Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
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Abstract
References (43)
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A polypeptide bound by the chaperonin groEL is localized within a central cavity.
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Specificity in chaperonin-mediated protein folding
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Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds
1995 • 130 citations
Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP.
1992 • 115 citations
The formation of symmetrical GroEL‐GroES complexes in the presence of ATP
1994 • 90 citations
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1994 • 83 citations
Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.
1994 • 75 citations
Structure of holo‐chaperonin studied with electron microscopy Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each
1992 • 73 citations
Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES
1994 • 73 citations
GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.
1993 • 64 citations
Purification of ornithine transcarbamylase from rat liver by affinity chromatography with immobilized transition-state analog
1980 • 58 citations
Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
1995 • 52 citations
Folding Intermediate Binds to the Bottom of Bullet-shaped Holo-chaperonin and is Readily Accessible to Antibody
1994 • 47 citations
A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL.
1992 • 38 citations
Restriction map of 5S RNA genes of Drosophila melanogaster
1976 • 36 citations
Stability of the Asymmetric Escherichia coli Chaperonin Complex
1995 • 35 citations
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