A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.
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Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemiaParkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavageTHAP5 is a human cardiac-specific inhibitor of cell cycle that is cleaved by the proapoptotic Omi/HtrA2 protease during cell deathImplications of the serine protease HtrA1 in amyloid precursor protein processingA decade of Burkholderia cenocepacia virulence determinant researchColicin biologyRelease of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress responseProtein quality control in the bacterial periplasmKeeping up with protein foldingMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationCrystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritimaThe 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triadStructural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domainCovalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic CagesThe Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assembliesMolecular Adaptation of the DegQ Protease to Exert Protein Quality Control in the Bacterial Cell EnvelopeNewly folded substrates inside the molecular cage of the HtrA chaperone DegQThe yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress.A secretory multifunctional serine protease, DegP of Plasmodium falciparum, plays an important role in thermo-oxidative stress, parasite growth and developmentThe HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cellsDistribution of the serine protease HtrA1 in normal human tissuesThe serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activityDnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteinsA chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem IIAdaptive Posttranslational Control in Cellular Stress Response Pathways and Its Relationship to Toxicity Testing and Safety AssessmentTranscriptomics responses in marine diatom Thalassiosira pseudonana exposed to the polycyclic aromatic hydrocarbon benzo[a]pyreneThe Pseudomonas aeruginosa sensor kinase KinB negatively controls alginate production through AlgW-dependent MucA proteolysisNeuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in miceDevelopmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signalingOmi / HtrA2 is relevant to the selective vulnerability of striatal neurons in Huntington's diseaseReversal of the ΔdegP phenotypes by a novel rpoE allele of Escherichia coliClassifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Outer membrane protein biogenesis in Gram-negative bacteriaDegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli.Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditionsProtease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.Insights into the structure and assembly of Escherichia coli outer membrane protein AAssembly of Outer Membrane β-Barrel Proteins: the Bam Complex.The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli
P2860
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P2860
A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
A temperature-dependent switch ...... conserved heat shock protein.
@en
A temperature-dependent switch ...... conserved heat shock protein.
@nl
type
label
A temperature-dependent switch ...... conserved heat shock protein.
@en
A temperature-dependent switch ...... conserved heat shock protein.
@nl
prefLabel
A temperature-dependent switch ...... conserved heat shock protein.
@en
A temperature-dependent switch ...... conserved heat shock protein.
@nl
P1433
P1476
A temperature-dependent switch ...... y conserved heat shock protein
@en
P2093
P304
P356
10.1016/S0092-8674(00)80743-6
P407
P577
1999-04-01T00:00:00Z