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188 related items for PubMed ID: 16926148

  • 1. The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.
    Merz F, Hoffmann A, Rutkowska A, Zachmann-Brand B, Bukau B, Deuerling E.
    J Biol Chem; 2006 Oct 20; 281(42):31963-71. PubMed ID: 16926148
    [Abstract] [Full Text] [Related]

  • 2. Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.
    Kramer G, Rutkowska A, Wegrzyn RD, Patzelt H, Kurz TA, Merz F, Rauch T, Vorderwülbecke S, Deuerling E, Bukau B.
    J Bacteriol; 2004 Jun 20; 186(12):3777-84. PubMed ID: 15175291
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  • 3. Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from SurA with an unrelated chaperone domain.
    Geitner AJ, Varga E, Wehmer M, Schmid FX.
    J Mol Biol; 2013 Nov 15; 425(22):4089-98. PubMed ID: 23871892
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  • 4. Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium.
    Bang H, Pecht A, Raddatz G, Scior T, Solbach W, Brune K, Pahl A.
    Eur J Biochem; 2000 Jun 15; 267(11):3270-80. PubMed ID: 10824113
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  • 6. High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA.
    Ramm K, Plückthun A.
    J Mol Biol; 2001 Jul 06; 310(2):485-98. PubMed ID: 11428902
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  • 7. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
    Behrens S, Maier R, de Cock H, Schmid FX, Gross CA.
    EMBO J; 2001 Jan 15; 20(1-2):285-94. PubMed ID: 11226178
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  • 8. L23 protein functions as a chaperone docking site on the ribosome.
    Kramer G, Rauch T, Rist W, Vorderwülbecke S, Patzelt H, Schulze-Specking A, Ban N, Deuerling E, Bukau B.
    Nature; 2002 Sep 12; 419(6903):171-4. PubMed ID: 12226666
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  • 11. Effect of C-terminal truncation on the molecular chaperone function and dimerization of Escherichia coli trigger factor.
    Zeng LL, Yu L, Li ZY, Perrett S, Zhou JM.
    Biochimie; 2006 Jun 12; 88(6):613-9. PubMed ID: 16380200
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  • 12. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.
    Xu X, Wang S, Hu YX, McKay DB.
    J Mol Biol; 2007 Oct 19; 373(2):367-81. PubMed ID: 17825319
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  • 13. Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function.
    Schulze-Gahmen U, Aono S, Chen S, Yokota H, Kim R, Kim SH.
    Acta Crystallogr D Biol Crystallogr; 2005 Oct 19; 61(Pt 10):1343-7. PubMed ID: 16204885
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  • 14. 1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli.
    Jia M, Hu Y, Jin C.
    Biomol NMR Assign; 2019 Apr 19; 13(1):183-186. PubMed ID: 30684235
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  • 16. PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor.
    Liu CP, Zhou QM, Fan DJ, Zhou JM.
    Int J Biochem Cell Biol; 2010 Jun 19; 42(6):890-901. PubMed ID: 20096367
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  • 17. Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD.
    Zoldák G, Schmid FX.
    J Mol Biol; 2011 Feb 11; 406(1):176-94. PubMed ID: 21147124
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  • 18. Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activity.
    Geitner AJ, Schmid FX.
    J Mol Biol; 2012 Jul 20; 420(4-5):335-49. PubMed ID: 22542528
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  • 19. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.
    Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N.
    Nature; 2004 Sep 30; 431(7008):590-6. PubMed ID: 15334087
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  • 20. NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function.
    Weininger U, Haupt C, Schweimer K, Graubner W, Kovermann M, Brüser T, Scholz C, Schaarschmidt P, Zoldak G, Schmid FX, Balbach J.
    J Mol Biol; 2009 Mar 27; 387(2):295-305. PubMed ID: 19356587
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