Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains
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Molecular chaperones: guardians of the proteome in normal and disease statesSolution structure of the dimeric zinc binding domain of the chaperone ClpXOrientation of the amino-terminal domain of ClpB affects the disaggregation of the proteinCharacterization of Rv3868, an essential hypothetical protein of the ESX-1 secretion system in Mycobacterium tuberculosisAggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensisSynergistic cooperation between two ClpB isoforms in aggregate reactivation.Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogansSeqA protein aggregation is necessary for SeqA function.Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria.The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and functionIntracellular complexes of the early-onset torsion dystonia-associated AAA+ ATPase TorsinA.Stability and interactions of the amino-terminal domain of ClpB from Escherichia coliStructure and function of the middle domain of ClpB from Escherichia coli.Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli.Aggregate reactivation mediated by the Hsp100 chaperonesclpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance.Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.Characterization of a unique ClpB protein of Mycoplasma pneumoniae and its impact on growth.Comparison of two label-free global quantitation methods, APEX and 2D gel electrophoresis, applied to the Shigella dysenteriae proteome.The elusive middle domain of Hsp104 and ClpB: location and function.ClpB/Hsp100 proteins and heat stress tolerance in plants.Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.Improvement in the production of the human recombinant enzyme N-acetylgalactosamine-6-sulfatase (rhGALNS) in Escherichia coli using synthetic biology approaches.Structural and functional conversion of molecular chaperone ClpB from the gram-positive halophilic lactic acid bacterium Tetragenococcus halophilus mediated by ATP and stress.Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.Domain stability in the AAA+ ATPase ClpB from Escherichia coli.Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB.Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity.Toward a semisynthetic stress response system to engineer microbial solvent toleranceCoordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress.The clpB gene is involved in the stress response of Myxococcus xanthus during vegetative growth and development.Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB.Nucleotide utilization requirements that render ClpB active as a chaperone.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.Functional domains of Brevibacillus thermoruber lon protease for oligomerization and DNA binding: role of N-terminal and sensor and substrate discrimination domains.
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P2860
Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@ast
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@en
type
label
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@ast
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@en
prefLabel
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@ast
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@en
P2093
P2860
P356
P1476
Structure and activity of ClpB ...... and -carboxyl-terminal domains
@en
P2093
A Zolkiewska
M E Barnett
M Zolkiewski
P2860
P304
37565-37571
P356
10.1074/JBC.M005211200
P407
P577
2000-12-01T00:00:00Z