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Volumn 3, Issue , 2004, Pages

A step ahead: Combining protein purification and correct folding selection

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY SCREENING; ARTICLE; AUTOMATION; PHAGE DISPLAY; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN TARGETING; QUALITY CONTROL;

EID: 13644264347     PISSN: 14752859     EISSN: None     Source Type: Journal    
DOI: 10.1186/1475-2859-3-12     Document Type: Article
Times cited : (8)

References (12)
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    • Recombinant proteins fused to thermostable partners can be purified by heat incubation
    • de Marco A, Casatta E, Savaresi S, Geerlof A: Recombinant proteins fused to thermostable partners can be purified by heat incubation. J Biotechnol 2004, 107:125-133.
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    • de Marco, A.1    Casatta, E.2    Savaresi, S.3    Geerlof, A.4
  • 3
    • 0034956228 scopus 로고    scopus 로고
    • A strategy for optimizing the monodispersity of fusion proteins: Application to purification of recombinant HPV E6 oncoprotein
    • Nominé Y, Ristriani T, Laurent C, Lefevre J-F, Weiss E, Travé G: A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein. Prot Engineer 2001, 14:297-305.
    • (2001) Prot. Engineer. , vol.14 , pp. 297-305
    • Nominé, Y.1    Ristriani, T.2    Laurent, C.3    Lefevre, J.-F.4    Weiss, E.5    Travé, G.6
  • 4
    • 4444302074 scopus 로고    scopus 로고
    • Aggregation-resistant domain antibodies selected on phage by heat denaturation
    • Jespers L, Schon O, Famm K, Winter G: Aggregation-resistant domain antibodies selected on phage by heat denaturation. Nat Biotechnol 2004, 22:1161-1165.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1161-1165
    • Jespers, L.1    Schon, O.2    Famm, K.3    Winter, G.4
  • 5
    • 0036213467 scopus 로고    scopus 로고
    • Gene expression response to misfolded protein as a screen for soluble recombinant protein
    • Lesley SA, Graziano J, Cho CY, Knuth MW, Klock HE: Gene expression response to misfolded protein as a screen for soluble recombinant protein. Prot Engineer 2002, 15:153-160.
    • (2002) Prot. Engineer , vol.15 , pp. 153-160
    • Lesley, S.A.1    Graziano, J.2    Cho, C.Y.3    Knuth, M.W.4    Klock, H.E.5
  • 7
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley WC, Stidham RD, Smith NM, Hunt JF, Thomas PJ: Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat Biotechnol 2001, 19:131-136.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4    Thomas, P.J.5
  • 9
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • Carrió MM, Villaverde A: Protein aggregation as bacterial inclusion bodies is reversible. FEBS Letters 2001, 489:29-33.
    • (2001) FEBS Letters , vol.489 , pp. 29-33
    • Carrió, M.M.1    Villaverde, A.2
  • 10
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A, Schlieker C, Friedrich K, Schönfeld H-J, Vierling E, Bukau B: Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 2003, 278:31033-31042.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.3    Schönfeld, H.-J.4    Vierling, E.5    Bukau, B.6
  • 11
    • 0032079487 scopus 로고    scopus 로고
    • The small heatshock protein IbpB from Escherichia coli stabilizes stress-denaturated proteins for subsequent refolding by a multichaperone network
    • Veinger L, Diamant S, Buchner J, Goloubinoff P: The small heatshock protein IbpB from Escherichia coli stabilizes stress-denaturated proteins for subsequent refolding by a multichaperone network. J Biol Chem 1998, 273:11032-11037.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 12
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    • Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning
    • de Marco A, De Marco V: Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J Biotechnol 2004, 109: 5-52.
    • (2004) J. Biotechnol. , vol.109 , pp. 45-52
    • de Marco, A.1    De Marco, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.