Maurizio Molinari
Institute for Research in Biomedicine
Via V. Vela 6
CH-6500 Bellinzona
Switzerland
Name/email consistency: high
- N-glycan structure dictates extension of protein folding or onset of disposal. Molinari, M. Nat. Chem. Biol. (2007)
- Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Molinari, M., Galli, C., Vanoni, O., Arnold, S.M., Kaufman, R.J. Mol. Cell (2005)
- The secretory capacity of a cell depends on the efficiency of endoplasmic reticulum-associated degradation. Molinari, M., Sitia, R. Curr. Top. Microbiol. Immunol. (2005)
- Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Molinari, M., Eriksson, K.K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., Helenius, A. Mol. Cell (2004)
- Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Molinari, M., Calanca, V., Galli, C., Lucca, P., Paganetti, P. Science (2003)
- Folding of viral glycoproteins in the endoplasmic reticulum. Molinari, M. Virus Res. (2002)
- Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. Molinari, M., Galli, C., Piccaluga, V., Pieren, M., Paganetti, P. J. Cell Biol. (2002)
