Maurizio Molinari mostly deals with Cell biology, Endoplasmic reticulum, Biochemistry, Protein folding and Glycoprotein. His Cell biology research integrates issues from Autophagy, Calpain and Protease. Particularly relevant to Chaperone-mediated autophagy is his body of work in Autophagy.
His work in Calnexin, Unfolded protein response and Endoplasmic-reticulum-associated protein degradation are all subfields of Endoplasmic reticulum research. His Calnexin research incorporates themes from Folding, Cell, Chaperone and Hemagglutinin. His research investigates the connection between Protein folding and topics such as Protein structure that intersect with problems in ERAD pathway, Signal transduction and Organelle.
Maurizio Molinari mainly investigates Endoplasmic reticulum, Cell biology, Biochemistry, Protein folding and Unfolded protein response. His study in Endoplasmic reticulum is interdisciplinary in nature, drawing from both Glycoprotein and Proteasome. The concepts of his Cell biology study are interwoven with issues in Autophagy, Secretory protein, Lysosome and Cytosol.
His work in the fields of Autophagy, such as Autophagosome and Autolysosome, overlaps with other areas such as Biogenesis. His work deals with themes such as Folding and Protein disulfide-isomerase, which intersect with Protein folding. His Unfolded protein response study integrates concerns from other disciplines, such as Proteome and Homeostasis.
The scientist’s investigation covers issues in Cell biology, Endoplasmic reticulum, Unfolded protein response, Autophagy and Proteostasis. In the subject of general Cell biology, his work in Endolysosome is often linked to Factory, thereby combining diverse domains of study. His studies deal with areas such as Secretory protein, Lysosome, Organelle and Protein folding as well as Endoplasmic reticulum.
His Lysosome study combines topics from a wide range of disciplines, such as Crosstalk, Autophagosome and Calnexin. Computational biology, Chaperone-mediated autophagy, Multicellular organism and Autolysosome is closely connected to Programmed cell death in his research, which is encompassed under the umbrella topic of Protein folding. His biological study spans a wide range of topics, including Receptor, Stimulation, Compartment and Cytotoxicity.
Maurizio Molinari mainly focuses on Endoplasmic reticulum, Cell biology, Proteostasis, Autophagy and Lysosome. He studied Endoplasmic reticulum and Secretory protein that intersect with Protein folding, ATF6 and Endoplasmic-reticulum-associated protein degradation. His Autolysosome study in the realm of Autophagy interacts with subjects such as Interpretation and Knowledge base.
His Lysosome study combines topics in areas such as Ubiquitin ligase complex, Sec61, Calnexin and Proteasome. Maurizio Molinari interconnects Autophagosome, Lipid bilayer fusion, Crosstalk and Chaperone in the investigation of issues within Calnexin. His research integrates issues of ESCRT, Endosome, VPS4A, Lipid-anchored protein and Translocon in his study of Unfolded protein response.
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)
Daniel J. Klionsky;Amal Kamal Abdel-Aziz;Sara Abdelfatah;Mahmoud Abdellatif.
Autophagy (2021)
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Daniel J. Klionsky;Kotb Abdelmohsen;Akihisa Abe;Joynal Abedin.
Autophagy (2016)
Setting the standards: quality control in the secretory pathway.
Lars Ellgaard;Maurizio Molinari;Ari Helenius.
Science (1999)
In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
Daniel N. Hebert;Maurizio Molinari.
Physiological Reviews (2007)
Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle.
Maurizio Molinari;Verena Calanca;Carmela Galli;Paola Lucca.
Science (2003)
Calpain: a protease in search of a function?
Ernesto Carafoli;Maurizio Molinari.
Biochemical and Biophysical Research Communications (1998)
N-glycan structures: recognition and processing in the ER
Markus Aebi;Riccardo Bernasconi;Simone Clerc;Maurizio Molinari.
Trends in Biochemical Sciences (2010)
Chaperone Selection During Glycoprotein Translocation into the Endoplasmic Reticulum
Maurizio Molinari;Ari Helenius.
Science (2000)
Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
Maurizio Molinari;Ari Helenius.
Nature (1999)
Selective Inhibition of Ii-dependent Antigen Presentation by Helicobacter pylori Toxin VacA
Maurizio Molinari;Mariolina Salio;Carmela Galli;Nathalie Norais.
Journal of Experimental Medicine (1998)
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