Literature DB >> 9285577

Protein folding. Folding with a two-stroke motor.

G Lorimer.   

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Year:  1997        PMID： 9285577     DOI： 10.1038/41892

Source DB:  PubMed          Journal:  Nature        ISSN： 0028-0836            Impact factor:   49.962


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  28 in total

1.  Chaperonin function: folding by forced unfolding.

Authors:  M Shtilerman; G H Lorimer; S W Englander
Journal:  Science       Date:  1999-04-30       Impact factor: 47.728

2.  GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism.

Authors:  P M Horowitz; G H Lorimer; J Ybarra
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-16       Impact factor: 11.205

3.  Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.

Authors:  Jaime Martín-Benito; Jasminka Boskovic; Paulino Gómez-Puertas; José L Carrascosa; C Torrey Simons; Sally A Lewis; Francesca Bartolini; Nicholas J Cowan; José M Valpuesta
Journal:  EMBO J       Date:  2002-12-02       Impact factor: 11.598

4.  A mobile loop order-disorder transition modulates the speed of chaperonin cycling.

Authors:  Frank Shewmaker; Michael J Kerner; Manajit Hayer-Hartl; Gracjana Klein; Costa Georgopoulos; Samuel J Landry
Journal:  Protein Sci       Date:  2004-07-06       Impact factor: 6.725

5.  The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein.

Authors:  Patrick J Bakkes; Bart W Faber; Harm van Heerikhuizen; Saskia M van der Vies
Journal:  Proc Natl Acad Sci U S A       Date:  2005-05-26       Impact factor: 11.205

6.  Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study.

Authors:  Begoña Sot; Fritzthof von Germar; Werner Mäntele; Jose María Valpuesta; Stefka G Taneva; Arturo Muga
Journal:  Protein Sci       Date:  2005-08-04       Impact factor: 6.725

7.  Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.

Authors:  Melissa Illingworth; Andrew Ramsey; Zhida Zheng; Lingling Chen
Journal:  J Biol Chem       Date:  2011-07-10       Impact factor: 5.157

8.  Residues in substrate proteins that interact with GroEL in the capture process are buried in the native state.

Authors:  George Stan; Bernard R Brooks; George H Lorimer; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  2006-03-14       Impact factor: 11.205

9.  GroEL stimulates protein folding through forced unfolding.

Authors:  Zong Lin; Damian Madan; Hays S Rye
Journal:  Nat Struct Mol Biol       Date:  2008-03-02       Impact factor: 15.369

10.  Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation.

Authors:  Riina Tehver; D Thirumalai
Journal:  J Mol Biol       Date:  2008-01-31       Impact factor: 5.469
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