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Volumn 377, Issue 7-8, 1996, Pages 497-503

Phosphoamino acids in proteasome subunits

Author keywords

Phosphorylated subunit; Phosphoserine; Phosphothreonine; Phosphotyrosine; Proteasome (rat, human)

Indexed keywords

ANTIBODY; PHENYL ISOTHIOCYANATE; PHOSPHOAMINO ACID; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTYROSINE; PROTEASOME;

EID: 0029826248     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (31)

References (65)
  • 2
    • 0027234323 scopus 로고
    • HeLa cells proteasome interacts with leucine-rich polypeptides and contains a phosphorylated subunit
    • Arrigo, A.P., and Mehlen, P. (1993). HeLa cells proteasome interacts with leucine-rich polypeptides and contains a phosphorylated subunit. Biochem. Biophys. Res. Commun. 194, 1387-1393.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1387-1393
    • Arrigo, A.P.1    Mehlen, P.2
  • 3
    • 0024244675 scopus 로고
    • Electron microscopy and image analysis of the multicatalytic proteinase
    • Baumeister, W., Dahlmann, B., Hegerl, R., Kopp, F., Kuehn, L., and Pfeifer, G. (1988). Electron microscopy and image analysis of the multicatalytic proteinase. FEBS-Lett. 241, 239-245.
    • (1988) FEBS-Lett. , vol.241 , pp. 239-245
    • Baumeister, W.1    Dahlmann, B.2    Hegerl, R.3    Kopp, F.4    Kuehn, L.5    Pfeifer, G.6
  • 4
    • 0029143239 scopus 로고
    • Nuclear multicatalytic proteinase αsubunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment
    • Benedict, C.M., Ren, L, and Clawson, G.A. (1995). Nuclear multicatalytic proteinase αsubunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment. Biochemistry 34, 9587-9598.
    • (1995) Biochemistry , vol.34 , pp. 9587-9598
    • Benedict, C.M.1    Ren, L.2    Clawson, G.A.3
  • 5
    • 0028097823 scopus 로고
    • Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • Boes, B., Hengel, H., Ruppert, Th., Multhaupt, G., Koszinowski, U.H., and Kloetzel, P.M. (1994). Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 179, 901-909.
    • (1994) J. Exp. Med. , vol.179 , pp. 901-909
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaupt, G.4    Koszinowski, U.H.5    Kloetzel, P.M.6
  • 6
    • 0026506729 scopus 로고
    • Purification and characteriztion of a protein inhibitor of the 20S proteasome (macropain)
    • Chu-Ping, M., Slaughter, C.A., and DeMartino, G.N. (1992a). Purification and characteriztion of a protein inhibitor of the 20S proteasome (macropain). Biochim. Biophys. Acta 1119, 303-311.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 303-311
    • Chu-Ping, M.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 7
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) for the 20S proteasome (macropain)
    • Chu-Ping, M., Slaughter, C.A., and DeMartino, G.N. (1992b). Identification, purification, and characterization of a protein activator (PA28) for the 20S proteasome (macropain). J. Biol. Chem. 267, 10515-10523.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Chu-Ping, M.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 8
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome
    • Chu-Ping, M., Vu, J.H., Proske, R.J., Slaughter, C.A., and DeMartino, G.N. (1994). Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome. J. Biol. Chem. 269, 3539-3547.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3539-3547
    • Chu-Ping, M.1    Vu, J.H.2    Proske, R.J.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 9
    • 0021824670 scopus 로고
    • Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscle
    • Dahlmann, B., Kuehn, L., Rutschmann, M., and Reinauer, H. (1985). Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscle. Biochem. J. 228, 161-170.
    • (1985) Biochem. J. , vol.228 , pp. 161-170
    • Dahlmann, B.1    Kuehn, L.2    Rutschmann, M.3    Reinauer, H.4
  • 11
    • 0026498493 scopus 로고
    • Purification of an 11S regulator of the multicatalytic protease
    • Dubiel, W., Pratt, G., Ferrell, K., and Rechsteiner, M. (1992). Purification of an 11S regulator of the multicatalytic protease. J. Biol. Chem. 267, 22369-22377.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 12
    • 0028265471 scopus 로고
    • Pre-3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolysing activity
    • Enenkel, C., Lehmann, H., Kipper, J., Gückel, R., Hilt, W., and Wolf, D.H. (1994). Pre-3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolysing activity. FEBS-Lett. 341, 193-196.
    • (1994) FEBS-Lett. , vol.341 , pp. 193-196
    • Enenkel, C.1    Lehmann, H.2    Kipper, J.3    Gückel, R.4    Hilt, W.5    Wolf, D.H.6
  • 13
    • 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., and 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
  • 15
    • 0027214605 scopus 로고
    • γ-Interferon and expression of the MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska, M., Rock, K.L., and Goldberg, A.L. (1993). γ-Interferon and expression of the MHC genes regulate peptide hydrolysis by proteasomes. Nature 365, 264-267.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 16
    • 0028136465 scopus 로고
    • Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7
    • Gaczynska, M., Rock, K.L., Spies, T., and Goldberg, A.L. (1994). Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7. Proc. Natl. Acad. Sci. USA 91, 9213-9217.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9213-9217
    • Gaczynska, M.1    Rock, K.L.2    Spies, T.3    Goldberg, A.L.4
  • 17
    • 0028970626 scopus 로고
    • The interleron-γ-in-ducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro
    • Groettrup, M., Ruppert, T., Kuehn, L., Seeger, M., Standera, S., Koszinowski, U., and Kloetzel, P.M. (1995). The interleron-γ-in-ducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro. J. Biol. Chem. 270, 23808-23815.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23808-23815
    • Groettrup, M.1    Ruppert, T.2    Kuehn, L.3    Seeger, M.4    Standera, S.5    Koszinowski, U.6    Kloetzel, P.M.7
  • 19
    • 0025886124 scopus 로고
    • Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy
    • Grziwa, A., Baumeister, W., Dahlmann, B., and 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
  • 20
    • 0024497473 scopus 로고
    • The Drosophila proteasome undergoes changes in its subunit pattern during development
    • Haass, C., and 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
  • 22
    • 0025952461 scopus 로고
    • Generation and use of antibodies to phosphothreonine
    • Heffetz, D., Fridkin, M., and Zick, Y. (1991). Generation and use of antibodies to phosphothreonine. Meth. Enzymol. 201, 44-53.
    • (1991) Meth. Enzymol. , vol.201 , pp. 44-53
    • Heffetz, D.1    Fridkin, M.2    Zick, Y.3
  • 23
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase. Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • Heinemeyer, W., Kleinschmidt, J.A., Saidowsky, J., Escher, C., and Wolf, D.H. (1991). Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase. Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10, 555-562.
    • (1991) EMBO J. , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowsky, J.3    Escher, C.4    Wolf, D.H.5
  • 24
    • 0027418063 scopus 로고
    • Pre2, highly homologous to the MHC-linked Ring 10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer, W., Gruhler, A., Möhrle, V., Mahé, Y., and Wolf, D.H. (1993). Pre2, highly homologous to the MHC-linked Ring 10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268, 5115-5129.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5115-5129
    • Heinemeyer, W.1    Gruhler, A.2    Möhrle, V.3    Mahé, Y.4    Wolf, D.H.5
  • 25
    • 0026013112 scopus 로고
    • The human multicatalytic proteinase: Affinity purification using a monoclonal antibody
    • Hendil, K.B., and Uerkvrtz, W. (1991). The human multicatalytic proteinase: affinity purification using a monoclonal antibody. J. Biochem. Biophys. Meth. 22, 159-165.
    • (1991) J. Biochem. Biophys. Meth. , vol.22 , pp. 159-165
    • Hendil, K.B.1    Uerkvrtz, W.2
  • 26
    • 0028894198 scopus 로고
    • Human proteasomes analyzed with monoclonal antibodies
    • Hendil, K.B., Kristensen, P., and Uerkvitz, W. (1995). Human proteasomes analyzed with monoclonal antibodies. Biochem. J. 305, 245-252.
    • (1995) Biochem. J. , vol.305 , pp. 245-252
    • Hendil, K.B.1    Kristensen, P.2    Uerkvitz, W.3
  • 27
    • 0027457543 scopus 로고
    • The PRE4 gene codes for a subunit of the yeast proteasome necessary for petidyl-glutamyl peptide-hydrolyzing activity
    • Hilt, W., Enenkel, C., Gruhler, A., Singer, T., and Wolf, D.H. (1993). The PRE4 gene codes for a subunit of the yeast proteasome necessary for petidyl-glutamyl peptide-hydrolyzing activity J. Biol. Chem. 268, 3479-3486.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3479-3486
    • Hilt, W.1    Enenkel, C.2    Gruhler, A.3    Singer, T.4    Wolf, D.H.5
  • 28
    • 0026079536 scopus 로고
    • Generation and use of anti-phosphotyrosine antibodies for immunoblotting
    • Kamps, M.P. (1991). Generation and use of anti-phosphotyrosine antibodies for immunoblotting . Meth. Enzymol. 201, 101-110.
    • (1991) Meth. Enzymol. , vol.201 , pp. 101-110
    • Kamps, M.P.1
  • 29
    • 0029874055 scopus 로고    scopus 로고
    • The proteasome subunit, C2, contains an important site for binding of PA28 (11S) activator
    • Kania, M.A., DeMartino, G.N., Baumeister, W., and Goldberg, A.L. (1996). The proteasome subunit, C2, contains an important site for binding of PA28 (11S) activator. Eur. J. Biochem. 236, 510-516.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 510-516
    • Kania, M.A.1    DeMartino, G.N.2    Baumeister, W.3    Goldberg, A.L.4
  • 30
    • 0022533464 scopus 로고
    • Size and shape of the multicatalytic proteinase from rat skeletal muscle
    • Kopp, F., Steiner, R., Dahlmann, B., Kuehn, L., and Reinauer, H. (1986). Size and shape of the multicatalytic proteinase from rat skeletal muscle. Biochim. Biophys. Acta 872, 253-260.
    • (1986) Biochim. Biophys. Acta , vol.872 , pp. 253-260
    • Kopp, F.1    Steiner, R.2    Dahlmann, B.3    Kuehn, L.4    Reinauer, H.5
  • 31
    • 0027392566 scopus 로고
    • Evidence indicating that the human proteasome is a complex dimer
    • Kopp, F, Dahlmann, B., and Hendil, K.B. (1993). Evidence indicating that the human proteasome is a complex dimer. J. Mol. Biol. 229, 14-19.
    • (1993) J. Mol. Biol. , vol.229 , pp. 14-19
    • Kopp, F.1    Dahlmann, B.2    Hendil, K.B.3
  • 32
    • 0029021194 scopus 로고
    • The human proteasome subunit HsN3 is located in the inner rings of the complex dimer
    • Kopp, F., Kristensen, P., Hendil, K.B., Johnsen, A., Sobek, A., and Dahlmann, B. (1995). The human proteasome subunit HsN3 is located in the inner rings of the complex dimer. J. Mol. Biol. 248, 264-272.
    • (1995) J. Mol. Biol. , vol.248 , pp. 264-272
    • Kopp, F.1    Kristensen, P.2    Hendil, K.B.3    Johnsen, A.4    Sobek, A.5    Dahlmann, B.6
  • 35
    • 0025163557 scopus 로고
    • A facile method for the isolation and preparation of proteins and peptides for sequence analysis in the picomolar range
    • Kurth, J., and Stoffel, W. (1990). A facile method for the isolation and preparation of proteins and peptides for sequence analysis in the picomolar range. Biol. Chem. Hoppe-Seyler 371, 675 -683.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 675-683
    • Kurth, J.1    Stoffel, W.2
  • 36
    • 0025990207 scopus 로고
    • Isolation and characterization of a novel endogenous inhibitor of the proteasome
    • Li, X., Gu, M., and Etlinger, J.D. (1991). Isolation and characterization of a novel endogenous inhibitor of the proteasome. Biochemistry 30, 9709-9715.
    • (1991) Biochemistry , vol.30 , pp. 9709-9715
    • Li, X.1    Gu, M.2    Etlinger, J.D.3
  • 37
    • 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., and 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
  • 38
    • 0027267492 scopus 로고
    • Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30 kDa proteasome subunit
    • Ludemann, R., Lerea, K.M., and Etlinger, J.D. (1993). Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30 kDa proteasome subunit. J. Biol. Chem. 268, 17413-17417.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17413-17417
    • Ludemann, R.1    Lerea, K.M.2    Etlinger, J.D.3
  • 40
    • 0027496897 scopus 로고
    • cDNA cloning of rat proteasome subunit RC7-1, a homologue of yeast Pre1 essential for chymotrypsin-like activity
    • Nishimura, C., Tamura, T., Tokunaga, F., Tanaka, K., Ichihara, A. (1993a). cDNA cloning of rat proteasome subunit RC7-1, a homologue of yeast Pre1 essential for chymotrypsin-like activity. FEBS-Lett. 332, 52-56.
    • (1993) FEBS-Lett. , vol.332 , pp. 52-56
    • Nishimura, C.1    Tamura, T.2    Tokunaga, F.3    Tanaka, K.4    Ichihara, A.5
  • 41
    • 0027732882 scopus 로고
    • cDNA cloning of rat proteasome subunit RC10-II, assumed to be responsible for trypsin-like catalytic activity
    • Nishimura, C., Tamura, T., Akioka, H., Tokunaga, F., Tanaka, K., and Ichihara, A. (1993b). cDNA cloning of rat proteasome subunit RC10-II, assumed to be responsible for trypsin-like catalytic activity. FEBS-Lett. 336, 462-466.
    • (1993) FEBS-Lett. , vol.336 , pp. 462-466
    • Nishimura, C.1    Tamura, T.2    Akioka, H.3    Tokunaga, F.4    Tanaka, K.5    Ichihara, A.6
  • 42
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P.Z., Goodman, H.,M., and O'Farrell, P.H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12, 1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 43
    • 0025012292 scopus 로고
    • Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase
    • Pereira, M.E., and Wilk, S. (1990). Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase. Arch. Biochem. Biophys. 283, 68-74.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 68-74
    • Pereira, M.E.1    Wilk, S.2
  • 44
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters, J.M. (1994). Proteasomes: protein degradation machines of the cell. TIBS 19, 377-382.
    • (1994) TIBS , vol.19 , pp. 377-382
    • Peters, J.M.1
  • 45
    • 0021484814 scopus 로고
    • Electrophoretic transfer of proteins from fixed and stained gels
    • Phelps, D.S. (1984). Electrophoretic transfer of proteins from fixed and stained gels. Anal. Biochem. 141, 409-412.
    • (1984) Anal. Biochem. , vol.141 , pp. 409-412
    • Phelps, D.S.1
  • 46
    • 0026600786 scopus 로고
    • Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum
    • Pühler, G., Weinkauf, S., Bachmann, L., Müller, S., Engel, A., Hegerl, R., and Baumeister, W. (1992). Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum. The EMBO J. 11, 1607-1616.
    • (1992) The EMBO J. , vol.11 , pp. 1607-1616
    • Pühler, G.1    Weinkauf, S.2    Bachmann, L.3    Müller, S.4    Engel, A.5    Hegerl, R.6    Baumeister, W.7
  • 47
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett, A.J. (1993). Proteasomes: multicatalytic proteinase complexes. Biochem. J. 292, 1-10.
    • (1993) Biochem. J. , vol.292 , pp. 1-10
    • Rivett, A.J.1
  • 49
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 52
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using Coomassie Brilliant Blue G250
    • Sedmak, J.J., and Grossberg, S.E. (1977). A rapid, sensitive, and versatile assay for protein using Coomassie Brilliant Blue G250. Anal. Biochem. 79, 544-552.
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 55
    • 0026481112 scopus 로고
    • Molecular cloning of cDNAs from rat proteasome. - Deduced primary structures of 4 other subunits
    • Tamura, T., Shimbara, N., Aki, M., Ishida, N., Bey, F., Scherrer, K., Tanaka, K., and Ichihara, A. (1992). Molecular cloning of cDNAs from rat proteasome. - Deduced primary structures of 4 other subunits. J. Biochem. 112, 530-534.
    • (1992) J. Biochem. , vol.112 , pp. 530-534
    • Tamura, T.1    Shimbara, N.2    Aki, M.3    Ishida, N.4    Bey, F.5    Scherrer, K.6    Tanaka, K.7    Ichihara, A.8
  • 60
    • 0023733118 scopus 로고
    • Prosomes, small cytoplasmic RNP particles, contain glycoproteins
    • Tomek, W., Adam, G., and Schmid, H.P. (1988). Prosomes, small cytoplasmic RNP particles, contain glycoproteins. FEBS-Lett. 239, 155-158.
    • (1988) FEBS-Lett. , vol.239 , pp. 155-158
    • Tomek, W.1    Adam, G.2    Schmid, H.P.3
  • 61
    • 0025075365 scopus 로고
    • Large scale purification of prosomes from calf liver
    • Tomek, W., Buri, J., Vallon, R., and Schmid, H.P. (1990). Large scale purification of prosomes from calf liver. J. Chromatogr. 521, 221-229.
    • (1990) J. Chromatogr. , vol.521 , pp. 221-229
    • Tomek, W.1    Buri, J.2    Vallon, R.3    Schmid, H.P.4
  • 62
    • 0028890880 scopus 로고
    • Effects of interferon-γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases
    • Ustrell, V., Pratt, G., and Rechsteiner, M. (1995). Effects of interferon-γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases. Proc. Natl. Acad. Sci. USA 92, 584-588.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 584-588
    • Ustrell, V.1    Pratt, G.2    Rechsteiner, M.3
  • 64
    • 0025052281 scopus 로고
    • A multiple staining procedure for the detection of different DNA fragments on a single blot
    • West, S., Schröder, J., and Kunz, W. (1990). A multiple staining procedure for the detection of different DNA fragments on a single blot. Anal. Biochem. 190, 254-258.
    • (1990) Anal. Biochem. , vol.190 , pp. 254-258
    • West, S.1    Schröder, J.2    Kunz, W.3
  • 65
    • 0026600718 scopus 로고
    • Primary structure of the Thermoplasma proteasome and its implications for the structure, function and evolution of the multicatalytic proteinase
    • Zwickl, P., Grziwa, A., Pühler, G., Dahlmann, B., Lottspeich, F., and Baumeister, W. (1992). Primary structure of the Thermoplasma proteasome and its implications for the structure, function and evolution of the multicatalytic proteinase. Biochemistry 31, 964-972.
    • (1992) Biochemistry , vol.31 , pp. 964-972
    • Zwickl, P.1    Grziwa, A.2    Pühler, G.3    Dahlmann, B.4    Lottspeich, F.5    Baumeister, W.6


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