Quality and quantity control at the endoplasmic reticulum.
about
Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsHRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradationIdentifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class IProtein folding and quality control in the EREndoplasmic reticulum stress in the β-cell pathogenesis of type 2 diabetesThe yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronDegradation-mediated protein quality control at the inner nuclear membraneFive Questions (with their Answers) on ER-Associated DegradationEffects of Different Variants in the ENPP1 Gene on the Functional Properties of Ectonucleotide Pyrophosphatase/Phosphodiesterase Family Member 1Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-LOrganizing principles of mammalian nonsense-mediated mRNA decayERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machineryTMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I.Minireview: the intimate link between calcium sensing receptor trafficking and signaling: implications for disorders of calcium homeostasis.Novel, gel-free proteomics approach identifies RNF5 and JAMP as modulators of GPCR stability.Inefficient translocation of preproinsulin contributes to pancreatic β cell failure and late-onset diabetes.Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins.Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER.ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway.Membrane protein insertion at the endoplasmic reticulum.Sequences at the interface of the fifth immunoglobulin domain and first fibronectin type III repeat of the neural cell adhesion molecule are critical for its polysialylationA context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradationAn unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme.Structure and assembly pathway of the ribosome quality control complex.Quantity control of the ErbB3 receptor tyrosine kinase at the endoplasmic reticulumCharacterization of early EDEM1 protein maturation events and their functional implications.The chaperone BAG6 captures dislocated glycoproteins in the cytosol.Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity.The VLDL receptor promotes lipotoxicity and increases mortality in mice following an acute myocardial infarction.Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis.Endoplasmic reticulum stress-related factors protect against diabetic retinopathyRole of Derlin-1 protein in proteostasis regulation of ATP-sensitive potassium channels.A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein.Whole genome expression profiling associates activation of unfolded protein response with impaired production and release of epinephrine after recurrent hypoglycemia.The cystic-fibrosis-associated ΔF508 mutation confers post-transcriptional destabilization on the C. elegans ABC transporter PGP-3.XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats.Impaired surface expression and conductance of the KCNQ4 channel lead to sensorineural hearing lossMHC class I molecules are preferentially ubiquitinated on endoplasmic reticulum luminal residues during HRD1 ubiquitin E3 ligase-mediated dislocation.Molecular chaperones as therapeutic targets to counteract proteostasis defects.Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation.
P2860
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P2860
Quality and quantity control at the endoplasmic reticulum.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Quality and quantity control at the endoplasmic reticulum.
@ast
Quality and quantity control at the endoplasmic reticulum.
@en
Quality and quantity control at the endoplasmic reticulum.
@nl
type
label
Quality and quantity control at the endoplasmic reticulum.
@ast
Quality and quantity control at the endoplasmic reticulum.
@en
Quality and quantity control at the endoplasmic reticulum.
@nl
prefLabel
Quality and quantity control at the endoplasmic reticulum.
@ast
Quality and quantity control at the endoplasmic reticulum.
@en
Quality and quantity control at the endoplasmic reticulum.
@nl
P2860
P1476
Quality and quantity control at the endoplasmic reticulum.
@en
P2093
Hidde L Ploegh
P2860
P304
P356
10.1016/J.CEB.2010.05.005
P577
2010-06-01T00:00:00Z