메뉴 건너뛰기




Volumn 46, Issue 1, 2006, Pages 23-32

An optimized system for expression and purification of secreted bacterial proteins

Author keywords

Pathogens; Secreted proteins; Toxins; Virulence factors

Indexed keywords

BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; PEPTIDE HYDROLASE; VIRUS PROTEIN;

EID: 32644473351     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.09.003     Document Type: Article
Times cited : (99)

References (21)
  • 1
    • 20444503899 scopus 로고    scopus 로고
    • The Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens
    • B.V. Geisbrecht, B.Y. Hamaoka, B. Perman, A. Zemla, and D.J. Leahy The Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens J. Biol. Chem. 280 2005 17243 17250
    • (2005) J. Biol. Chem. , vol.280 , pp. 17243-17250
    • Geisbrecht, B.V.1    Hamaoka, B.Y.2    Perman, B.3    Zemla, A.4    Leahy, D.J.5
  • 4
    • 0033618161 scopus 로고    scopus 로고
    • Characterization of PECI, a novel monofunctional Delta(3),Delta(2)-enoyl- CoA isomerase of mammalian peroxisomes
    • B.V. Geisbrecht, D. Zhang, H. Schulz, and S.J. Gould Characterization of PECI, a novel monofunctional Delta(3),Delta(2)-enoyl-CoA isomerase of mammalian peroxisomes J. Biol. Chem. 274 1999 21797 21803
    • (1999) J. Biol. Chem. , vol.274 , pp. 21797-21803
    • Geisbrecht, B.V.1    Zhang, D.2    Schulz, H.3    Gould, S.J.4
  • 5
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco Etch Virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • R.B. Kapust, J. Tozser, J.D. Fox, D.E. Anderson, S. Cherry, T.D. Copeland, and D.S. Waugh Tobacco Etch Virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency Prot. Eng. 14 2001 993 1000
    • (2001) Prot. Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 6
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • G.I. Evan, G.K. Lewis, G. Ramsay, and J.M. Bishop Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product Mol. Cell. Biol. 5 1985 3610 3616
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 7
    • 0024004266 scopus 로고
    • Biochemical and mutational analysis of a plant virus polyprotein cleavage site
    • W.G. Dougherty, J.C. Carrington, S.M. Cary, and T.D. Parks Biochemical and mutational analysis of a plant virus polyprotein cleavage site EMBO J. 7 1988 1281 1287
    • (1988) EMBO J. , vol.7 , pp. 1281-1287
    • Dougherty, W.G.1    Carrington, J.C.2    Cary, S.M.3    Parks, T.D.4
  • 8
    • 0028110821 scopus 로고
    • The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly
    • D.I. Crane, J.E. Kalish, and S.J. Gould The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly J. Biol. Chem. 269 1994 21835 21844
    • (1994) J. Biol. Chem. , vol.269 , pp. 21835-21844
    • Crane, D.I.1    Kalish, J.E.2    Gould, S.J.3
  • 9
    • 0033662957 scopus 로고    scopus 로고
    • A mammalian expression vector for expression and purification of secreted proteins for structural studies
    • D.J. Leahy, C.E. Dann 3rd, P. Longo, B. Perman, and K.X. Ramyar A mammalian expression vector for expression and purification of secreted proteins for structural studies Protein Expr. Purif. 20 2000 500 506
    • (2000) Protein Expr. Purif. , vol.20 , pp. 500-506
    • Leahy, D.J.1    Dann III, C.E.2    Longo, P.3    Perman, B.4    Ramyar, K.X.5
  • 10
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • J. Marmur A procedure for the isolation of deoxyribonucleic acid from micro-organisms J. Mol. Biol. 3 1961 208 218
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 11
    • 0029000550 scopus 로고
    • Expression and purification of a recombinant Tobacco Etch Virus NIa proteinase: Biochemical analyses of the full-length and a naturally occurring truncated proteinase form
    • T.D. Parks, E.D. Howard, T.J. Wolpert, D.J. Arp, and W.G. Dougherty Expression and purification of a recombinant Tobacco Etch Virus NIa proteinase: biochemical analyses of the full-length and a naturally occurring truncated proteinase form Virology 210 1995 194 201
    • (1995) Virology , vol.210 , pp. 194-201
    • Parks, T.D.1    Howard, E.D.2    Wolpert, T.J.3    Arp, D.J.4    Dougherty, W.G.5
  • 12
    • 0035095521 scopus 로고    scopus 로고
    • Large-scale purification of a stable form of recombinant Tobacco Etch Virus protease
    • L.J. Lucast, R.T. Batey, and J.A. Doudna Large-scale purification of a stable form of recombinant Tobacco Etch Virus protease Biotechniques 30 2001 544 554
    • (2001) Biotechniques , vol.30 , pp. 544-554
    • Lucast, L.J.1    Batey, R.T.2    Doudna, J.A.3
  • 13
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • D.N. Garboczi, D.T. Hung, and D.C. Wiley HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides Proc. Natl. Acad. Sci. USA 89 1992 3429 3433
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 14
  • 16
    • 0028286641 scopus 로고
    • Cloning and characterization of a gene for a 19 kDa fibrinogen-binding protein from Staphylococcus aureus
    • M.K. Boden, and J.-I. Flock Cloning and characterization of a gene for a 19 kDa fibrinogen-binding protein from Staphylococcus aureus Mol. Microbiol. 12 1994 599 606
    • (1994) Mol. Microbiol. , vol.12 , pp. 599-606
    • Boden, M.K.1    Flock, J.-I.2
  • 19
    • 0025263886 scopus 로고
    • Molecular cloning and amino acid sequence of peptide-N4-(N-acteyl-β- d-glucosaminyl)asparagine amidase from Flavobacterium meningosepticum
    • A.L. Tarentino, G. Quinones, A. Trumble, L.-M. Changchien, B. Duceman, F. Maley, and T.H. Plummer Jr. Molecular cloning and amino acid sequence of peptide-N4-(N-acteyl-β-d-glucosaminyl)asparagine amidase from Flavobacterium meningosepticum J. Biol. Chem. 265 1990 6961 6966
    • (1990) J. Biol. Chem. , vol.265 , pp. 6961-6966
    • Tarentino, A.L.1    Quinones, G.2    Trumble, A.3    Changchien, L.-M.4    Duceman, B.5    Maley, F.6    Plummer Jr., T.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.