Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.
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Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinAEffect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutantA virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatusUnscrambling an egg: protein disaggregation by AAA+ proteinsMolecular chaperones: guardians of the proteome in normal and disease statesDisaggregases, molecular chaperones that resolubilize protein aggregatesThe Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.Molecular Basis for the Unique Role of the AAA+ Chaperone ClpV in Type VI Protein SecretionStructural basis for intersubunit signaling in a protein disaggregating machineHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationPspF-binding domain PspA1-144 and the PspA·F complex: New insights into the coiled-coil-dependent regulation of AAA+ proteinsSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationSubstrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S maturationCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationTorsins: not your typical AAA+ ATPasesMoyamoya disease-associated protein mysterin/RNF213 is a novel AAA+ ATPase, which dynamically changes its oligomeric stateOrientation 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 thermophilusAdaptor protein controlled oligomerization activates the AAA+ protein ClpCSuramin inhibits Hsp104 ATPase and disaggregase activityIdentification and mapping of self-assembling protein domains encoded by the Escherichia coli K-12 genome by use of lambda repressor fusions.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ proteinDissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domainsTorsin ATPases: Harnessing Dynamic Instability for Function.Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation.Biochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1APrion propagation can occur in a prokaryote and requires the ClpB chaperone.A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding.ClpB chaperone passively threads soluble denatured proteins through its central pore.CLPB variants associated with autosomal-recessive mitochondrial disorder with cataract, neutropenia, epilepsy, and methylglutaconic aciduriaDisruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria.The mechanism of Torsin ATPase activation.The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and functionThe 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteinsN-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpressionRemodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretionAsymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.
P2860
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P2860
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Roles of individual domains an ...... lysis, and chaperone activity.
@en
Roles of individual domains an ...... lysis, and chaperone activity.
@nl
type
label
Roles of individual domains an ...... lysis, and chaperone activity.
@en
Roles of individual domains an ...... lysis, and chaperone activity.
@nl
prefLabel
Roles of individual domains an ...... lysis, and chaperone activity.
@en
Roles of individual domains an ...... lysis, and chaperone activity.
@nl
P2860
P50
P356
P1476
Roles of individual domains an ...... lysis, and chaperone activity.
@en
P2093
Christian Schlieker
Christine Strub
P2860
P304
17615-17624
P356
10.1074/JBC.M209686200
P407
P577
2003-03-06T00:00:00Z