Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. - Wikidata - awgldk - TriplyDB

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

http://www.wikidata.org/entity/Q37276384

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Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution Heat shock and stress response of Taenia solium and T. crassiceps (Cestoda).Proteomic analysis reveals the participation of energy- and stress-related proteins in the response of Pseudomonas putida DOT-T1E to toluene.The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli.Possible association of GroES and antigen 85 proteins with heat resistance of Mycobacterium paratuberculosis Global analysis of host response to induction of a latent bacteriophage.Mesencephalic astrocyte-derived neurotrophic factor reduces cell apoptosis via upregulating HSP70 in SHSY-5Y cells.Functional insights from the distribution and role of homopeptide repeat-containing proteins A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32.Molecular chaperone function of mammalian Hsp70 and Hsp40--a review.Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)Molecular basis for interactions of the DnaK chaperone with substrates.Side effects of chaperone gene co-expression in recombinant protein production.In vivo analysis of the overlapping functions of DnaK and trigger factor rpoE, the gene encoding the second heat-shock sigma factor, sigma E, in Escherichia coli.Nanovesicle trapping for studying weak protein interactions by single-molecule FRET Functional cooperation between BiP and calreticulin in the folding maturation of a glycoprotein in Trypanosoma cruzi.LuxS coexpression enhances yields of recombinant proteins in Escherichia coli in part through posttranscriptional control of GroEL.Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control.Isolation and characterization of Bacillus subtilis groE regulatory mutants: evidence for orf39 in the dnaK operon as a repressor gene in regulating the expression of both groE and dnaK A Chlamydia-specific C-terminal region of the stress response regulator HrcA modulates its repressor activity.Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.Chemical definition, cloning, and expression of the major protein of the leprosy bacillus.A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.Gene Expression Analysis of Four Radiation-resistant Bacteria.Global analysis of chaperone effects using a reconstituted cell-free translation system.Structural basis for accommodation of nonsteroidal ligands in the androgen receptor Molecular chaperones and selection against mutations Time-dependent translational response of E. coli to excess Zn(II).Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae.Mutations in the C-terminal fragment of DnaK affecting peptide binding.

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Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

http://www.wikidata.org/entity/Q37276384

description

1992 nî lūn-bûn

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1992年の論文

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年學術文章

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1992年學術文章

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1992年學術文章

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name

Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

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Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

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type

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Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

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Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

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Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

@en

Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

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PNAS.89.21.10341

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

P1476

Cooperation of GroEL/GroES and ...... isfolding in Escherichia coli.

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P2093

Gaitanaris GA

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Gottesman ME

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Gragerov A

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Komissarova N

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Nikiforov V

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Nudler E

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

Protein folding in the cell

The heat-shock proteins

Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.

Host participation in bacteriophage lambda head assembly.

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures.

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

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21

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1359538

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Escherichia coli

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50334

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