Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli. - Wikidata - awgldk - TriplyDB

Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli.

Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli.

http://www.wikidata.org/entity/Q35749852

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Unscrambling an egg: protein disaggregation by AAA+ proteins Structural basis for intersubunit signaling in a protein disaggregating machine Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.Structure and function of the middle domain of ClpB from Escherichia coli.Aggregate reactivation mediated by the Hsp100 chaperones Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system.DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.ClpB/Hsp100 proteins and heat stress tolerance in plants.Characterization of human torsinA and its dystonia-associated mutant form.A systematic evaluation of the function of the protein-remodeling factor Hsp104 in [PSI+] prion propagation in S. cerevisiae by comprehensive chromosomal mutations.Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB.Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli.Dynamic structural states of ClpB involved in its disaggregation function.

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Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli.

http://www.wikidata.org/entity/Q35749852

description

2002 nî lūn-bûn

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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2002年论文

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2002年论文

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name

Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

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Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

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type

label

Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

@ast

Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

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prefLabel

Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

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Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

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Site-directed mutagenesis of c ...... in ClpB from Escherichia coli.

@en

P2093

Michal Zolkiewski

http://www.w3.org/2001/XMLSchema#string

Micheal E Barnett

http://www.w3.org/2001/XMLSchema#string

P2860

The structures of HsIU and the ATP-dependent protease HsIU-HsIV

Structure of the AAA ATPase p97

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein.

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome

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

An improved assay for nanomole amounts of inorganic phosphate

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

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11277-11283

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scholarly article

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10.1021/BI026161S

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37

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41

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2002-09-01T00:00:00Z

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11169642

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12220194

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1851691

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