pp. 521-536
    • Pacifici, R.E.1    Salo, D.C.2    Davies, K.J.3
  • 111
    • 0028077607 scopus 로고
    • Differential synthesis and cytolocalization of prosomes in chick embryos during development
    • Pal, J.K., Martins, d.S., Scherrer, K., 1994. Differential synthesis and cytolocalization of prosomes in chick embryos during development. Int. J. Dev. Biol. 38, 525-534.
    • (1994) Int. J. Dev. Biol. , vol.38 , pp. 525-534
    • Pal, J.K.1    Martins, D.S.2    Scherrer, K.3
  • 112
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C.M., 2001. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 113
    • 0033959311 scopus 로고    scopus 로고
    • Characterization of the 20S proteasome from the actinomycete Frankia
    • Pouch, M.N., Cournoyer, B., Baumeister, W., 2000. Characterization of the 20S proteasome from the actinomycete Frankia. Mol. Microbiol. 35, 368-377.
    • (2000) Mol. Microbiol. , vol.35 , pp. 368-377
    • Pouch, M.N.1    Cournoyer, B.2    Baumeister, W.3
  • 114
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Frohlich, K.-U., Diamant, N., Bar-Nun, S., 2002. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22, 626-634.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.-U.3    Diamant, N.4    Bar-Nun, S.5
  • 115
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • Ramos, P.C., Hockendorff, J., Johnson, E.S., Varshavsky, A., Dohmen, R.J., 1998. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92, 489-499.
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Hockendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 116
    • 0033965851 scopus 로고    scopus 로고
    • The proteasome activator 11 S REG (PA28) and class I antigen presentation
    • Rechsteiner, M., Realini, C., Ustrell, V., 2000. The proteasome activator 11 S REG (PA28) and class I antigen presentation. Biochem. J. 345, 1-15.
    • (2000) Biochem. J. , vol.345 , pp. 1-15
    • Rechsteiner, M.1    Realini, C.2    Ustrell, V.3
  • 117
    • 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
  • 118
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by γ-interferon and phosphorylation
    • Rivett, A.J., Bose, S., Brooks, P., Broadfoot, K.I., 2001. Regulation of proteasome complexes by γ-interferon and phosphorylation. Biochimie 83, 363-366.
    • (2001) Biochimie , vol.83 , pp. 363-366
    • Rivett, A.J.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 119
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K.L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., Goldberg, A.L., 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 120
    • 0032909548 scopus 로고    scopus 로고
    • Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography
    • Rockel, B., Walz, J., Hegerl, R., Peters, J., Typke, D., Baumeister, W., 1999. Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography. FEBS Lett. 451, 27-32.
    • (1999) FEBS Lett. , vol.451 , pp. 27-32
    • Rockel, B.1    Walz, J.2    Hegerl, R.3    Peters, J.4    Typke, D.5    Baumeister, W.6
  • 121
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S., Finley, D., 1998. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17, 4909-4919.
    • (1998) EMBO J. , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 122
    • 0032549642 scopus 로고    scopus 로고
    • Proteasome function is dispensable under normal but not under heat shock conditions in Thermoplasma acidophilum
    • Ruepp, A., Eckerskorn, C., Bogyo, M., Baumeister, W., 1998. Proteasome function is dispensable under normal but not under heat shock conditions in Thermoplasma acidophilum. FEBS Lett. 425, 87-90.
    • (1998) FEBS Lett. , vol.425 , pp. 87-90
    • Ruepp, A.1    Eckerskorn, C.2    Bogyo, M.3    Baumeister, W.4
  • 123
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • Russell, S.J., Reed, S.H., Huang, W., Friedberg, E.C., Johnston, S.A., 1999. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol. Cell 3, 687-695.
    • (1999) Mol. Cell , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 124
    • 0036382885 scopus 로고    scopus 로고
    • Identification of ubiquitin-like protein-binding subunits of the 26S proteasome
    • Saeki, Y., Sone, T., Yokosawa, H., Yokosawa, H., 2002. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Biochem. Biophys. Res. Commun. 296, 813-819.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 813-819
    • Saeki, Y.1    Sone, T.2    Yokosawa, H.3    Yokosawa, H.4
  • 125
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P.R., Wittinghofer, A., 1990. The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 126
    • 0035895354 scopus 로고    scopus 로고
    • Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit
    • Satoh, K., Sasajima, H., Nyoumura, K., Yokosawa, H., Sawada, H., 2001. Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. Biochemistry 40, 314-319.
    • (2001) Biochemistry , vol.40 , pp. 314-319
    • Satoh, K.1    Sasajima, H.2    Nyoumura, K.3    Yokosawa, H.4    Sawada, H.5
  • 127
    • 0032859319 scopus 로고    scopus 로고
    • Structure and mechanism of ATP-dependent proteases
    • Schmidt, M., Lupas, A.N., Finley, D., 1999. Structure and mechanism of ATP-dependent proteases. Curr. Opin. Chem. Biol. 3, 584-591.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 584-591
    • Schmidt, M.1    Lupas, A.N.2    Finley, D.3
  • 128
    • 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, P., Frommel, C., Löwe, J., Huber, R., Kloetzel, P.M., 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, P.4    Frommel, C.5    Löwe, J.6    Huber, R.7    Kloetzel, P.M.8    Schmidt, M.9
  • 129
    • 0031585998 scopus 로고    scopus 로고
    • Maturation of mammalian 20S proteasome: Purification and characterization of 13S and 16S proteasome precursor complexes
    • Schmidtke, G., Schmidt, M., Kloetzel, P.-M., 1997. Maturation of mammalian 20S proteasome: purification and characterization of 13S and 16S proteasome precursor complexes. J. Mol. Biol. 268, 95-106.
    • (1997) J. Mol. Biol. , vol.268 , pp. 95-106
    • Schmidtke, G.1    Schmidt, M.2    Kloetzel, P.-M.3
  • 131
    • 0034698121 scopus 로고    scopus 로고
    • Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20S proteasome
    • Schmidtke, G., Emch, S., Groettrup, M., Holzhutter, H.G., 2000. Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20S proteasome. J. Biol. Chem. 275, 22056-22063.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22056-22063
    • Schmidtke, G.1    Emch, S.2    Groettrup, M.3    Holzhutter, H.G.4
  • 132
    • 0027433027 scopus 로고
    • Drosophila proteasome Dm25 subunit substitutes the mouse MC3 subunit in hybrid proteasomes. The N-terminal domain is essential for subunit incorporation
    • Seelig, A., Multhaup, G., Pesold-Hurt, B., Beyreuther, K., Kloetzel, P.M., 1993. Drosophila proteasome Dm25 subunit substitutes the mouse MC3 subunit in hybrid proteasomes. The N-terminal domain is essential for subunit incorporation. J. Biol. Chem. 268, 25561-25567.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25561-25567
    • Seelig, A.1    Multhaup, G.2    Pesold-Hurt, B.3    Beyreuther, K.4    Kloetzel, P.M.5
  • 134
    • 0029789918 scopus 로고    scopus 로고
    • Autocatalytic processing of the 20S proteasome
    • Seemüller, E., Lupas, A., Baumeister, W., 1996. Autocatalytic processing of the 20S proteasome. Nature 382, 468-470.
    • (1996) Nature , vol.382 , pp. 468-470
    • Seemüller, E.1    Lupas, A.2    Baumeister, W.3
  • 135
    • 0026783274 scopus 로고
    • Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells
    • Shimbara, N., Orino, E., Sone, S., Ogura, T., Takashina, M., Shono, M., Tamura, T., Yasuda, H., Tanaka, K., Ichihara, A., 1992. Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells. J. Biol. Chem. 267, 18100-18109.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18100-18109
    • Shimbara, N.1    Orino, E.2    Sone, S.3    Ogura, T.4    Takashina, M.5    Shono, M.6    Tamura, T.7    Yasuda, H.8    Tanaka, K.9    Ichihara, A.10
  • 136
    • 0037423187 scopus 로고    scopus 로고
    • ATPase activity of p97-VCP: D2 mediates the major enzyme activity and D1 contributes to the heat-induced activity
    • Song, C., Wang, Q., Liu, C.C., 2003. ATPase activity of p97-VCP: D2 mediates the major enzyme activity and D1 contributes to the heat-induced activity. J. Biol. Chem. 278, 3648-3655.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Liu, C.C.3
  • 137
    • 0033780126 scopus 로고    scopus 로고
    • Kinetic evidences for facilitation of peptide channelling by the proteasome activator PA28
    • Stohwasser, R., Salzmann, U., Giesebrecht, J., Kloetzel, P.M., Holzhutter, H.G., 2000. Kinetic evidences for facilitation of peptide channelling by the proteasome activator PA28. Eur. J. Biochem. 267, 6221-6230.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6221-6230
    • Stohwasser, R.1    Salzmann, U.2    Giesebrecht, J.3    Kloetzel, P.M.4    Holzhutter, H.G.5
  • 138
    • 0034090632 scopus 로고    scopus 로고
    • Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome
    • Strickland, E., Hakala, K., Thomas, P.J., DeMartino, G.N., 2000. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome. J. Biol. Chem. 275, 5565-5572.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5565-5572
    • Strickland, E.1    Hakala, K.2    Thomas, P.J.3    DeMartino, G.N.4
  • 140
    • 0028000102 scopus 로고
    • Role of proteasomes modifed by interferon-γ in antigen processing
    • Tanaka, K., 1994. Role of proteasomes modifed by interferon-γ in antigen processing. J. Leuk. Biol. 56, 571-575.
    • (1994) J. Leuk. Biol. , vol.56 , pp. 571-575
    • Tanaka, K.1
  • 141
    • 0031819536 scopus 로고    scopus 로고
    • The MHC class I ligand-generating system: Roles of immunoproteasomes and the interferon-γ-inducible proteasome activator PA28
    • Tanaka, K., Kasahara, M., 1998. The MHC class I ligand-generating system: roles of immunoproteasomes and the interferon-γ-inducible proteasome activator PA28. Immunol. Rev. 163, 161-176.
    • (1998) Immunol. Rev. , vol.163 , pp. 161-176
    • Tanaka, K.1    Kasahara, M.2
  • 142
    • 0024459376 scopus 로고
    • Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival
    • Teichert, U., Mechler, B., Muller, H., Wolf, D.H., 1989. Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. J. Biol. Chem. 264, 16037-16045.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16037-16045
    • Teichert, U.1    Mechler, B.2    Muller, H.3    Wolf, D.H.4
  • 143
    • 0037115555 scopus 로고    scopus 로고
    • Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae
    • Tone, Y., Toh-e, A., 2002. Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae. Genes Dev. 16, 3142-3157.
    • (2002) Genes Dev. , vol.16 , pp. 3142-3157
    • Tone, Y.1    Toh-e, A.2
  • 144
    • 0033953565 scopus 로고    scopus 로고
    • Nob1p, a new essential protein, associates with the 26S proteasome of growing Saccharomyces cerevisiae cells
    • Tone, Y., Tanahashi, N., Tanaka, K., Fujimuro, M., Yokosawa, H., Toh-e, A., 2000. Nob1p, a new essential protein, associates with the 26S proteasome of growing Saccharomyces cerevisiae cells. Gene 243, 37-45.
    • (2000) Gene , vol.243 , pp. 37-45
    • Tone, Y.1    Tanahashi, N.2    Tanaka, K.3    Fujimuro, M.4    Yokosawa, H.5    Toh-e, A.6
  • 145
    • 0028352980 scopus 로고
    • Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90
    • Tsubuki, S., Saito, Y., Kawashima, S., 1994. Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90. FEBS Lett. 344, 229-233.
    • (1994) FEBS Lett. , vol.344 , pp. 229-233
    • Tsubuki, S.1    Saito, Y.2    Kawashima, S.3
  • 146
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • Turner, G.C., Varshavsky, A., 2000. Detecting and measuring cotranslational protein degradation in vivo. Science 289, 2117-2120.
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 147
    • 0035314002 scopus 로고    scopus 로고
    • Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome
    • Van den Eynde, B.J., Morel, S., 2001. Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome. Curr. Opin. Immunol. 13, 147-153.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 147-153
    • Van Den Eynde, B.J.1    Morel, S.2
  • 148
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma, R., Chen, S., Feldman, R., Schieltz, D., Yates, J., Dohmen, J., Deshaies, R.J., 2000. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11, 3425-3439.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 149
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P., Baumeister, W., 1999. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 150
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J., Gay, N.J., 1982. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 151
    • 0032469437 scopus 로고    scopus 로고
    • Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask
    • Wang, J., Hartling, J.A., Flanagan, J.M., 1998. Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J. Struct. Biol. 124, 151-163.
    • (1998) J. Struct. Biol. , vol.124 , pp. 151-163
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 152
    • 0026758195 scopus 로고
    • A monoclonal antibody that distinguishes latent and active forms of the proteasome (multicatalytic proteinase complex)
    • Weitman, D., Etlinger, J.D., 1992. A monoclonal antibody that distinguishes latent and active forms of the proteasome (multicatalytic proteinase complex). J. Biol. Chem. 267, 6977-6982.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6977-6982
    • Weitman, D.1    Etlinger, J.D.2
  • 153
    • 0027289155 scopus 로고
    • Thermoplasma acidophilum proteasomes degrade partially unfolded and ubiquitin-associated proteins
    • Wenzel, T., Baumeister, W., 1993. Thermoplasma acidophilum proteasomes degrade partially unfolded and ubiquitin-associated proteins. FEBS Lett. 326, 215-218.
    • (1993) FEBS Lett. , vol.326 , pp. 215-218
    • Wenzel, T.1    Baumeister, W.2
  • 154
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel, T., Baumeister, W., 1995. Conformational constraints in protein degradation by the 20S proteasome. Nat. Struct. Biol. 2, 199-204.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 156
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M.R., Gottesman, S., 1999. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286, 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 157
    • 0032836107 scopus 로고    scopus 로고
    • Halophilic 20S proteasomes of the archaeon Haloferax volcanii: Purification, characterization, and gene sequence analysis
    • Wilson, H.L., Aldrich, H.C., Maupin-Furlow, J.A., 1999. Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis. J. Bacteriol. 181, 5814-5824.
    • (1999) J. Bacteriol. , vol.181 , pp. 5814-5824
    • Wilson, H.L.1    Aldrich, H.C.2    Maupin-Furlow, J.A.3
  • 158
    • 0034100371 scopus 로고    scopus 로고
    • Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome
    • Wilson, H.L., Ou, M.S., Aldrich, H.C., Maupin-Furlow, J.A., 2000. Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome. J. Bacteriol. 182, 1680-1692.
    • (2000) J. Bacteriol. , vol.182 , pp. 1680-1692
    • Wilson, H.L.1    Ou, M.S.2    Aldrich, H.C.3    Maupin-Furlow, J.A.4
  • 160
    • 0028788228 scopus 로고
    • In vivo assembly of the proteasomal complexes, implications for antigen processing
    • Yang, Y., Früh, K., Ahn, K., Peterson, P.A., 1995. In vivo assembly of the proteasomal complexes, implications for antigen processing. J. Biol. Chem. 270, 27687-27964.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27687-27964
    • Yang, Y.1    Früh, K.2    Ahn, K.3    Peterson, P.A.4
  • 161
    • 0033408417 scopus 로고    scopus 로고
    • α5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings
    • Yao, Y., Toth, C.R., Huang, L., Wong, M.L., Dias, P., Burlingame, A.L., Coffino, P., Wang, C.C., 1999. α5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings. Biochem. J. 344, 349-358.
    • (1999) Biochem. J. , vol.344 , pp. 349-358
    • Yao, Y.1    Toth, C.R.2    Huang, L.3    Wong, M.L.4    Dias, P.5    Burlingame, A.L.6    Coffino, P.7    Wang, C.C.8
  • 162
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R.C., Hanson, P.I., Jahn, R., Brunger, A.T., 1998. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5, 803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 163
    • 0039660001 scopus 로고    scopus 로고
    • Dissecting the assembly pathway of the 20S proteasome
    • Zühl, F., Seemüller, E., Golbik, R., Baumeister, W., 1997. Dissecting the assembly pathway of the 20S proteasome. FEBS Lett. 418, 189-194.
    • (1997) FEBS Lett. , vol.418 , pp. 189-194
    • Zühl, F.1    Seemüller, E.2    Golbik, R.3    Baumeister, W.4
  • 164
    • 0033174071 scopus 로고    scopus 로고
    • AAA-ATPases at the crossroads of protein life and death
    • Zwickl, P., Baumeister, W., 1999. AAA-ATPases at the crossroads of protein life and death. Nat. Cell Biol. 1, E97-E98.
    • (1999) Nat. Cell Biol. , vol.1
    • Zwickl, P.1    Baumeister, W.2
  • 165
    • 0025957995 scopus 로고
    • Cloning and sequencing of the gene encoding the large (α-) subunit of the proteasome from Thermoplasma acidophilum
    • Zwickl, P., Lottspeich, F., Dahlmann, B., Baumeister, W., 1991. Cloning and sequencing of the gene encoding the large (α-) subunit of the proteasome from Thermoplasma acidophilum. FEBS Lett. 278, 217-221.
    • (1991) FEBS Lett. , vol.278 , pp. 217-221
    • Zwickl, P.1    Lottspeich, F.2    Dahlmann, B.3    Baumeister, W.4
  • 167
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26S proteasome, activates protein breakdown by 20S proteasomes
    • Zwickl, P., Ng, D., Woo, K.M., Klenk, H.-P., Goldberg, A.L., 1999. An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26S proteasome, activates protein breakdown by 20S proteasomes. J. Biol. Chem. 274, 26008-26014.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26008-26014
    • Zwickl, P.1    Ng, D.2    Woo, K.M.3    Klenk, H.-P.4    Goldberg, A.L.5
  • 168
    • 0034076210 scopus 로고    scopus 로고
    • Dis-assembly lines: The proteasome and related ATPase-assisted proteases
    • Zwickl, P., Baumeister, W., Steven, A., 2000. Dis-assembly lines: the proteasome and related ATPase-assisted proteases. Curr. Opin. Struct. Biol. 10, 242-250.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 242-250
    • Zwickl, P.1    Baumeister, W.2    Steven, A.3
  • 169
    • 0035716877 scopus 로고    scopus 로고
    • The proteasome: A supramolecular assembly designed for controlled proteolysis
    • Zwickl, P., Seemuller, E., Kapelari, B., Baumeister, W., 2002. The proteasome: a supramolecular assembly designed for controlled proteolysis. Adv. Protein Chem. 59, 187-222.
    • (2002) Adv. Protein Chem. , vol.59 , pp. 187-222
    • Zwickl, P.1    Seemuller, E.2    Kapelari, B.3    Baumeister, W.4


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