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Volumn 398, Issue , 2005, Pages 540-554

Using deubiquitylating enzymes as research tools

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; HYBRID PROTEIN; ISOPEPTIDE; LYSINE; PEPTIDE; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 27644595172     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)98044-0     Document Type: Review
Times cited : (110)

References (23)
  • 2
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A., Finley D., and Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue Science 234 1986 179 186
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 3
    • 0030272645 scopus 로고    scopus 로고
    • Protein expression using ubiquitin fusion and cleavage
    • Baker R.T. Protein expression using ubiquitin fusion and cleavage Curr. Opin. Biotechnol. 7 1996 541 546
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 541-546
    • Baker, R.T.1
  • 4
    • 0026062590 scopus 로고
    • The human Ub-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes
    • Baker R.T., and Board P.G. The human Ub-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes Nucleic Acids Res. 19 1991 1035 1040
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1035-1040
    • Baker, R.T.1    Board, P.G.2
  • 5
    • 0028142992 scopus 로고
    • Protein expression using cotranslational fusion and cleavage of ubiquitin: Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferase
    • Baker R.T., Smith S.A., Marano R., McKee J., and Board P.G. Protein expression using cotranslational fusion and cleavage of ubiquitin: Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferase J. Biol. Chem. 269 1994 25381 25386
    • (1994) J. Biol. Chem. , vol.269 , pp. 25381-25386
    • Baker, R.T.1    Smith, S.A.2    Marano, R.3    McKee, J.4    Board, P.G.5
  • 6
    • 0026023373 scopus 로고
    • Inhibition of the N-end rule pathway in living cells
    • Baker R.T., and Varshavsky A. Inhibition of the N-end rule pathway in living cells Proc. Natl. Acad. Sci. USA 88 1991 1090 1094
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1090-1094
    • Baker, R.T.1    Varshavsky, A.2
  • 7
    • 0033180148 scopus 로고    scopus 로고
    • Identification, functional characterization and chromosomal localisation of USP15, a novel human ubiquitin-specific protease related to the Unp/USP4 oncoprotein, and a systematic nomenclature proposal for human ubiquitin-specific proteases
    • Baker R.T., Wang X.-W., Woollatt E., White J., and Sutherland G.R. Identification, functional characterization and chromosomal localisation of USP15, a novel human ubiquitin-specific protease related to the Unp/USP4 oncoprotein, and a systematic nomenclature proposal for human ubiquitin-specific proteases Genomics 59 1999 264 274
    • (1999) Genomics , vol.59 , pp. 264-274
    • Baker, R.T.1    Wang, X.-W.2    Woollatt, E.3    White, J.4    Sutherland, G.R.5
  • 10
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • Catanzariti A.-M., Soboleva T.A., Jans D.A., Board P.G., and Baker R.T. An efficient system for high-level expression and easy purification of authentic recombinant proteins Protein Sci. 13 2004 1331 1339
    • (2004) Protein Sci. , vol.13 , pp. 1331-1339
    • Catanzariti, A.-M.1    Soboleva, T.A.2    Jans, D.A.3    Board, P.G.4    Baker, R.T.5
  • 13
    • 0031463942 scopus 로고    scopus 로고
    • A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond
    • Gilchrist C.A., Gray D.A., and Baker R.T. A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond J. Biol. Chem. 272 1997 32280 32285
    • (1997) J. Biol. Chem. , vol.272 , pp. 32280-32285
    • Gilchrist, C.A.1    Gray, D.A.2    Baker, R.T.3
  • 14
    • 0345602153 scopus 로고    scopus 로고
    • Gene structure, alternate splicing, tissue distribution, cellular localization, and developmental expression pattern of mouse deubiquitinating enzyme isoforms Usp2-45 and Usp2-69
    • Gousseva N., and Baker R.T. Gene structure, alternate splicing, tissue distribution, cellular localization, and developmental expression pattern of mouse deubiquitinating enzyme isoforms Usp2-45 and Usp2-69 Gene Expr. 11 2003 163 179
    • (2003) Gene Expr. , vol.11 , pp. 163-179
    • Gousseva, N.1    Baker, R.T.2
  • 15
    • 0033080490 scopus 로고    scopus 로고
    • Use of ubiquitin fusions to augment protein expression in transgenic plants
    • Hondred D., Walker J.M., Mathews D.E., and Vierstra R.D. Use of ubiquitin fusions to augment protein expression in transgenic plants Plant Physiol. 119 1999 713 724
    • (1999) Plant Physiol. , vol.119 , pp. 713-724
    • Hondred, D.1    Walker, J.M.2    Mathews, D.E.3    Vierstra, R.D.4
  • 16
    • 0021114727 scopus 로고
    • Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials: Serum protein affinities for gel-immobilized iron and nickel ions
    • Porath J., and Olin B. Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials: Serum protein affinities for gel-immobilized iron and nickel ions Biochemistry 22 1983 1621 1630
    • (1983) Biochemistry , vol.22 , pp. 1621-1630
    • Porath, J.1    Olin, B.2
  • 17
    • 1942521481 scopus 로고    scopus 로고
    • Modelling and bioinformatics studies of the human Kappa class glutathione transferase predict a novel third glutathione transferase family with homology to prokaryotic 2-hydroxychromene-2-carboxylate (HCCA) isomerases
    • Robinson A., Huttley G.A., Booth H.S., and Board P.G. Modelling and bioinformatics studies of the human Kappa class glutathione transferase predict a novel third glutathione transferase family with homology to prokaryotic 2-hydroxychromene-2-carboxylate (HCCA) isomerases Biochem. J. 379 2004 541 552
    • (2004) Biochem. J. , vol.379 , pp. 541-552
    • Robinson, A.1    Huttley, G.A.2    Booth, H.S.3    Board, P.G.4
  • 18
    • 0034665455 scopus 로고    scopus 로고
    • Design of high-throughput methods of protein production for structural biology
    • Stevens R.C. Design of high-throughput methods of protein production for structural biology Struct. Fold. Des. 8 2000 R177 R185
    • (2000) Struct. Fold. Des. , vol.8
    • Stevens, R.C.1
  • 19
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., and Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J. Mol. Biol. 189 1986 113 130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 20
    • 0025365143 scopus 로고
    • Gene fusions for purpose of expression: An introduction
    • Uhlen M., and Moks T. Gene fusions for purpose of expression: An introduction Methods Enzymol. 185 1990 129 143
    • (1990) Methods Enzymol. , vol.185 , pp. 129-143
    • Uhlen, M.1    Moks, T.2
  • 21
    • 0034581529 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and its descendants
    • Varshavsky A. Ubiquitin fusion technique and its descendants Methods Enzymol. 327 2000 578 593
    • (2000) Methods Enzymol. , vol.327 , pp. 578-593
    • Varshavsky, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.