Chaperone-client complexes: A dynamic liaison.

No abstract is available for this paper.

• Publication year

  2018

• Venue

  Journal of magnetic resonance (San Diego, Calif. 1997 : Print)

• Publication date

  2018-04-01

• Fields of study

  Biology, Medicine, Chemistry, Computer Science

• Identifiers
  DOI 10.1016/j.jmr.2017.12.008PMID 29544626
• 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.

• Folding while bound to chaperones.

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• The dynamic dimer structure of the chaperone Trigger Factor

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• Chaperone-client interactions: Non-specificity engenders multifunctionality

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• Author response: Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles

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• Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles

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• A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone.

  2017cited by this paper
• Conformational heterogeneity in the Hsp70 chaperone‐substrate ensemble identified from analysis of NMR‐detected titration data

  2017cited by this paper
• Structures of Large Protein Complexes Determined by Nuclear Magnetic Resonance Spectroscopy.

  2017cited by this paper
• Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins.

  2016cited by this paper
• Visualizing chaperone-assisted protein folding

  2016cited by this paper
• Forces Driving Chaperone Action.

  2016cited by this paper
• Skp is a multivalent chaperone of outer membrane proteins

  2016cited by this paper
• Hsp70 biases the folding pathways of client proteins

  2016cited by this paper
• Structural basis for the antifolding activity of a molecular chaperone

  2016cited by this paper
• Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling.

  2016cited by this paper
• A molecular mechanism of chaperone-client recognition

  2016cited by this paper
• Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor

  2016cited by this paper
• Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy.

  2016cited by this paper
• Visualizing chaperone-assisted protein folding

  2016cited by this paper
• Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone

  2015cited by this paper
• Protein folding occurs while bound to the ATP-independent chaperone Spy

  2015cited by this paper
• ClpB N-terminal domain plays a regulatory role in protein disaggregation

  2015cited by this paper
• Mapping the conformation of a client protein through the Hsp70 functional cycle

  2015cited by this paper
• Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR

  2015cited by this paper
• Substrate-binding domain conformational dynamics mediate Hsp70 allostery

  2015cited by this paper
• Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins

  2015cited by this paper
• Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.

  2015cited by this paper
• Revisiting the interaction between the chaperone Skp and lipopolysaccharide.

  2015cited by this paper
• Supplementary Materials for Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

  2014cited by this paper
• Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

  2014cited by this paper
• Modulation of the Hsp90 chaperone cycle by a stringent client protein.

  2014cited by this paper
• Super Spy variants implicate flexibility in chaperone action

  2014cited by this paper
• Structural mapping of a chaperone-substrate interaction surface.

  2014cited by this paper
• Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.

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• Multitasking SecB chaperones in bacteria

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• Dimeric Structure of the Bacterial Extracellular Foldase PrsA*

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• NMR approaches for structural analysis of multidomain proteins and complexes in solution.

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• Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins.

  2013cited by this paper
• Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction

  2013cited by this paper
• Structure and allostery of the chaperonin GroEL.

  2013cited by this paper
• Molecular chaperone functions in protein folding and proteostasis.

  2013cited by this paper
• Solution NMR studies of membrane-protein-chaperone complexes.

  2012cited by this paper
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  2012cited by this paper
• An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.

  2012cited by this paper
• Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.

  2011cited by this paper
• The client protein p53 forms a molten globule-like state in the presence of Hsp90

  2011cited by this paper
• Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

  2011cited by this paper
• Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single‐ring variant SR1 of the E. coli chaperonin GroEL

  2011cited by this paper
• Dynamic Interaction of Hsp90 with Its Client Protein p53.

  2011cited by this paper
• Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

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  2011cited by this paper
• β-Barrel membrane protein assembly by the Bam complex.

  2011cited by this paper
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  2011cited by this paper
• The heat shock response: life on the verge of death.

  2010cited by this paper
• HSP90 at the hub of protein homeostasis: emerging mechanistic insights

  2010cited by this paper
• The HSP70 chaperone machinery: J proteins as drivers of functional specificity

  2010cited by this paper
• Structure and function of the molecular chaperone Trigger Factor.

  2010cited by this paper
• Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

  2009cited by this paper
• GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side*

  2009cited by this paper
• Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands

  2009cited by this paper
• Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

  2009cited by this paper
• Allostery in Hsp70 chaperones is transduced by subdomain rotations.

  2009cited by this paper
• Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

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• Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

  2008cited by this paper
• Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

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• Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches.

  2007cited by this paper
• Direct Observation of Chaperone-Induced Changes in a Protein Folding Pathway

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• The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions.

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• Direct Comparison of a Stable Isolated Hsp70 Substrate-binding Domain in the Empty and Substrate-bound States*

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• A cradle for new proteins: trigger factor at the ribosome.

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  2005cited by this paper
• Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

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• NMR Study of Nucleotide-induced Changes in the Nucleotide Binding Domain of Thermus thermophilus Hsp70 Chaperone DnaK

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• SecB is a bona fide generalized chaperone in Escherichia coli.

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  2003cited by this paper
• Structural determinants of SecB recognition by SecA in bacterial protein translocation

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• How do Chaperones Bind (Partly) Unfolded Client Proteins?

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• Molecular chaperones and their denaturing effect on client proteins

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• Unveiling invisible protein states with NMR spectroscopy.

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• Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones

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• Chaperone-Bound Clients: The Importance of Being Dynamic.

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