Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent.

No abstract is available for this paper.

• Publication year

  1995

• Venue

  Biochimica et Biophysica Acta

• Publication date

  1995-03-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/0167-4838(94)00231-5PMID 7696310
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

  1994cited by this paper
• The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60).

  1993cited by this paper
• A comment on: ‘The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): Evidence for the presence of a single tryptophan’, by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9–12

  1993cited by this paper
• Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides

  1993cited by this paper
• Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

  1992cited by this paper
• Protein folding in the cell

  1992cited by this paper
• Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.

  1991cited by this paper
• GroE facilitates refolding of citrate synthase by suppressing aggregation.

  1991cited by this paper
• Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase.

  1991cited by this paper
• Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast.

  1991cited by this paper
• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

  1991cited by this paper
• Binding of a chaperonin to the folding intermediates of lactate dehydrogenase.

  1991cited by this paper
• (Mg–ATP)-dependent self-assembly of molecular chaperone GroEL

  1990cited by this paper
• Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

  1990cited by this paper
• The Escherichia coli groE chaperonins.

  1990cited by this paper
• The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta‐lactamase precursor.

  1990cited by this paper
• GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

  1989cited by this paper
• Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

  1989cited by this paper
• Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein

  1988cited by this paper
• Purification and properties of the groES morphogenetic protein of Escherichia coli.

  1986cited by this paper
• Purification and properties of groE, a host protein involved in bacteriophage assembly.

  1979cited by this paper
• Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly.

  1979cited by this paper
• Boundary analysis of sedimentation‐velocity experiments with monodisperse and paucidisperse solutes

  1978cited by this paper
• Purification of thiosulfate sulfurtransferase by selective immobilization on blue agarose.

  1978cited by this paper
• The covalent and tertiary structure of bovine liver rhodanese

  1978cited by this paper
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

  1970cited by this paper
• Crystalline Rhodanese. I. Purification and Physicochemical Examination.

  1953cited by this paper

• From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study

  2023cites this paper
• Improvement of structural stability and functional efficiency of chaperonin GroEL mediated by mixed salt.

  2019cites this paper
• Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition

  2014cites this paper
• Molecular chaperone GroEL/ES: Unfolding and refolding processes

  2013cites this paper
• Hydrogen peroxide induces the dissociation of GroEL into monomers that can facilitate the reactivation of oxidatively inactivated rhodanese.

  2004cites this paper
• Denaturation and reassembly of chaperonin GroEL studied by solution X‐ray scattering

  2003cites this paper
• Direct detection of the protein quaternary structure and denatured entity by small-angle scattering: guanidine hydrochloride denaturation of chaperonin protein GroEL

  2002cites this paper
• Assembly of chaperonin complexes

  2001influential citation
• Excluded Volume Effects on the Refolding and Assembly of an Oligomeric Protein

  2001cites this paper
• Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model.

  1999cites this paper
• Nucleotide and Mg2+ Induced Conformational Changes in GroEL can be Detected by Sulfhydryl Labeling

  1999cites this paper
• Inactive GroEL Monomers Can Be Isolated and Reassembled to Functional Tetradecamers That Contain Few Bound Peptides (*)

  1995cites this paper
• Refolding and Reassembly of Active Chaperonin GroEL After Denaturation (*)

  1995cites this paper
• The Chaperonin GroEL Is Destabilized by Binding of ADP (*)

  1995cites this paper