Browsing by Author "Vendruscolo, Michele"

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  • Ciryam, Prajwal; Antalek, Matthew; Cid Samper, Fernando, 1991-; Tartaglia, Gian Gaetano; Dobson, Christopher M.; Guettsches, Katrin; Eggers, Britta; Vorgerd, Matthias; Marcus, Katrin; Kley, Rudolf A.; Morimoto, Richard I.; Vendruscolo, Michele; Weihl, Conrad C. (BioMed Central, 2019)
    Protein aggregation is a pathological feature of neurodegenerative disorders. We previously demonstrated that protein inclusions in the brain are composed of supersaturated proteins, which are abundant and aggregation-prone, ...
  • Baum, Jean; Chiti, Fabrizio; de Simone, Alfonso; Knowles, Tuomas P.J.; Kumita, Janet R.; Radford, Sheena E.; Robinson, Carol V.; Salvatella, Xavier; Valelli, Karen; Vendruscolo, Michele; Pastore, Annalisa; Tartaglia, Gian Gaetano (Frontiers, 2019)
  • Vecchi, Giulia; Sormanni, Pietro; Mannini, Benedetta; Vandelli, Andrea; Tartaglia, Gian Gaetano; Dobson, Christopher M.; Hartl, F. Ulrich; Vendruscolo, Michele (National Academy of Sciences, 2020)
    To function effectively proteins must avoid aberrant aggregation, and hence they are expected to be expressed at concentrations safely below their solubility limits. By analyzing proteome-wide mass spectrometry data of ...
  • Porcari, Riccardo; Proukakis, Christos; Waudby, Christopher A.; Bolognesi, Benedetta; Mangione, P. Patrizia; Paton, Jack F. S.; Mullin, Stephen; Cabrita, Lisa D.; Penco, Amanda; Relini, Annalisa; Verona, Guglielmo; Vendruscolo, Michele; Stoppini, Monica; Tartaglia, Gian Gaetano; Camilloni, Carlo; Christodoulou, John; Schapira, Anthony H. V.; Bellotti, Vittorio (American Society for Biochemistry and Molecular Biology, 2015)
    The conversion of α-synuclein from its intrinsically disordered monomeric state into the fibrillar cross-β aggregates characteristically present in Lewy bodies is largely unknown. The investigation of α-synuclein variants ...
  • Ciryam, Prajwal; Tartaglia, Gian Gaetano; Morimoto, Richard I.; Dobson, Christopher M.; Vendruscolo, Michele (Elsevier, 2013)
    The maintenance of protein solubility is a fundamental aspect of cellular homeostasis because protein aggregation is associated with a wide variety of human diseases. Numerous proteins unrelated in sequence and structure, ...

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