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329 related items for PubMed ID: 21147124

  • 1. 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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  • 3. Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding.
    Knappe TA, Eckert B, Schaarschmidt P, Scholz C, Schmid FX.
    J Mol Biol; 2007 May 18; 368(5):1458-68. PubMed ID: 17397867
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  • 4. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities.
    Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid FX.
    Biochemistry; 2006 Jan 10; 45(1):20-33. PubMed ID: 16388577
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  • 6. 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 10; 42(6):890-901. PubMed ID: 20096367
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  • 9. The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client protein.
    Zoldák G, Geitner AJ, Schmid FX.
    J Am Chem Soc; 2013 Mar 20; 135(11):4372-9. PubMed ID: 23445547
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  • 11. Binding specificity of Escherichia coli trigger factor.
    Patzelt H, Rüdiger S, Brehmer D, Kramer G, Vorderwülbecke S, Schaffitzel E, Waitz A, Hesterkamp T, Dong L, Schneider-Mergener J, Bukau B, Deuerling E.
    Proc Natl Acad Sci U S A; 2001 Dec 04; 98(25):14244-9. PubMed ID: 11724963
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  • 12. Transient enzyme-substrate recognition monitored by real-time NMR.
    Haupt C, Patzschke R, Weininger U, Gröger S, Kovermann M, Balbach J.
    J Am Chem Soc; 2011 Jul 27; 133(29):11154-62. PubMed ID: 21661729
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  • 20. NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
    Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Rüterjans H, Griesinger C, Fiebig KM.
    J Mol Biol; 2002 May 10; 318(4):1097-115. PubMed ID: 12054805
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