A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein.
about
Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesNot all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsHsp70 chaperones: cellular functions and molecular mechanismInteraction of murine BiP/GRP78 with the DnaJ homologue MTJ1Insights into the molecular mechanism of allostery in Hsp70s.The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJCombining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJZuotin, a ribosome-associated DnaJ molecular chaperonePrion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Mitochondrial Hsp70 Ssc1: role in protein folding.The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains.Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cellsHSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptorAllostery in the Hsp70 chaperone proteinsLow resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structuresIts substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solutionA review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Pathways of allosteric regulation in Hsp70 chaperones.Characterization of the anti-DnaJ monoclonal antibodies and their use to compare immunological properties of DnaJ and its human homologue HDJ-1Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.Structure of CbpA J-domain bound to the regulatory protein Cbpm explains its specificity and suggests evolutionary link between Cbpm and transcriptional regulators.The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1.Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide releaseThe djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth.Strong precursor-pore interactions constrain models for mitochondrial protein importThe lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides.Hsp40 proteins modulate humoral and cellular immune response in rheumatoid arthritis patients.Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.T antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesisSmall tumor antigen of polyomaviruses: role in viral life cycle and cell transformationThe unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.
P2860
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P2860
A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein.
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-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
1996年學術文章
@zh-hant
name
A bipartite signaling mechanis ...... Escherichia coli DnaK protein.
@en
type
label
A bipartite signaling mechanis ...... Escherichia coli DnaK protein.
@en
prefLabel
A bipartite signaling mechanis ...... Escherichia coli DnaK protein.
@en
P2860
P356
P1476
A bipartite signaling mechanis ...... Escherichia coli DnaK protein.
@en
P2093
P2860
P304
11236-11246
P356
10.1074/JBC.271.19.11236
P407
P577
1996-05-01T00:00:00Z