Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
Top Cited Papers
Open Access
- 1 July 2005
- Vol. 122 (2), 209-220
- https://doi.org/10.1016/j.cell.2005.05.028
Abstract
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This publication has 40 references indexed in Scilit:
- Function of Trigger Factor and DnaK in Multidomain Protein FoldingCell, 2004
- Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseasesProceedings of the National Academy of Sciences, 2002
- Dual Function of Protein Confinement in Chaperonin-Assisted Protein FoldingCell, 2001
- GroEL/GroES-Mediated Folding of a Protein Too Large to Be EncapsulatedCell, 2001
- Trigger factor and DnaK cooperate in folding of newly synthesized proteinsNature, 1999
- Protein Folding: A Perspective from Theory and ExperimentAngewandte Chemie International Edition, 1998
- In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin SystemCell, 1997
- Protein folding in the cell: competing models of chaperonin functionThe FASEB Journal, 1996
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperaturesJournal of Bacteriology, 1989