Posttranslational quality control: folding, refolding, and degrading proteins.
about
Mutation of a gene encoding a putative chaperonin causes McKusick-Kaufman syndromeHsp90: a specialized but essential protein-folding toolCHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradationAn abundant erythroid protein that stabilizes free alpha-haemoglobinParkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavageAmyloid aggregates of the HET-s prion protein are infectious.A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasomeThe role of disulfide bonds in the assembly and function of MD-2Protein quality control in the bacterial periplasmNPGPx (GPx7): a novel oxidative stress sensor/transmitter with multiple roles in redox homeostasisCHIP: A new modulator of human malignant disordersStructural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein AlphaSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationMolecular chaperones and co-chaperones in Parkinson diseaseQuality control and fate determination of Hsp90 client proteinsLongitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative diseaseDirect visualization of CHIP-mediated degradation of alpha-synuclein in vivo: implications for PD therapeuticsStructure of the reovirus core at 3.6 A resolutionCrystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP proteaseCrystal 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 triadThe catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active siteA new native EcHsp31 structure suggests a key role of structural flexibility for chaperone functionRegulation of the E stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stressThe solution structure of the C-terminal domain of NfeD reveals a novel membrane-anchored OB-foldMcsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsRCrystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a GrooveA conformational switch underlies ClpP protease functionMolecular 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 DegQStructures of an ATP-independent Lon-like protease and its complexes with covalent inhibitorsThe N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperonesIn vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and is required for its proteolytic cleavage.Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1.Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationHRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.The cell biology of agingInteraction of Hsp90 with 20S proteasome: thermodynamic and kinetic characterization
P2860
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P2860
Posttranslational quality control: folding, refolding, and degrading proteins.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Posttranslational quality control: folding, refolding, and degrading proteins.
@ast
Posttranslational quality control: folding, refolding, and degrading proteins.
@en
type
label
Posttranslational quality control: folding, refolding, and degrading proteins.
@ast
Posttranslational quality control: folding, refolding, and degrading proteins.
@en
prefLabel
Posttranslational quality control: folding, refolding, and degrading proteins.
@ast
Posttranslational quality control: folding, refolding, and degrading proteins.
@en
P2093
P921
P1433
P1476
Posttranslational quality control: folding, refolding, and degrading proteins.
@en
P2093
Gottesman S
Maurizi MR
P304
P356
10.1126/SCIENCE.286.5446.1888
P407
P577
1999-12-01T00:00:00Z