Structure and function of the GroE chaperone

No abstract is available for this paper.

• Publication year

  2002

• Venue

  Cellular and Molecular Life Sciences (CMLS)

• Publication date

  2002-10-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1007/PL00012485PMID 12475168PMCID PMC11337506
• 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.

• Molecular chaperones--cellular machines for protein folding.

  2002cited by this paper
• Chaperonin-mediated protein folding.

  2001cited by this paper
• Review: a structural view of the GroE chaperone cycle.

  2001cited by this paper
• Structural changes in GroEL effected by binding a denatured protein substrate.

  2001cited by this paper
• A personal account of chaperonin history.

  2001cited by this paper
• Review: allostery in chaperonins.

  2001cited by this paper
• Folding of malate dehydrogenase inside the GroEL–GroES cavity

  2001cited by this paper
• The Importance of a Mobile Loop in Regulating Chaperonin/ Co-chaperonin Interaction

  2001cited by this paper
• GroEL/GroES-mediated folding of a protein too large to be encapsulated.

  2001cited by this paper
• Dual function of protein confinement in chaperonin-assisted protein folding.

  2001cited by this paper
• Limits of Protein Folding Inside GroE Complexes*

  2000cited by this paper
• Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

  2000cited by this paper
• GroEL Binds Artificial Proteins with Random Sequences*

  2000cited by this paper
• Chaperonin function: folding by forced unfolding.

  1999cited by this paper
• GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.

  1999cited by this paper
• On the Maximum Size of Proteins to Stay and Fold in the Cavity of GroEL underneath GroES*

  1999cited by this paper
• Identification of in vivo substrates of the chaperonin GroEL

  1999cited by this paper
• The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity.

  1999cited by this paper
• On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein Folding

  1999cited by this paper
• Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.

  1999cited by this paper
• Basis of substrate binding by the chaperonin GroEL.

  1999cited by this paper
• The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

  1999cited by this paper
• Structure and function in GroEL-mediated protein folding.

  1998cited by this paper
• Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non‐identical requirement for hsp60 and hsp10

  1998cited by this paper
• Protein aggregation: folding aggregates, inclusion bodies and amyloid.

  1998cited by this paper
• Protein misassembly in vitro.

  1997cited by this paper
• The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

  1997cited by this paper
• In vivo observation of polypeptide flux through the bacterial chaperonin system.

  1997cited by this paper
• How GroES Regulates Binding of Nonnative Protein to GroEL*

  1997cited by this paper
• Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction*

  1997cited by this paper
• Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

  1997cited by this paper
• Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.

  1997cited by this paper
• GroEL‐Mediated protein folding

  1997cited by this paper
• Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

  1997cited by this paper
• Catalysis of protein folding by symmetric chaperone complexes.

  1997cited by this paper
• A structural model for GroEL-polypeptide recognition.

  1997cited by this paper
• Effect of GroEL on the re-folding kinetics of alpha-lactalbumin.

  1996cited by this paper
• A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo

  1996cited by this paper
• The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

  1996cited by this paper
• Characterization of the Active Intermediate of a GroEL – GroES-Mediated Protein Folding Reaction

  1996cited by this paper
• The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.

  1996cited by this paper
• The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

  1996cited by this paper
• A thermodynamic coupling mechanism for GroEL-mediated unfolding.

  1996cited by this paper
• Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction.

  1996cited by this paper
• The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

  1996cited by this paper
• Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB

  1996cited by this paper
• Protein folding in the central cavity of the GroEL–GroES chaperonin complex

  1996cited by this paper
• Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.

  1996cited by this paper
• Release of both native and non-native proteins from a cis-only GroEL ternary complex

  1996cited by this paper
• The origins and consequences of asymmetry in the chaperonin reaction cycle.

  1995cited by this paper
• The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.

  1995cited by this paper
• Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding

  1995cited by this paper
• Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

  1995cited by this paper
• Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.

  1995cited by this paper
• The Hydrophobic Nature of GroEL-Substrate Binding (*)

  1995cited by this paper
• Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.

  1995cited by this paper
• Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

  1995cited by this paper
• Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

  1994cited by this paper
• The formation of symmetrical GroEL‐GroES complexes in the presence of ATP

  1994cited by this paper
• Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy

  1994cited by this paper
• GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms.

  1994cited by this paper
• Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

  1994cited by this paper
• Symmetric complexes of GroE chaperonins as part of the functional cycle.

  1994cited by this paper
• Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.

  1994cited by this paper
• Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.

  1994cited by this paper
• Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

  1994cited by this paper
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

  1994cited by this paper
• Residues in chaperonin GroEL required for polypeptide binding and release

  1994cited by this paper
• A polypeptide bound by the chaperonin groEL is localized within a central cavity.

  1993cited by this paper
• Characterization of a functionally important mobile domain of GroES

  1993cited by this paper
• Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

  1993cited by this paper
• Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

  1992cited by this paper
• Interaction of GroE with an all-beta-protein.

  1992cited by this paper
• Positive cooperativity in the functioning of molecular chaperone GroEL.

  1992cited by this paper
• Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

  1992cited by this paper
• Binding of chaperonins

  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
• The chaperonin GroEL binds a polypeptide in an alpha-helical conformation.

  1991cited by this paper
• Cooperativity in ATP hydrolysis by GroEL is increased by GroES

  1991cited by this paper
• GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

  1989cited by this paper
• The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

  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
• 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
• Host participation in bacteriophage lambda head assembly.

  1973cited by this paper

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  2020cites this paper
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  2018cites this paper
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  2017cites this paper
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  2017cites this paper
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  2017cites this paper
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  2017cites this paper
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• A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.

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