Search Results - "Molinari, Maurizio"
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N-glycan structure dictates extension of protein folding or onset of disposal
Published in Nature chemical biology (01-06-2007)“…The endoplasmic reticulum (ER) is the site of folding for proteins that are resident in the ER or that are destined for the Golgi, endosomes, lysosomes, the…”
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Proteasomal and lysosomal clearance of faulty secretory proteins: ER-associated degradation (ERAD) and ER-to-lysosome-associated degradation (ERLAD) pathways
Published in Critical reviews in biochemistry and molecular biology (04-03-2019)“…About 40% of the eukaryotic cell's proteins are inserted co- or post-translationally in the endoplasmic reticulum (ER), where they attain the native structure…”
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ESCRT-III-driven piecemeal micro-ER-phagy remodels the ER during recovery from ER stress
Published in Nature communications (07-11-2019)“…The endoplasmic reticulum (ER) produces about 40% of the nucleated cell’s proteome. ER size and content in molecular chaperones increase upon physiologic and…”
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In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
Published in Physiological reviews (01-10-2007)“…Institute for Research in Biomedicine, Bellinzona, Switzerland; and Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular…”
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ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER
Published in Current opinion in cell biology (01-04-2011)“…The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. Unsuccessful folding attempts are eventually…”
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N‐glycan processing selects ERAD‐resistant misfolded proteins for ER‐to‐lysosome‐associated degradation
Published in The EMBO journal (02-08-2021)“…Efficient degradation of by‐products of protein biogenesis maintains cellular fitness. Strikingly, the major biosynthetic compartment in eukaryotic cells, the…”
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Endoplasmic reticulum turnover: ER-phagy and other flavors in selective and non-selective ER clearance [version 1; peer review: 2 approved]
Published in F1000 research (2018)“…The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells. It is deputed to lipid and protein biosynthesis, calcium storage, and the…”
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Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery
Published in Nature cell biology (01-11-2016)“…The endoplasmic reticulum (ER) is a site of protein biogenesis in eukaryotic cells. Perturbing ER homeostasis activates stress programs collectively called the…”
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N-glycan processing in ER quality control
Published in Journal of cell science (01-11-2006)“…Glycosylation of asparagine residues in Asn-x-Ser/Thr motifs is a common covalent modification of proteins in the lumen of the endoplasmic reticulum (ER). By…”
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Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates
Published in The Journal of cell biology (25-01-2010)“…Sophisticated quality control mechanisms prolong retention of protein-folding intermediates in the endoplasmic reticulum (ER) until maturation while sorting…”
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Five Questions (with their Answers) on ER‐Associated Degradation
Published in Traffic (Copenhagen, Denmark) (01-04-2016)“…Production of a functional proteome is a major burden for our cells. Native proteins operate inside and outside the cells to eventually warrant life and…”
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Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins
Published in FEBS letters (31-07-2007)“…Proteins synthesized in the endoplasmic reticulum (ER) lumen are exposed to several dedicated chaperones and folding factors that ensure efficient maturation…”
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How viruses hijack the ERAD tuning machinery
Published in Journal of virology (01-09-2014)“…An essential step during the intracellular life cycle of many positive-strand RNA viruses is the rearrangement of host cell membranes to generate…”
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14
Deep learning approach for quantification of organelles and misfolded polypeptide delivery within degradative compartments
Published in Molecular biology of the cell (01-07-2020)“…LysoQuant is a deep learning approach to segmentation and classification of fluorescent images capturing cargo delivery within endolysosomes for clearance. It…”
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TMX4-driven LINC complex disassembly and asymmetric autophagy of the nuclear envelope upon acute ER stress
Published in Nature communications (13-06-2023)“…The endoplasmic reticulum (ER) is an organelle of nucleated cells that produces proteins, lipids and oligosaccharides. ER volume and activity are increased…”
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Thioredoxin-Related Transmembrane Proteins: TMX1 and Little Brothers TMX2, TMX3, TMX4 and TMX5
Published in Cells (Basel, Switzerland) (31-08-2020)“…The endoplasmic reticulum (ER) is site of synthesis and maturation of membrane and secretory proteins in eukaryotic cells. The ER contains more than 20 members…”
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Tau accumulation in degradative organelles is associated to lysosomal stress
Published in Scientific reports (21-10-2023)“…Neurodegenerative disorders are characterized by the brain deposition of insoluble amyloidogenic proteins, such as α-synuclein or Tau, and the concomitant…”
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Identification of signal peptide features for substrate specificity in human Sec62/Sec63‐dependent ER protein import
Published in The FEBS journal (01-11-2020)“…In mammalian cells, one‐third of all polypeptides are integrated into the membrane or translocated into the lumen of the endoplasmic reticulum (ER) via the…”
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Selective involvement of UGGT variant: UGGT2 in protecting mouse embryonic fibroblasts from saturated lipid-induced ER stress
Published in Proceedings of the National Academy of Sciences - PNAS (20-12-2022)“…Secretory proteins and lipids are biosynthesized in the endoplasmic reticulum (ER). The "protein quality control" system (PQC) monitors glycoprotein folding…”
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Specificity and Regulation of the Endoplasmic Reticulum‐Associated Degradation Machinery
Published in Traffic (Copenhagen, Denmark) (01-07-2013)“…The endoplasmic reticulum‐associated degradation (ERAD) machinery selects native and misfolded polypeptides for dislocation across the ER membrane and…”
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