Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes

Principles of Fluorescence Spectroscopy

1999 • 27,045 citations

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

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1988 • 1,316 citations

Principles of fluorescence spectroscopy

1984 • 1,031 citations

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

1991 • 853 citations

Labeling of proteins by reductive methylation using sodium cyanoborohydride.

1979 • 776 citations

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

1989 • 737 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

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

1979 • 426 citations

Purification and properties of the groES morphogenetic protein of Escherichia coli.

1986 • 364 citations

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

1994 • 334 citations

Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers

1989 • 321 citations

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1991 • 298 citations

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

1993 • 266 citations

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

1996 • 244 citations

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

1993 • 212 citations

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

1993 • 192 citations

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1991 • 190 citations

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1995 • 176 citations

Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP

1992 • 139 citations

The Hydrophobic Nature of GroEL-Substrate Binding

1995 • 135 citations

Refolding of Barnase in the Presence of GroE

1993 • 108 citations

Allosteric Control by ATP of Non-folded Protein Binding to GroEL

1996 • 105 citations

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

1994 • 92 citations

Hydrophobic Surfaces That Are Hidden in Chaperonin Cpn60 Can Be Exposed by Formation of Assembly-Competent Monomers or by Ionic Perturbation of the Oligomer

1995 • 80 citations

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted folding

1994 • 75 citations

Effect of Divalent Cations on the Molecular Structure of the GroEL Oligomer

1994 • 51 citations

Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.

1992 • 43 citations

Photoincorporation of 4,4'-Bis(1-anilino-8-naphthalenesulfonic Acid) into the Apical Domain of GroEL: Specific Information from a Nonspecific Probe

1995 • 37 citations

The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli Evidence for the existence of an unfolding intermediate state

1994 • 36 citations

Inactive GroEL Monomers Can Be Isolated and Reassembled to Functional Tetradecamers That Contain Few Bound Peptides

1995 • 33 citations

ATP induces non-identity of two rings in chaperonin GroEL.

1994 • 33 citations

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

1995 • 32 citations

The Chaperonin GroEL Is Destabilized by Binding of ADP

1995 • 22 citations

Ligand-induced Conformational Changes in the Apical Domain of the Chaperonin GroEL

1996 • 20 citations

Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers

1994 • 19 citations

A physical characterization of sulfane sulfurtransferase

1990 • 5 citations