Literature DB >> 16249079

Allosteric regulation of chaperonins.

Amnon Horovitz1, Keith R Willison.   

Abstract

Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling between allosteric transitions and protein folding reactions. However, various mechanistic issues remain to be resolved.

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Year:  2005        PMID: 16249079     DOI: 10.1016/j.sbi.2005.10.001

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  57 in total

1.  Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations.

Authors:  Gabriel A Frank; Mila Goomanovsky; Amit Davidi; Guy Ziv; Amnon Horovitz; Gilad Haran
Journal:  Proc Natl Acad Sci U S A       Date:  2010-03-22       Impact factor: 11.205

Review 2.  Chaperone machines for protein folding, unfolding and disaggregation.

Authors:  Helen Saibil
Journal:  Nat Rev Mol Cell Biol       Date:  2013-09-12       Impact factor: 94.444

Review 3.  The substrate specificity of eukaryotic cytosolic chaperonin CCT.

Authors:  Keith R Willison
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2018-06-19       Impact factor: 6.237

4.  Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.

Authors:  Oded Danziger; Liat Shimon; Amnon Horovitz
Journal:  Protein Sci       Date:  2006-05-02       Impact factor: 6.725

5.  Dynamics of allosteric transitions in GroEL.

Authors:  Changbong Hyeon; George H Lorimer; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-29       Impact factor: 11.205

6.  The inter-ring arrangement of the cytosolic chaperonin CCT.

Authors:  Jaime Martín-Benito; Julie Grantham; Jasminka Boskovic; Karen I Brackley; José L Carrascosa; Keith R Willison; José M Valpuesta
Journal:  EMBO Rep       Date:  2007-02-16       Impact factor: 8.807

7.  Communication over the network of binary switches regulates the activation of A2A adenosine receptor.

Authors:  Yoonji Lee; Sun Choi; Changbong Hyeon
Journal:  PLoS Comput Biol       Date:  2015-02-09       Impact factor: 4.475

8.  Using affinity chromatography to engineer and characterize pH-dependent protein switches.

Authors:  Martin Sagermann; Richard R Chapleau; Elaine DeLorimier; Margarida Lei
Journal:  Protein Sci       Date:  2009-01       Impact factor: 6.725

9.  The ClpP N-terminus coordinates substrate access with protease active site reactivity.

Authors:  Laura D Jennings; Jen Bohon; Mark R Chance; Stuart Licht
Journal:  Biochemistry       Date:  2008-09-25       Impact factor: 3.162

10.  Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases.

Authors:  Jin Liu; Ruth Nussinov
Journal:  J Mol Biol       Date:  2010-01-18       Impact factor: 5.469

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