The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites.
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Unscrambling an egg: protein disaggregation by AAA+ proteinsThe Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium ChlorideStructural Dynamics of the MecA-ClpC Complex: A TYPE II AAA+ PROTEIN UNFOLDING MACHINEElements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motorAnalysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationCooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.Orientation of the amino-terminal domain of ClpB affects the disaggregation of the proteinRoles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilusAnalysis of gene order data supports vertical inheritance of the leukotoxin operon and genome rearrangements in the 5' flanking region in genus Mannheimia.ClpB chaperone passively threads soluble denatured proteins through its central pore.trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteinsAsymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.Stability and interactions of the amino-terminal domain of ClpB from Escherichia coliSite-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli.On the design of broad based screening assays to identify potential pharmacological chaperones of protein misfolding diseasesCryo electron microscopy structures of Hsp100 proteins: crowbars in or out?Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangementFusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1.Allosteric communication between the nucleotide binding domains of caseinolytic peptidase B.Mutant Analysis Reveals Allosteric Regulation of ClpB DisaggregaseRoles of the two ClpC ATP binding sites in the regulation of competence and the stress response.Roles of the two ATP binding sites of ClpB from Thermus thermophilus.ATP-dependent hexameric assembly of the heat shock protein Hsp101 involves multiple interaction domains and a functional C-proximal nucleotide-binding domain.The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity.Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.Characterization of a trap mutant of the AAA+ chaperone ClpB.Poly-L-lysine enhances the protein disaggregation activity of ClpB.Substrate recognition by the AAA+ chaperone ClpB.Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides.Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity.ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2.VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase.Examination of the dynamic assembly equilibrium for E. coli ClpB.A tightly regulated molecular toggle controls AAA+ disaggregase.Dynamic structural states of ClpB involved in its disaggregation function.Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms.
P2860
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P2860
The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The chaperone function of ClpB ...... of its two ATP-binding sites.
@ast
The chaperone function of ClpB ...... of its two ATP-binding sites.
@en
type
label
The chaperone function of ClpB ...... of its two ATP-binding sites.
@ast
The chaperone function of ClpB ...... of its two ATP-binding sites.
@en
prefLabel
The chaperone function of ClpB ...... of its two ATP-binding sites.
@ast
The chaperone function of ClpB ...... of its two ATP-binding sites.
@en
P2093
P356
P1476
The chaperone function of ClpB ...... of its two ATP-binding sites.
@en
P2093
P304
P356
10.1006/JMBI.2001.4455
P407
P577
2001-03-01T00:00:00Z