Michele Vendruscolo, Professor
Affiliations: | Chemistry | University of Cambridge, Cambridge, England, United Kingdom |
Area:
Protein biophysicsGoogle:
"Michele Vendruscolo"Parents
Sign in to add mentor| Christopher M. Dobson | post-doc | Cambridge (Chemistry Tree) | |
| Martin Karplus | post-doc | (Chemistry Tree) |
Children
Sign in to add trainee| biao fu | grad student | University of Cambridge (UK) (Chemistry Tree) | |
| Michele 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) |
BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| Olivieri C, Wang Y, Walker C, et al. (2024) The αC-β4 loop controls the allosteric cooperativity between nucleotide and substrate in the catalytic subunit of protein kinase A. Elife. 12 |
| Rinauro DJ, Chiti F, Vendruscolo M, et al. (2024) Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases. Molecular Neurodegeneration. 19: 20 |
| Olivieri C, Wang Y, Walker C, et al. (2023) The αC-β4 loop controls the allosteric cooperativity between nucleotide and substrate in the catalytic subunit of protein kinase A. Biorxiv : the Preprint Server For Biology |
| Vendruscolo M. (2023) Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation. Expert Opinion On Drug Discovery. 18: 881-891 |
| Miller A, Wei J, Meehan S, et al. (2023) Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains. Proceedings of the National Academy of Sciences of the United States of America. 120: e2216234120 |
| Limbocker R, Cremades N, Cascella R, et al. (2023) Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases. Accounts of Chemical Research |
| Bhardwaj T, Gadhave K, Kapuganti SK, et al. (2023) Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes. Nature Communications. 14: 945 |
| Baumann KN, Šneiderienė G, Sanguanini M, et al. (2022) A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ Aggregation. Acs Chemical Neuroscience. 14: 323-329 |
| 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 |