Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1991 • 14,222 citations

Protein folding in the cell

1992 • 4,138 citations

Molecular chaperones in cellular protein folding

1996 • 3,540 citations

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

1994 • 1,322 citations

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

1997 • 1,250 citations

[5] Avidin and streptavidin

1990 • 1,005 citations

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

1991 • 853 citations

Protein Folding: A Perspective from Theory and Experiment

1998 • 840 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

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

1998 • 576 citations

Effects of macromolecular crowding on protein folding and aggregation

1999 • 506 citations

Identification of in vivo substrates of the chaperonin GroEL

1999 • 499 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

Chaperonin-Mediated Protein Folding

2001 • 407 citations

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

1997 • 406 citations

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

1996 • 403 citations

The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL

1996 • 385 citations

Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent

1990 • 384 citations

Protein folding in the central cavity of the GroEL–GroES chaperonin complex

1996 • 373 citations

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

1994 • 359 citations

Principles of protein folding in the cellular environment

1999 • 349 citations

Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL

1993 • 345 citations

In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

1997 • 345 citations

GroEL-GroES Cycling

1999 • 303 citations

Chaperonin Function: Folding by Forced Unfolding

1999 • 294 citations

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.

1996 • 249 citations

Protein folding in the cell: competing models of chaperonin function

1996 • 238 citations

A computational approach to simplifying the protein folding alphabet.

1999 • 230 citations

Confinement as a determinant of macromolecular structure and reactivity

1992 • 192 citations

Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL

2000 • 191 citations

Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms

1997 • 174 citations

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

1994 • 166 citations

Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin.

1994 • 147 citations

Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity

1999 • 143 citations

Asymmetrical Interaction of GroEL and GroES in the ATPase Cycle of Assisted Protein Folding

1995 • 142 citations

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1996 • 137 citations

Cloning and expression of the Rhodospirillum rubrum ribulosebisphosphate carboxylase gene in E. coli

1984 • 137 citations

The effect of macromolecular crowding on chaperonin-mediated protein folding

1997 • 117 citations

Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins

2000 • 116 citations

GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine

1998 • 111 citations

The ins and outs of a molecular chaperone machine

1998 • 110 citations

Conformational states of ribulose bisphosphate carboxylase and their interaction with chaperonin 60

1992 • 108 citations

To Fold or Not to Fold . . .

1993 • 94 citations

Molecular Chaperones: Opening and closing the Anfinsen cage

1994 • 93 citations

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

1997 • 92 citations

Catalysis of protein folding by symmetric chaperone complexes

1997 • 84 citations

Folding of malate dehydrogenase inside the GroEL-GroES cavity.

2001 • 84 citations

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.

1996 • 82 citations

Functional Significance of Symmetrical Versus Asymmetrical GroEL-GroES Chaperonin Complexes

1995 • 81 citations

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

1979 • 79 citations

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

1998 • 77 citations

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

1999 • 68 citations

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.

1995 • 64 citations

Structural and mechanistic consequences of polypeptide binding by GroEL

1997 • 43 citations

GroEL–Substrate Interactions

2000 • 39 citations

Examination of the intersubunit interaction between glutamate-48 and lysine-168 of ribulose-bisphosphate carboxylase/oxygenase by site-directed mutagenesis.

1990 • 21 citations

The Dimerization of Folded Monomers of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase

2001 • 7 citations