about
Role of EDEM in the release of misfolded glycoproteins from the calnexin cycleA dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposalN-linked sugar-regulated protein folding and quality control in the ERChaperone selection during glycoprotein translocation into the endoplasmic reticulum.Five Questions (with their Answers) on ER-Associated DegradationIn and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human DiseasesN-glycan processing in ER quality controlA novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradationCyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradationMalectin participates in a backup glycoprotein quality control pathway in the mammalian ER.Chronic delivery of antibody fragments using immunoisolated cell implants as a passive vaccination toolHow viruses hijack the ERAD tuning machinery.Unconventional use of LC3 by coronaviruses through the alleged subversion of the ERAD tuning pathway.A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residueDivision of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.beta-site specific intrabodies to decrease and prevent generation of Alzheimer's Abeta peptide.Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER.N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality controlConsequences of individual N-glycan deletions and of proteasomal inhibition on secretion of active BACE.UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum.The endoplasmic reticulum crossroads for newly synthesized polypeptide chains.N-glycan structures: recognition and processing in the ER.ERAD substrates: which way out?ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.Proteostasis: bad news and good news from the endoplasmic reticulum.PEST sequences do not influence substrate susceptibility to calpain proteolysis.Substrate-specific requirements for UGT1-dependent release from calnexin.The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein.Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities.EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation.Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle.Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence.The use of calnexin and calreticulin by cellular and viral glycoproteins.Degradation of trafficking-defective long QT syndrome type II mutant channels by the ubiquitin-proteasome pathway.Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control.The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity.Analyzing cotranslational protein folding and disulfide formation by diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
P50
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P50
description
hulumtues
@sq
onderzoeker
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researcher
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հետազոտող
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name
Maurizio Molinari
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Maurizio Molinari
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Maurizio Molinari
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Maurizio Molinari
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Maurizio Molinari
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type
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Maurizio Molinari
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Maurizio Molinari
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Maurizio Molinari
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Maurizio Molinari
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Maurizio Molinari
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prefLabel
Maurizio Molinari
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Maurizio Molinari
@en
Maurizio Molinari
@es
Maurizio Molinari
@nl
Maurizio Molinari
@sl
P106
P21
P31
P496
0000-0002-7636-5829