Michele Vendruscolo, Professor
Affiliations: | Chemistry | University of Cambridge, Cambridge, England, United Kingdom |
Area:
Protein biophysicsGoogle:
"Michele Vendruscolo"Parents
Sign in to add mentorChristopher M. Dobson | post-doc | Cambridge (Chemistry Tree) | |
Martin Karplus | post-doc | (Chemistry Tree) |
Children
Sign in to add traineeMichele Sanguanini | grad student | (Neurotree) | |
Kai J Kohlhoff | grad student | 2005-2008 | Cambridge |
Aleksandr B. Sahakyan | grad student | 2009-2012 | Cambridge (Chemistry Tree) |
Robert B. Best | post-doc | (Chemistry Tree) | |
Subrata Mondal | post-doc | (Chemistry Tree) | |
Massimo Sandal | post-doc | 2009- | Cambridge |
Reynier Suardíaz | post-doc | 2010-2011 | Cambridge (Chemistry Tree) |
Carlo Camilloni | post-doc | 2009-2015 | Cambridge (Chemistry Tree) |
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Publications
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Bell R, Thrush RJ, Castellana-Cruz M, et al. (2022) N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates. Biochemistry |
Olivieri C, Li GC, Wang Y, et al. (2022) ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy. Science Advances. 8: eabo0696 |
Löhr T, Kohlhoff K, Heller GT, et al. (2022) A Small Molecule Stabilizes the Disordered Native State of the Alzheimer's Aβ Peptide. Acs Chemical Neuroscience. 13: 1738-1745 |
Schneider MM, Gautam S, Herling TW, et al. (2021) The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends. Nature Communications. 12: 5999 |
Scheidt T, Carozza JA, Kolbe CC, et al. (2021) The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces. Proceedings of the National Academy of Sciences of the United States of America. 118 |
Morgunov AS, Liis Saar K, Vendruscolo M, et al. (2021) New frontiers for machine learning in protein science. Journal of Molecular Biology. 167232 |
Joshi P, Perni M, Limbocker R, et al. (2021) Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response. Communications Biology. 4: 930 |
Nowicka U, Chroscicki P, Stroobants K, et al. (2021) Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins. Elife. 10 |
Perni M, Mannini B, Xu CK, et al. (2021) Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans. Scientific Reports. 11: 14391 |
Joshi P, Perni M, Limbocker R, et al. (2021) Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response. Communications Biology. 4: 843 |