DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. - Wikidata - wikimedia - TriplyDB

DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.

DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.

http://www.wikidata.org/entity/Q37611390

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Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78 Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Bacterial signalling involving eukaryotic-type protein kinases Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization Proteome analysis of the Chlamydia pneumoniae elementary body.Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption Identification of a novel inducible cytosolic Hsp70 gene in Chinese shrimp Fenneropenaeus chinensis and comparison of its expression with the cognate Hsc70 under different stresses.Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release Cross-talk involving extracellular sensors and extracellular alarmones gives early warning to unstressed Escherichia coli of impending lethal chemical stress and leads to induction of tolerance responses.Recombinant protein expression in Escherichia coli: advances and challenges In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.Global response of Plasmodium falciparum to hyperoxia: a combined transcriptomic and proteomic approach.Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones A gene encoding a DnaK/hsp70 homolog in Escherichia coli.Alpha-crystallin/small heat shock protein has autokinase activity.Regulation of survival gene hsp70.The Bacillus subtilis heat shock stimulon A distinct segment of the sigma 32 polypeptide is involved in DnaK-mediated negative control of the heat shock response in Escherichia coli.Mapping the conformation of a client protein through the Hsp70 functional cycle.Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a "fluidity gene".Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli.DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation.Temperature sensing in Yersinia pestis: regulation of yopE transcription by lcrF.Monoclonal antibody recognition and function of a DnaK (HSP70) epitope found in gram-negative bacteria.Stress response of Escherichia coli to elevated hydrostatic pressure.Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro.Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker 83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases.Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli.The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation.Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coli.Stress-induced transcriptional activation.Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.Mutations in the C-terminal fragment of DnaK affecting peptide binding.Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Global transcriptome analysis of the heat shock response of Shewanella oneidensis.

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P2860

DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.

http://www.wikidata.org/entity/Q37611390

description

1991 nî lūn-bûn

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1991年の論文

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1991年学术文章

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1991年学术文章

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1991年学术文章

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1991年学术文章

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1991年学术文章

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1991年學術文章

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1991年學術文章

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1991年學術文章

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name

DnaK as a thermometer: threoni ...... critical for ATPase activity.

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DnaK as a thermometer: threoni ...... critical for ATPase activity.

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type

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DnaK as a thermometer: threoni ...... critical for ATPase activity.

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DnaK as a thermometer: threoni ...... critical for ATPase activity.

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DnaK as a thermometer: threoni ...... critical for ATPase activity.

@en

DnaK as a thermometer: threoni ...... critical for ATPase activity.

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Proceedings of the National Academy of Sciences of the United States of America

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DnaK as a thermometer: threoni ...... critical for ATPase activity.

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G C Walker

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J S McCarty

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P2860

Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Prediction of protein conformation

Spectroscopic determination of tryptophan and tyrosine in proteins

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.

A member of the Hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK

Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origins.

Speculations on the functions of the major heat shock and glucose-regulated proteins.

Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities.

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