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Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

Data up to Jan 2025

Published1995
Citations423
References43

Total Citations Per Year

Abstract

References (43)

Protein folding in the cell

1992 • 4,138 citations

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

1994 • 1,322 citations

The Biology of heat shock proteins and molecular chaperones.

1994 • 1,226 citations

The biology of heat shock proteins and molecular chaperones

1994 • 1,203 citations

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1991 • 853 citations

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

1989 • 703 citations

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

1989 • 693 citations

Residues in chaperonin GroEL required for polypeptide binding and release

1994 • 645 citations

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

1993 • 593 citations

Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding

1994 • 461 citations

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

1992 • 412 citations

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1994 • 359 citations

Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy

1994 • 334 citations

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1991 • 298 citations

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

1993 • 288 citations

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding

1993 • 266 citations

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.

1990 • 250 citations

Characterization of a functionally important mobile domain of GroES

1993 • 222 citations

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1991 • 190 citations

Symmetric Complexes of GroE Chaperonins as Part of the Functional Cycle

1994 • 190 citations

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1991 • 189 citations

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

1986 • 181 citations

A polypeptide bound by the chaperonin groEL is localized within a central cavity.

1993 • 177 citations

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1995 • 176 citations

On the role of groES in the chaperonin-assisted folding reaction. Three case studies.

1994 • 166 citations

Positive cooperativity in the functioning of molecular chaperone GroEL.

1992 • 160 citations

Characterization of a Functional GroEL 14 (GroES 7 ) 2 Chaperonin Hetero-Oligomer

1994 • 154 citations

Specificity in chaperonin-mediated protein folding

1995 • 132 citations

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

Polypeptide Interactions with Molecular Chaperones and their Relationship to In Vivo Protein Folding

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

Chaperonin-mediated reconstitution of the phytochrome photoreceptor.

1993 • 33 citations

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Mechanism of GroEL action: Productive release of polypeptide from a sequestered position… (1995) – Cell | Metascience Observatory Explorer