The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Improved methods for building protein models in electron density maps and the location of errors in these models

1991 • 12,831 citations

The interpretation of protein structures: Estimation of static accessibility

1971 • 5,771 citations

Protein folding in the cell

1992 • 4,138 citations

Assessment of protein models with three-dimensional profiles

1992 • 3,317 citations

Improved Fourier coefficients for maps using phases from partial structures with errors

1986 • 1,897 citations

MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS

1993 • 1,591 citations

MOLECULAR CHAPERONES

1991 • 1,089 citations

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1989 • 933 citations

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

1991 • 853 citations

The structure of protein-protein recognition sites.

1990 • 825 citations

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

1989 • 737 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

Surface, subunit interfaces and interior of oligomeric proteins

1988 • 644 citations

A cytoplasmic chaperonin that catalyzes β-actin folding

1992 • 498 citations

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

1994 • 461 citations

Purification and properties of groE, a host protein involved in bacteriophage assembly

1979 • 426 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

MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement

1988 • 348 citations

Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL

1993 • 345 citations

A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1

1991 • 340 citations

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

1993 • 288 citations

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL

1992 • 285 citations

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

1993 • 266 citations

Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring.

1992 • 217 citations

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

1993 • 212 citations

Data collection and processing

2013 • 199 citations

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion

1993 • 192 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 yeast homolog to mouse Tcp-1 affects microtubule-mediated processes.

1991 • 175 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

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

1994 • 147 citations

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

1994 • 142 citations

Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

1993 • 117 citations

The structure of interfaces between subunits of dimeric and tetrameric proteins

1989 • 103 citations

The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state

1994 • 94 citations

Isomorphous replacement and anomalous scattering

2006 • 93 citations

A Normal Mitochondrial Protein is Selectively Synthesized and Accumulated During Heat Shock in Tetrahymena Thermophila

1987 • 88 citations

High molecular weight pea leaf protein similar to the groE protein of escherichia coli

1982 • 71 citations

The strongly conserved carboxyl‐terminus glycine‐methionine motif of the Escherichia coli GroEL chaperonin is dispensable

1993 • 66 citations

Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

1991 • 65 citations

A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophila.

1987 • 58 citations

Folding Intermediate Binds to the Bottom of Bullet-shaped Holo-chaperonin and is Readily Accessible to Antibody

1994 • 47 citations

The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography

1994 • 9 citations