Successive action of Escherichia coli chaperones in vivo (original) (raw)
Protein folding in Escherichia coli: the chaperonin GroE and its substrates
Vollodymyr Yerko
Research in Microbiology, 2009
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The chaperonin GroEL and other heat-shock proteins, besides DnaK, participate in ribosome biogenesis in Escherichia coli
Aziz Hage
Molecular and General Genetics, 2001
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Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
Manajit Hayer-Hartl
Cell, 2005
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The 70-kDa Heat-Shock Protein/DnaK Chaperone System is Required for the Productive Folding of Ribulose-Bisphosphate Carboxylase Subunits in Escherichia Coli
Susana Checa
European Journal of Biochemistry, 1997
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Molecular Chaperones involved in Heterologous Protein Folding in Escherichia coli
Eriola Betiku
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Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins
Ron Unger
Bioinformatics, 2007
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Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
Alexander Gragerov
Proceedings of the National Academy of Sciences, 1992
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Chaperone-mediated protein folding
Andreas Plückthun
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A Novel Function of Escherichia coli Chaperone DnaJ
Al Maghfirah chanel
Journal of Biological Chemistry, 1995
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SecB is a bona fide generalized chaperone in Escherichia coli
F. Schwager
Proceedings of the National Academy of Sciences, 2004
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Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli
F. Schwager
Proceedings of the National Academy of Sciences, 2007
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Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
Shannon Doyle
Proceedings of the National Academy of Sciences of the United States of America, 2011
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Unique unfoldase/aggregase activity of a molecular chaperone that dysregulates a translational elongation factor
Kyoung-Seok Ryu
2018
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DnaK functions as a central hub in the E. coli chaperone network
Manajit Hayer-Hartl
Cell Reports, 2012
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The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor
Andreas Plückthun
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Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
Axel Mogk, Toshifumi Tomoyasu
Molecular Microbiology, 2001
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Catalysis of protein folding by symmetric chaperone complexes
Helmut Sparrer
Proceedings of the …, 1997
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mRNA Engineering for the Efficient Chaperone-Mediated Co-Translational Folding of Recombinant Proteins in Escherichia coli
almando geraldi
International Journal of Molecular Sciences
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The role of molecular chaperones in protein folding
Florian Georgescauld
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1995
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Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
Heather Hundley, Renee Wegrzyn
Molecular Microbiology, 2005
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Role of Molecular Chaperones in Protein Folding
Manajit Hayer-Hartl
Current and Emerging Principles and Therapies, 2010
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The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli
Manajit Hayer-Hartl
Cell Reports, 2019
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The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
Bogdan Banecki
The EMBO journal, 1995
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Physical map and dynamics of the chaperone network in Escherichia coli
mohit kumar
Molecular microbiology, 2012
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Catalysis of protein folding by chaperones in pathogenic bacteria
Jerome Pinkner
Proceedings of the National Academy of Sciences, 2004
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A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32
Toshifumi Tomoyasu
The EMBO journal, 1996
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Concerted Action of the Ribosome and the Associated Chaperone Trigger Factor Confines Nascent Polypeptide Folding
Annemarie Becker
Molecular Cell, 2012
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Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery
Nam Lam
Protein Science, 2012
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Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude ofEscherichia coliproteins
George Lorimer
Protein Science, 2008
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A Set of pBR322-Compatible Plasmids Allowing the Testing of Chaperone-Assisted Folding of Proteins Overexpressed inEscherichia coli
Hélène Bergès
Analytical Biochemistry, 1997
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