(Q27932701)

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

Benjamin Bösl

series ordinal

1

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Valerie Grimminger

series ordinal

2

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Stefan Walter

series ordinal

3

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language of work or name

English

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publication date

18 November 2005

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published in

1 reference

1 December 2016

280

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page(s)

38170-6

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issue

46

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cites work

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Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

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Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

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AAA+ proteins and substrate recognition, it all depends on their partner in crime

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Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones

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The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

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Protein binding and disruption by Clp/Hsp100 chaperones

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The role of the ClpA chaperone in proteolysis by ClpAP

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Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

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HSP100/Clp proteins: a common mechanism explains diverse functions

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Protein disaggregation mediated by heat-shock protein Hsp104.

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The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites

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Subunit interactions influence the biochemical and biological properties of Hsp104

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Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants

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The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity

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Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

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Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein

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Characterization of a trap mutant of the AAA+ chaperone ClpB.

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AAA proteins. Lords of the ring

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Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity

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Roles of the two ATP binding sites of ClpB from Thermus thermophilus

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Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.

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

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Kinetics of molecular chaperone action

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N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion

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Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease.

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The ATPase activity of Hsp104, effects of environmental conditions and mutations.

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Substrate recognition by the AAA+ chaperone ClpB.

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The amino-terminal domain of ClpB supports binding to strongly aggregated proteins

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CONTIN: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations

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