Football- and Bullet-shaped GroEL-GroES Complexes Coexist during the Reaction Cycle*♦

No abstract is available for this paper.

• Publication year

  2008

• Venue

  Journal of Biological Chemistry

• Publication date

  2008-08-29

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1074/jbc.M802541200PMID 18567585PMCID PMC3259762
• 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.

• Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.

  2008cited by this paper
• Fast‐scanning atomic force microscopy reveals the ATP/ADP‐dependent conformational changes of GroEL

  2006cited by this paper
• GroEL‐GroES‐mediated protein folding

  2006cited by this paper
• Allosteric signaling of ATP hydrolysis in GroEL–GroES complexes

  2006cited by this paper
• Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes

  2005cited by this paper
• BeFx Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers*

  2004cited by this paper
• GroEL mediates protein folding with a two successive timer mechanism.

  2004cited by this paper
• Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 → Ala

  2003cited by this paper
• Discrimination of ATP, ADP, and AMPPNP by Chaperonin GroEL

  2003cited by this paper
• Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis.

  2003cited by this paper
• Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

  2002cited by this paper
• Structure and function of the GroE chaperone

  2002cited by this paper
• ATP-bound states of GroEL captured by cryo-electron microscopy.

  2001cited by this paper
• Single-molecule observation of protein–protein interactions in the chaperonin system

  2001cited by this paper
• Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction.

  2001cited by this paper
• Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.

  2000cited by this paper
• Catalysis, commitment and encapsulation during GroE-mediated folding.

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

  1999cited by this paper
• A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.

  1999cited by this paper
• The Hsp70 and Hsp60 chaperone machines.

  1998cited by this paper
• Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

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

  1997cited by this paper
• Conditions for Nucleotide-dependent GroES-GroEL Interactions

  1997cited by this paper
• Fluorescence Detection of Symmetric GroEL14(GroES7)2 Heterooligomers Involved in Protein Release during the Chaperonin Cycle*

  1996cited by this paper
• GroEL Locked in a Closed Conformation by an Interdomain Cross-link Can Bind ATP and Polypeptide but Cannot Process Further Reaction Steps*

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

  1996cited by this paper
• Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

  1995cited by this paper
• Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes

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

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

  1995cited by this paper
• Symmetric complexes of GroE chaperonins as part of the functional cycle.

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

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

  1994cited by this paper
• Positive cooperativity in the functioning of molecular chaperone GroEL.

  1992cited by this paper
• Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology.

  1990cited by this paper
• Protein measurement with the Folin phenol reagent.

  1951cited by this paper

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  2026cites this paper
• From Microstates to Macrostates in the Conformational Dynamics of GroEL: a Single-Molecule FRET Study

  2023cites this paper
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  2023cites this paper
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  2021cites this paper
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  2020cites this paper
• [Analysis and Discovery of Functional Biomolecules Using a Combination of Fluorescence Microscopy and Micro- and Nano-devices for Single-molecule Detection].

  2020cites this paper
• Mechanisms of folding, assembly and remodelling chaperones

  2018cites this paper
• Physicochemical Properties of the Mammalian Molecular Chaperone HSP60

  2018cites this paper
• Functionally Significant Amino Acid Motifs of Heat Shock Proteins: Structural and Bioinformatics Analyses of Hsp60/Hsp10 in Five Classes of Chordata

  2018cites this paper
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  2018cites this paper
• A Glimpse Into the Structure and Function of Atypical Type I Chaperonins

  2018cites this paper
• GroEL Ring Separation and Exchange in the Chaperonin Reaction.

  2018cites this paper
• Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis

  2018cites this paper
• Electron microscopic and physicobiochemical studies of chaperonin GroEL and GroES complexes

  2017cites this paper
• GroEL and the GroEL-GroES Complex.

  2017cites this paper
• Title Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein

  2016cites this paper
• The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding.

  2016cites this paper
• Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle

  2016cites this paper
• Chaperonin GroEL-GroES Functions as both Alternating and Non-Alternating Engines.

  2016cites this paper
• Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins

  2016cites this paper
• IDENTIFICATION OF AMINO ACIDS INVOLVED IN THE MOONLIGHTING FUNCTIONS OF HTPB, THE LEGIONELLA PNEUMOPHILA CHAPERONIN

  2016cites this paper
• Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein*

  2015cites this paper
• Crystal structure of the human mitochondrial chaperonin symmetrical football complex

  2015cites this paper
• Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.

  2015cites this paper
• Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.

  2015cites this paper
• The Chaperonin GroEL Switches the Reaction Cycles in Response to the Concentration of Denatured Proteins

  2014cites this paper
• Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form

  2014cites this paper
• Structural Fluctuations of the Escherichia coli Co-chaperonin GroES Studied by the Hydrogen/Deuterium-Exchange Methods

  2014cites this paper
• Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.

  2014cites this paper
• Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange

  2013cites this paper
• Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine

  2013cites this paper
• An Analysis of the Stability, Aggregation Propensity, and Negative Cooperativity of the Escherichia coli Chaperonin GroEL

  2013cites this paper
• Anisotropic intersubunit and inter-ring interactions revealed in the native bullet-shaped chaperonin complex from Thermus thermophilus.

  2013cites this paper
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  2013cites this paper
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  2013cites this paper
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  2013cites this paper
• Repetitive Protein Unfolding by the trans Ring of the GroEL-GroES Chaperonin Complex Stimulates Folding*

  2013cites this paper
• Single-molecule Observation of Protein Folding in Symmetric GroEL-(GroES)2 Complexes*

  2012cites this paper
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  2012cites this paper
• Single-molecule Study on the Decay Process of the Football-shaped GroEL-GroES Complex Using Zero-mode Waveguides*

  2010cites this paper
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  2010cites this paper
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  2010cites this paper
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  2009cites this paper
• Probing Open Conformation of GroEL Rings by Cross-linking Reveals Single and Double Open Ring Structures of GroEL in ADP and ATP

  2009cites this paper
• GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future.

  2009cites this paper
• Reconciling theories of chaperonin accelerated folding with experimental evidence

  2009cites this paper
• Structure of the Chaperonin-Substrate Complex

  2009cites this paper
• Disaggregating chaperones: an unfolding story.

  2009cites this paper
• Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant*♦

  2008cites this paper