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Maurizio Molinari

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Related publications (57)

How Viruses Hijack the ERAD Tuning Machinery

An essential step during the intracellular life cycle of many positive-strand RNA viruses is the rearrangement of host cell membranes to generate membrane-bound replication platforms. For example, Nidovirales and Flaviviridae subvert the membrane of the en ...

American Society for Microbiology2014

PROTEIN TRAFFICKING RESETting proteostasis

Maurizio Molinari

Nature Publishing Group2014

Transgenic expression of beta 1 antibody in brain neurons impairs age-dependent amyloid deposition in APP23 mice

Maurizio Molinari, Paolo Paganetti

Heterologous expression of the functional amyloid beta (A beta) antibody beta 1 in the central nervous system was engineered to maximize antibody exposure in the brain and assess the effects on A beta production and accumulation in these conditions. A sing ...

Elsevier Science Inc2013

Specificity and Regulation of the Endoplasmic Reticulum-Associated Degradation Machinery

Maurizio Molinari

The endoplasmic reticulum-associated degradation (ERAD) machinery selects native and misfolded polypeptides for dislocation across the ER membrane and proteasomal degradation. Regulated degradation of native proteins is an important aspect of cell physiolo ...

Wiley-Blackwell2013

UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum

Maurizio Molinari

Protein folding in the endoplasmic reticulum (ER) is error prone, and ER quality control (ERQC) processes ensure that only correctly folded proteins are exported from the ER. Glycoproteins can be retained in the ER by ERQC, and this retention contributes t ...

Amer Soc Cell Biology2013

RETRACTED: Autoadaptive ER-Associated Degradation Defines a Preemptive Unfolded Protein Response Pathway

Maurizio Molinari, Riccardo Bernasconi

Folding-defective proteins must be cleared efficiently from the endoplasmic reticulum (ER) to prevent perturbation of the folding environment and to maintain cellular proteostasis. Misfolded proteins engage dislocation machineries (dislocons) built around ...

Cell Press2013

Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis

Maurizio Molinari

Nascent polypeptides entering the endoplasmic reticulum (ER) are covalently modified with pre-assembled oligosaccharides. The terminal glucose and mannose residues are immediately removed after transfer of the oligosaccharide onto newly synthesized polypep ...

Elsevier Science London2012

Unconventional roles of nonlipidated LC3 in ERAD tuning and coronavirus infection

Maurizio Molinari, Riccardo Bernasconi

Secretory and membrane proteins attain their native structure in the endoplasmic reticulum (ER). Folding-defective polypeptides are selected for degradation by processes collectively defined as ER-associated degradation (ERAD). Enhanced ERAD activity may i ...

Landes Bioscience2012

RETRACTED: Role of the SEL1L:LC3-I Complex as an ERAD Tuning Receptor in the Mammalian ER

Maurizio Molinari, Riccardo Bernasconi

Several regulators of endoplasmic reticulum (ER)associated degradation (ERAD) have a shorter half-life compared to conventional ER chaperones. At steady state, they are selectively removed from the ER by poorly defined events collectively referred to as ER ...

2012

Chronic delivery of antibody fragments using immunoisolated cell implants as a passive vaccination tool

Patrick Aebischer, Nicolas Bouche, Jean-Charles Bensadoun, Maria del Carmen Sandi Perez, Rolf Gruetter, Maria Isabel Cordero Campana, Osiris Marroquin Belaunzaran, Veronica Setola, Maurizio Molinari

BACKGROUND: Monoclonal antibodies and antibody fragments are powerful biotherapeutics for various debilitating diseases. However, high production costs, functional limitations such as inadequate pharmacokinetics and tissue accessibility are the current pri ...

Public Library of Science2011

ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER

Maurizio Molinari, Riccardo Bernasconi

The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. Unsuccessful folding attempts are eventually interrupted and most folding-defective polypeptides are dislocated across the ER membrane and deg ...

2011

System and Method For In Vivo Delivery of Antibodies and Fragments Thereof

Patrick Aebischer, Nicolas Bouche, Maurizio Molinari

The present invention is directed to devices and methods for in situ delivering an antibody or a fragment thereof to a host. In particular, the invention relates to devices and methods for in situ delivering an antibody or a fragment thereof to patient suf ...

2011

Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER

Maurizio Molinari, Riccardo Bernasconi

Malectin is a conserved, endoplasmic reticulum (ER)-resident lectin that recognizes high mannose oligosaccharides displaying terminal glucose residues. Here we show that Malectin is an ER stress-induced protein that selectively associates with glycopolypep ...

Public Library of Science2011

Coronaviruses Hijack the LC3-I-Positive EDEMosomes, ER-Derived Vesicles Exporting Short-Lived ERAD Regulators, for Replication

Maurizio Molinari, Riccardo Bernasconi

Coronaviruses (CoV), including SARS and mouse hepatitis virus (MHV), are enveloped RNA viruses that induce formation of double-membrane vesicles (DMVs) and target their replication and transcription complexes (RTCs) on the DMV-limiting membranes. The DMV b ...

2010

Autophagy-independent LC3 function in vesicular traffic

Maurizio Molinari

As protein folding is an imperfect process, the endoplasmic reticulum (ER) contains folding as well as ER-associated degradation (ERAD) machineries. In order to prevent premature interruption of folding, ERAD regulators and effectors such as EDEM1 and OS-9 ...

2010

Cyclosporine A-Sensitive, Cyclophilin B-Dependent Endoplasmic Reticulum-Associated Degradation

Maurizio Molinari, Riccardo Bernasconi

Peptidyl-prolyl cis/trans isomerases (PPIs) catalyze cis/trans isomerization of peptide bonds preceding proline residues. The involvement of PPI family members in protein refolding has been established in test tube experiments. Surprisingly, however, no da ...

Public Library of Science2010

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-L-S substrates

Maurizio Molinari, Riccardo Bernasconi

Sophisticated quality control mechanisms prolong retention of protein-folding intermediates in the endoplasmic reticulum (ER) until maturation while sorting out terminally misfolded polypeptides for ER-associated degradation (ERAD). The presence of structu ...

Rockefeller University Press2010

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