Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli-Reference-Cited by-同舟云学术

Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

Published:2005-07 Issue:2 Volume:122 Page:209-220
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Kerner Michael J.,Naylor Dean J.,Ishihama Yasushi,Maier Tobias,Chang Hung-Chun,Stines Anna P.,Georgopoulos Costa,Frishman Dmitrij,Hayer-Hartl Manajit,Mann Matthias,Hartl F. Ulrich

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference40 articles.

1. Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed;Agashe;Cell,2004

2. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å;Braig;Nature,1994

3. Dual function of protein confinement in chaperonin-assisted protein folding;Brinker;Cell,2001

4. GroEL/GroES-mediated folding of a protein too large to be encapsulated;Chaudhuri;Cell,2001

5. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases;Chiti;Proc. Natl. Acad. Sci. USA,2002

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