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

How to measure and predict the molar absorption coefficient of a protein

1995 • 3,771 citations

Molecular chaperones in cellular protein folding

1996 • 3,540 citations

The Hsp70 and Hsp60 Chaperone Machines

1998 • 2,793 citations

Analysis of gene control signals by DNA fusion and cloning in Escherichia coli

1980 • 2,499 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

Role of the Major Heat Shock Proteins as Molecular Chaperones

1993 • 1,096 citations

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

1991 • 853 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

GroE facilitates refolding of citrate synthase by suppressing aggregation

1991 • 486 citations

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

1994 • 461 citations

Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT

1998 • 423 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

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

Host participation in bacteriophage lambda head assembly

1973 • 381 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

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‐Mediated protein folding

1997 • 336 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

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

1996 • 249 citations

The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

1996 • 244 citations

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1998 • 226 citations

A new set of useful cloning and expression vectors derived from pBlueScript

1995 • 222 citations

ATP induces large quaternary rearrangements in a cage-like chaperonin structure

1993 • 212 citations

Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry

1994 • 199 citations

A structural model for GroEL–polypeptide recognition

1997 • 191 citations

Role of the Host Cell in Bacteriophage Morphogenesis: Effects of a Bacterial Mutation on T4 Head Assembly

1972 • 178 citations

Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin

1997 • 162 citations

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

1995 • 142 citations

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

1996 • 139 citations

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

1996 • 137 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

Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.

1986 • 127 citations

Refolding chromatography with immobilized mini-chaperones

1997 • 125 citations

The pRSET family of T7 promoter expression vectors for Escherichia coli

1993 • 113 citations

The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds

1989 • 104 citations

Renaturation of citrate synthase: Influence of denaturant and folding assistants

1992 • 103 citations

A thermodynamic coupling mechanism for GroEL-mediated unfolding.

1996 • 99 citations

Conformational States Bound by the Molecular Chaperones GroEL and SecB: A Hidden Unfolding (Annealing) Activity

1996 • 97 citations

Molecular Chaperones: Opening and closing the Anfinsen cage

1994 • 93 citations

Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL

1997 • 86 citations

Roles of molecular chaperones in protein folding

1994 • 77 citations

Role of the Major Heat Shock Proteins as Molecular Chaperones

1993 • 75 citations

Drifting Through the Year

1972 • 71 citations

Determination of Regions in the Dihydrofolate Reductase Structure That Interact with the Molecular Chaperonin GroEL

1996 • 69 citations

Significant hydrogen exchange protection in GroEL‐bound DHFR is maintained during iterative rounds of substrate cycling

1996 • 64 citations

Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth

1993 • 60 citations

Structural aspects of GroEl function

1998 • 58 citations

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

1995 • 52 citations

Structural and mechanistic consequences of polypeptide binding by GroEL

1997 • 43 citations

beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.

1996 • 39 citations

The 2.4 A crystal structure of the bacterial chaperonin GroEL complex with ATPγS

1996 • 29 citations

Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR

1997 • 26 citations