Maurizio Molinari, PhD
Controllo della produzione proteica
Direttore di laboratorio
Via Vela, 6
6500 Bellinzona,
Switzerland
- maurizio.molinari@irb.usi.ch
- +41 91 820 0319
- +41 91 820 0305
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Maurizio Molinari ha ricevuto il dottorato in Biochimica al Politecnico Federale di Zurigo nel 1995. Nel 1996-1997 ha lavorato come post-doc nel laboratorio di Cesare Montecucco al Dipartimento di Biomedicina dell’Università di Padova. Tra il 1998 e il 2000 è stato assistente nel laboratorio di Ari Helenius al Politecnico Federale di Zurigo. Dall’ottobre 2000, è Direttore di laboratorio all’IRB. Gli studi effettuati nel suo gruppo hanno dato un contributo significativo alla comprensione dei meccanismi che permettono la produzione delle proteine nelle cellule di mammifero e dei meccanismi che permettono alle cellule di eliminare proteine aberranti, potenzialmente tossiche. Questi studi hanno permesso, tra l’altro, di mettere a punto un nuovo approccio terapeutico basato sull’utilizzo di mini-anticorpi che permette di contrastare la produzione di beta-amiloide, un peptide il cui accumulo causa processi neurodegenerativi associati con la malattia di Alzheimer. Maurizio Molinari ha ricevuto lo Science Award 2002 della Fondazione per lo Studio delle Malattie Neurodegenerative, il Kiwanis Club Award 2002 per le Scienze Biomediche, il Friedrich-Miescher Award 2006 e il Research Award Aetas 2007. Nel 2008 è stato nominato Professore Associato al Politecnico Federale di Losanna. |
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Specificity and Regulation of the Endoplasmic Reticulum-Associated Degradation Machinery J. Merulla, E. Fasana, T. Solda, M. Molinari in Traffic (2013) |
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Endoplasmic Reticulum-Associated Protein Degradation R. Bernasconi, M. Molinari W.J. Lennarz, M.D. Lane, Editors in Encyclopedia of Biological Chemistry (2013) vol. 2 pp200-203 |
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Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis D. N. Hebert, M. Molinari in Trends Biochem Sci (2012) vol. 37 pp404-10 |
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Unconventional roles of nonlipidated LC3 in ERAD tuning and coronavirus infection R. Bernasconi, J. Noack, M. Molinari in Autophagy (2012) vol. 8 pp1534-6 |
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Role of the SEL1L:LC3-I Complex as an ERAD Tuning Receptor in the Mammalian ER R. Bernasconi, C. Galli, J. Noack, S. Bianchi, C. A. de Haan, F. Reggiori, M. Molinari in Mol Cell (2012) vol. 46 pp809-19 * Recommended by the Faculty of 1000 |
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Unconventional Use of LC3 by Coronaviruses through the Alleged Subversion of the ERAD Tuning Pathway F. Reggiori, C. A. de Haan, M. Molinari in Viruses (2011) vol. 3 pp1610-23 |
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Chronic delivery of antibody fragments using immunoisolated cell implants as a passive vaccination tool O. Marroquin Belaunzaran, M. I. Cordero, V. Setola, S. Bianchi, C. Galli, N. Bouche, V. Mlynarik, R. Gruetter, C. Sandi, J. C. Bensadoun, M. Molinari, P. Aebischer in PLoS One (2011) vol. 6 ppe18268 |
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Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER C. Galli, R. Bernasconi, T. Solda, V. Calanca, M. Molinari in PLoS One (2011) vol. 6 ppe16304 |
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ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER R. Bernasconi, M. Molinari in Curr Opin Cell Biol (2011) vol. 23 pp176-183 |
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Cyclosporine a-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation R. Bernasconi, T. Solda, C. Galli, T. Pertel, J. Luban, M. Molinari in PLoS One (2010) vol. 5 ppe13008 |
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Autophagy-independent LC3 function in vesicular traffic C. A. de Haan, M. Molinari, F. Reggiori in Autophagy (2010) vol. 6 pp994-6 |
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Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication F. Reggiori, I. Monastyrska, M. H. Verheije, T. Cali, M. Ulasli, S. Bianchi, R. Bernasconi, C. A. de Haan, M. Molinari in Cell Host Microbe (2010) vol. 7 pp500-8 * Highlights in Cell Host & Microbe 7, 424-426; Editors’ Choice in Science 329, 14; Leading Edge, Microbiology Select in Cell 142, 5; Recommended by the Faculty of 1000 |
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Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates R. Bernasconi, C. Galli, V. Calanca, T. Nakajima, M. Molinari in J Cell Biol (2010) vol. 188 pp223-35 * Highlights in J. Cell Biol 188, 176 |
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ERAD substrates: which way out? D. N. Hebert, R. Bernasconi, M. Molinari in Semin Cell Dev Biol (2010) vol. 21 pp526-32 |
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N-glycan structures: recognition and processing in the ER M. Aebi, R. Bernasconi, S. Clerc, M. Molinari in Trends Biochem Sci (2010) vol. 35 pp74-82 |
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The endoplasmic reticulum crossroads for newly synthesized polypeptide chains T. Cali, O. Vanoni, M. Molinari in Prog Mol Biol Transl Sci (2008) vol. 83 pp135-79 |
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Consequences of individual N-glycan deletions and of proteasomal inhibition on secretion of active BACE O. Vanoni, P. Paganetti, M. Molinari in Mol Biol Cell (2008) vol. 19 pp4086-98 |
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Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities T. Cali, C. Galli, S. Olivari, M. Molinari in Biochem Biophys Res Commun (2008) vol. 371 pp405-10 |
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A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal R. Bernasconi, T. Pertel, J. Luban, M. Molinari in J Biol Chem (2008) vol. 283 pp16446-54 |
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ER-Associated Folding and Degradation: Learning From Yeast? R. Bernasconi, M. Molinari C.B. O’Doherty, A.C. Byrne, Editors in Protein misfolding (2008) pp113-123 |
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In and out of the ER: protein folding, quality control, degradation, and related human diseases D. N. Hebert, M. Molinari in Physiol Rev (2007) vol. 87 pp1377-408 |
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Substrate-specific requirements for UGT1-dependent release from calnexin T. Solda, C. Galli, R. J. Kaufman, M. Molinari in Mol Cell (2007) vol. 27 pp238-49 |
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N-glycan structure dictates extension of protein folding or onset of disposal M. Molinari in Nat Chem Biol (2007) vol. 3 pp313-20 |
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Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins S. Olivari, M. Molinari in FEBS Lett (2007) vol. 581 pp3658-64 |
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N-glycan processing in ER quality control L. W. Ruddock, M. Molinari in J Cell Sci (2006) vol. 119 pp4373-80 |
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Microbiology: death of a chaperone C. Montecucco, M. Molinari in Nature (2006) vol. 443 pp511-2 |
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EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation S. Olivari, T. Cali, K. E. Salo, P. Paganetti, L. W. Ruddock, M. Molinari in Biochem Biophys Res Commun (2006) vol. 349 pp1278-84 * Recommended by the Faculty of 1000 |
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N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control K. W. Moremen, M. Molinari in Curr Opin Struct Biol (2006) vol. 16 pp592-9 |
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Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle T. Solda, N. Garbi, G. J. Hammerling, M. Molinari in J Biol Chem (2006) vol. 281 pp6219-26 |
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The secretory capacity of a cell depends on the efficiency of endoplasmic reticulum-associated degradation M. Molinari, R. Sitia in Curr Top Microbiol Immunol (2005) vol. 300 pp1-15 |
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Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence M. Molinari, C. Galli, O. Vanoni, S. M. Arnold, R. J. Kaufman in Mol Cell (2005) vol. 20 pp503-12 |
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The use of calnexin and calreticulin by cellular and viral glycoproteins M. Pieren, C. Galli, A. Denzel, M. Molinari in J Biol Chem (2005) vol. 280 pp28265-71 |
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The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags D. N. Hebert, S. C. Garman, M. Molinari in Trends Cell Biol (2005) vol. 15 pp364-70 |
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beta-site specific intrabodies to decrease and prevent generation of Alzheimer's Abeta peptide P. Paganetti, V. Calanca, C. Galli, M. Stefani, M. Molinari in J Cell Biol (2005) vol. 168 pp863-8 * Comments in NIBR Science Summer 2005 |
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Degradation of trafficking-defective long QT syndrome type II mutant channels by the ubiquitin-proteasome pathway Q. Gong, D. R. Keeney, M. Molinari, Z. Zhou in J Biol Chem (2005) vol. 280 pp19419-25 |
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Analyzing folding and degradation of metabolically labelled polypeptides by conventional and diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis T. Solda, S. Olivari, M. Molinari in Biol Proced Online (2005) vol. 7 pp136-43 |
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A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation S. Olivari, C. Galli, H. Alanen, L. Ruddock, M. Molinari in J Biol Chem (2005) vol. 280 pp2424-8 |
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EDEM contributes to maintenance of protein folding efficiency and secretory capacity K. K. Eriksson, R. Vago, V. Calanca, C. Galli, P. Paganetti, M. Molinari in J Biol Chem (2004) vol. 279 pp44600-5 |
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Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control M. Molinari, K. K. Eriksson, V. Calanca, C. Galli, P. Cresswell, M. Michalak, A. Helenius in Mol Cell (2004) vol. 13 pp125-35 |
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Endoplasmic Reticulum-Associated Protein Degradation M. Molinari W.J. Lennarz, M.D. Lane, Editors in Encyclopedia of Biological Chemistry (2004) vol. 2 pp20-23 |
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The Protein Factory M. Molinari in Protocols of the 30th Seminars of Biological Evolution (2004) vol. 108 pp117-122 |
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Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle M. Molinari, V. Calanca, C. Galli, P. Lucca, P. Paganetti in Science (2003) vol. 299 pp1397-400 * Comments in Science 299, 1330-1331; Nature Reviews Molecular and Cellular Biology, 4, 259; Nature Structural and Molecular Biology, 10, 319-321; Recommended by the Faculty of 1000 |
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Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression A. Denzel, M. Molinari, C. Trigueros, J. E. Martin, S. Velmurgan, S. Brown, G. Stamp, M. J. Owen in Mol Cell Biol (2002) vol. 22 pp7398-404 |
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Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER M. Molinari, C. Galli, V. Piccaluga, M. Pieren, P. Paganetti in J Cell Biol (2002) vol. 158 pp247-57 |
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The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity F. Fischer, M. Molinari, U. Bodendorf, P. Paganetti in J Neurochem (2002) vol. 80 pp1079-88 |
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Analyzing cotranslational protein folding and disulfide formation by diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis M. Molinari, A. Helenius in Methods Enzymol (2002) vol. 348 pp35-42 |
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Folding of viral glycoproteins in the endoplasmic reticulum M. Molinari in Virus Res (2002) vol. 82 pp83-6 |
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Role of Molecular Chaperones in Viral Glycoprotein Folding M. Molinari, A. Helenius in Intracellular and persistent infections, Nobel Symposium (2001) vol. 106 pp1-10 |
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Affinity purification of mu-calpain from erythrocytes on an immobilized peptide from the plasma membrane calcium pump. Some studies on erythrocyte mu-calpain M. Molinari, E. Carafoli in Methods Mol Biol (2000) vol. 144 pp41-6 |
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Chaperone selection during glycoprotein translocation into the endoplasmic reticulum M. Molinari, A. Helenius in Science (2000) vol. 288 pp331-3 |
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Site of Action and Cellular Effects Caused by the VacA Cytotoxin Released by Helicobacter pylori M. de Bernard, E. Papini, M. Molinari, B. Satin, J. R. Telford, R. Rappuoli, C. Montecucco J.E. Alouf, J.F. Freer, Editors in Bacterial Toxins: A comprehensive Sourcebook (1999) pp1-27 |
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Setting the standards: quality control in the secretory pathway L. Ellgaard, M. Molinari, A. Helenius in Science (1999) vol. 286 pp1882-8 |
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Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells M. Molinari, A. Helenius in Nature (1999) vol. 402 pp90-3 * News and Views in Nature 402, 27-29 |
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The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure F. Tonello, W. G. Dundon, B. Satin, M. Molinari, G. Tognon, G. Grandi, G. Del Giudice, R. Rappuoli, C. Montecucco in Mol Microbiol (1999) vol. 34 pp238-46 |
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Action site and cellular effects of cytotoxin VacA produced by Helicobacter pylori E. Papini, B. Satin, M. de Bernard, M. Molinari, B. Arico, C. Galli, J. R. Telford, R. Rappuoli, C. Montecucco in Folia Microbiol (Praha) (1998) vol. 43 pp279-84 |
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The acid activation of Helicobacter pylori toxin VacA: structural and membrane binding studies M. Molinari, C. Galli, M. de Bernard, N. Norais, J. M. Ruysschaert, R. Rappuoli, C. Montecucco in Biochem Biophys Res Commun (1998) vol. 248 pp334-40 |
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Calpain: a protease in search of a function? E. Carafoli, M. Molinari in Biochem Biophys Res Commun (1998) vol. 247 pp193-203 |
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Selective inhibition of Ii-dependent antigen presentation by Helicobacter pylori toxin VacA M. Molinari, M. Salio, C. Galli, N. Norais, R. Rappuoli, A. Lanzavecchia, C. Montecucco in J Exp Med (1998) vol. 187 pp135-40 |
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Vacuoles induced by Helicobacter pylori toxin contain both late endosomal and lysosomal markers M. Molinari, C. Galli, N. Norais, J. L. Telford, R. Rappuoli, J. P. Luzio, C. Montecucco in J Biol Chem (1997) vol. 272 pp25339-44 |
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Calpain: a cytosolic proteinase active at the membranes M. Molinari, E. Carafoli in J Membr Biol (1997) vol. 156 pp1-8 |
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Expression of the VacA Cytotoxin of Helicobacter pylori in the Cell Cytosol and Alteration of Membrane Trafficking M. de Bernard, E. Papini, M. Molinari, B. Arico, B. Satin, C. Galli, J. R. Telford, R. Rappuoli, C. Montecucco in Acta Med. Rom. (1997) vol. 35 pp625-633 |
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Purification of active calpain by affinity chromatography on an immobilized peptide inhibitor J. Anagli, E. M. Vilei, M. Molinari, S. Calderara, E. Carafoli in Eur J Biochem (1996) vol. 241 pp948-54 |
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Purification of mu-calpain by a novel affinity chromatography approach. New insights into the mechanism of the interaction of the protease with targets M. Molinari, M. Maki, E. Carafoli in J Biol Chem (1995) vol. 270 pp14576-81 |
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PEST sequences do not influence substrate susceptibility to calpain proteolysis M. Molinari, J. Anagli, E. Carafoli in J Biol Chem (1995) vol. 270 pp2032-5 |
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Ca(2+)-activated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form M. Molinari, J. Anagli, E. Carafoli in J Biol Chem (1994) vol. 269 pp27992-5 |