Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain. - Wikidata - awgldk - TriplyDB

Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.

Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.

http://www.wikidata.org/entity/Q34616289

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Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions The Crystal Structure of the Human Co-Chaperone P58IPK J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix.The J-protein family: modulating protein assembly, disassembly and translocation.Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor.The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum.Allostery in the Hsp70 chaperone proteins Structure of CbpA J-domain bound to the regulatory protein Cbpm explains its specificity and suggests evolutionary link between Cbpm and transcriptional regulators.Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis.A bacteriophage-encoded J-domain protein interacts with the DnaK/Hsp70 chaperone and stabilizes the heat-shock factor σ32 of Escherichia coli Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.Diverse evolutionary mechanisms shape the type III effector virulence factor repertoire in the plant pathogen Pseudomonas syringae.Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.Chaperone-assisted excisive recombination, a solitary role for DnaJ (Hsp40) chaperone in lysogeny escape.Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.The Hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae.Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK.Dimeric heat shock protein 40 binds radial spokes for generating coupled power strokes and recovery strokes of 9 + 2 flagella.Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural change Simian virus 40 T antigens and J domains: analysis of Hsp40 cochaperone functions in Escherichia coli.Curing of yeast [URE3] prion by the Hsp40 cochaperone Ydj1p is mediated by Hsp70.Hsp70 structure, function, regulation and influence on yeast prions.Pharmacological targeting of the Hsp70 chaperone.Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.Artificial DnaJ Protein for protein production and conformational diseases.Genetic analysis of the polyomavirus DnaJ domain Zuotin, a DnaJ molecular chaperone, stimulates cap-independent translation in yeast.The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.Protein polarization driven by nucleoid exclusion of DnaK(HSP70)-substrate complexes.Mycoplasma pneumoniae J-domain protein required for terminal organelle function.RNAi-dependent heterochromatin assembly in fission yeast Schizosaccharomyces pombe requires heat-shock molecular chaperones Hsp90 and Mas5.

P2860

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P2860

Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.

http://www.wikidata.org/entity/Q34616289

description

2002 nî lūn-bûn

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2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2002年の論文

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Scanning mutagenesis identifie ...... ia coli DnaJ (Hsp40) J-domain.

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Scanning mutagenesis identifie ...... ia coli DnaJ (Hsp40) J-domain.

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Scanning mutagenesis identifie ...... y of the Escherichia coli DnaJ

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Scanning mutagenesis identifie ...... ia coli DnaJ (Hsp40) J-domain.

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Scanning mutagenesis identifie ...... ia coli DnaJ (Hsp40) J-domain.

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Scanning mutagenesis identifie ...... ia coli DnaJ (Hsp40) J-domain.

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Scanning mutagenesis identifie ...... ia coli DnaJ (Hsp40) J-domain.

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Scanning mutagenesis identifie ...... y of the Escherichia coli DnaJ

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Costa Georgopoulos

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Françoise Schwager

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Pierre Genevaux

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William L Kelley

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P2860

A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions

The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone

NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens

Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen

Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain

NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

Rapid and efficient site-specific mutagenesis without phenotypic selection

Regulation of Hsp70 function by a eukaryotic DnaJ homolog.

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates.

A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s

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Escherichia coli

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