Literature DB >> 26604310

Reply to Marchenko et al.: Flux analysis of GroEL-assisted protein folding/unfolding.

David S Libich1, Vitali Tugarinov1, G Marius Clore2.   

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Year:  2015        PMID： 26604310      PMCID： PMC4687547          DOI： 10.1073/pnas.1520474112

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


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  5 in total

1.  Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps.

Authors:  Natalia Y Marchenko; Victor V Marchenkov; Gennady V Semisotnov; Alexei V Finkelstein
Journal:  Proc Natl Acad Sci U S A       Date:  2015-11-24       Impact factor: 11.205

2.  [The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure].

Authors:  V V Marchenkov; I V Sokolovskiĭ; N V Kotova; O V Galzitskaya; E S Bochkareva; A S Girshovich; G V Semisotnov
Journal:  Biofizika       Date:  2004 Nov-Dec

3.  Conformational selection or induced fit: a flux description of reaction mechanism.

Authors:  Gordon G Hammes; Yu-Chu Chang; Terrence G Oas
Journal:  Proc Natl Acad Sci U S A       Date:  2009-07-30       Impact factor: 11.205

4.  Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.

Authors:  David S Libich; Vitali Tugarinov; G Marius Clore
Journal:  Proc Natl Acad Sci U S A       Date:  2015-06-29       Impact factor: 11.205

5.  In vivo activities of GroEL minichaperones.

Authors:  J Chatellier; F Hill; P A Lund; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1998-08-18       Impact factor: 11.205
  5 in total
  1 in total

Review 1.  NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.

Authors:  Vitali Tugarinov; Alberto Ceccon; G Marius Clore
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2021-11-02       Impact factor: 9.795
  1 in total

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