Literature DB >> 1685325

Molecular chaperones: individualists or groupies?

M J Gething1.   

Abstract

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Year:  1991        PMID： 1685325     DOI： 10.1016/0955-0674(91)90030-3

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN： 0955-0674            Impact factor:   8.382


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  6 in total

1.  Modeling Hsp70-mediated protein folding.

Authors:  Bin Hu; Matthias P Mayer; Masaru Tomita
Journal:  Biophys J       Date:  2006-04-28       Impact factor: 4.033

2.  The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.

Authors:  H Y Lin; P Masso-Welch; Y P Di; J W Cai; J W Shen; J R Subjeck
Journal:  Mol Biol Cell       Date:  1993-11       Impact factor: 4.138

3.  Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin.

Authors:  Y Gao; I E Vainberg; R L Chow; N J Cowan
Journal:  Mol Cell Biol       Date:  1993-04       Impact factor: 4.272

4.  Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

Authors:  M Ehrnsperger; S Gräber; M Gaestel; J Buchner
Journal:  EMBO J       Date:  1997-01-15       Impact factor: 11.598

Review 5.  Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates.

Authors:  Chamithi Karunanayake; Richard C Page
Journal:  Exp Biol Med (Maywood)       Date:  2021-03-17

6.  The roles of the rod end and the tail in vimentin IF assembly and IF network formation.

Authors:  M B McCormick; P Kouklis; A Syder; E Fuchs
Journal:  J Cell Biol       Date:  1993-07       Impact factor: 10.539
  6 in total

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