Putting a lid on protein folding: structure and function of the co-chaperonin, GroES

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

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

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

1994 • 461 citations

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1996 • 436 citations

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

1995 • 423 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

Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction

1996 • 403 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

Characterization of a functionally important mobile domain of GroES

1993 • 222 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

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

Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae

1996 • 135 citations

Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB

1996 • 134 citations

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1995 • 130 citations

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.

1995 • 84 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

GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.

1993 • 64 citations

Interactions between the GroE Chaperonins and Rhodanese

1995 • 50 citations

Biochemical Characterization of Symmetric GroEL-GroES Complexes

1996 • 40 citations

A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL.

1992 • 38 citations

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

1995 • 33 citations