A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus.
about
Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsCombining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJRAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.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 thermophilusSequential action of two hsp70 complexes during protein import into mitochondriaMolecular identification of monomeric aspartate racemase from Bifidobacterium bifidum.ClpB chaperone passively threads soluble denatured proteins through its central pore.In vivo modulation of a DnaJ homolog, CbpA, by CbpM.A 70-kDa molecular chaperone, DnaK, from the industrial bacterium Bacillus licheniformis: gene cloning, purification and molecular characterization of the recombinant protein.Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperonesThe ClpB ATPase of Streptomyces albus G belongs to the HspR heat shock regulon.Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangementThe unique chaperone operon of Thermotoga maritima: cloning and initial characterization of a functional Hsp70 and small heat shock protein.Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli.Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone.Roles of the two ATP binding sites of ClpB from Thermus thermophilus.CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM.Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein.Balance of ATPase stimulation and nucleotide exchange is not required for efficient refolding activity of the DnaK chaperone.K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus.Dynamic structural states of ClpB involved in its disaggregation function.
P2860
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P2860
A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
A novel factor required for th ...... rones of Thermus thermophilus.
@en
A novel factor required for th ...... rones of Thermus thermophilus.
@nl
type
label
A novel factor required for th ...... rones of Thermus thermophilus.
@en
A novel factor required for th ...... rones of Thermus thermophilus.
@nl
prefLabel
A novel factor required for th ...... rones of Thermus thermophilus.
@en
A novel factor required for th ...... rones of Thermus thermophilus.
@nl
P2093
P2860
P356
P1476
A novel factor required for th ...... rones of Thermus thermophilus.
@en
P2093
P2860
P304
17343-17348
P356
10.1074/JBC.271.29.17343
P407
P577
1996-07-01T00:00:00Z