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Author Details

Michele Vendruscolo
University of Cambridge
1996
502
86
Andrej Sali (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
36374974Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates.Mol Pharm2023
37745542The αC-β4 loop controls the allosteric cooperativity between nucleotide and substrate in the catalytic subunit of protein kinase A.bioRxiv2023
37701726Optimization of a small molecule inhibitor of secondary nucleation in α-synuclein aggregation.Front Mol Biosci2023
37578897Secondary Processes Dominate the Quiescent, Spontaneous Aggregation of α-Synuclein at Physiological pH with Sodium Salts.ACS Chem Neurosci2023
37774095Multiomic prediction of therapeutic targets for human diseases associated with protein phase separation.Proc Natl Acad Sci U S A2023
37978172Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.Nat Commun2023
37972287Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores.J Am Chem Soc2023
37532408Probing the effects of N-terminal acetylation on α-synuclein structure, aggregation and cytotoxicity.Methods Enzymol2023
36993242ANXA11 biomolecular condensates facilitate protein-lipid phase coupling on lysosomal membranes.bioRxiv2023
37186840Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains.Proc Natl Acad Sci U S A2023
36987846FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins.Nucleic Acids Res2023
37313660Extracellular protein homeostasis: The dawning of a new age for human disease therapies?Clin Transl Med2023
37276120Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation.Expert Opin Drug Discov2023
37207400Towards sequence-based principles for protein phase separation predictions.Curr Opin Chem Biol2023
37071750Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases.Acc Chem Res2023
37477459Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy.Biochemistry2023
37433124Quantitative Attribution of the Protective Effects of Aminosterols against Protein Aggregates to Their Chemical Structures and Ability to Modulate Biological Membranes.J Med Chem2023
37264457Case report of a patient with unclassified tauopathy with molecular and neuropathological features of both progressive supranuclear palsy and corticobasal degeneration.Acta Neuropathol Commun2023
36994753The amyloid-β pathway in Alzheimer's disease: a plain language summary.Neurodegener Dis Manag2023
36719110Sequence-based prediction of pH-dependent protein solubility using CamSol.Brief Bioinform2023
36806058Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes.Nat Commun2023
36574473A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ<sub>42</sub> Aggregation.ACS Chem Neurosci2023
36536207Geniposide and asperuloside alter the COX-2 and GluN2B receptor expression after pilocarpine-induced seizures in mice.Naunyn Schmiedebergs Arch Pharmacol2023
36802433Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH.Proc Natl Acad Sci U S A2023
36535315EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity.Chem Biol Interact2023
36828943Extracellular protein homeostasis in neurodegenerative diseases.Nat Rev Neurol2023
36638180Enhanced surface nanoanalytics of transient biomolecular processes.Sci Adv2023
36939645Exploration and Exploitation Approaches Based on Generative Machine Learning to Identify Potent Small Molecule Inhibitors of α-Synuclein Secondary Nucleation.J Chem Theory Comput2023
36728544Combinations of Vitamin A and Vitamin E Metabolites Confer Resilience against Amyloid-β Aggregation.ACS Chem Neurosci2023
36099961Effects of N-terminal Acetylation on the Aggregation of Disease-related α-synuclein Variants.J Mol Biol2023
34478132Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods.Methods Mol Biol2022
35649268A Small Molecule Stabilizes the Disordered Native State of the Alzheimer's Aβ Peptide.ACS Chem Neurosci2022
35610022FuzDrop on AlphaFold: visualizing the sequence-dependent propensity of liquid-liquid phase separation and aggregation of proteins.Nucleic Acids Res2022
35404569A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents.ACS Chem Neurosci2022
35401104Lipid Homeostasis and Its Links With Protein Misfolding Diseases.Front Mol Neurosci2022
35834748Ï¿-Clamp-Mediated Homo- and Heterodimerization of Single-Domain Antibodies via Site-Specific Homobifunctional Conjugation.J Am Chem Soc2022
35858383Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes.Proc Natl Acad Sci U S A2022
35367314Vulnerability of the spinal motor neuron presynaptic terminal sub-proteome in ALS.Neurosci Lett2022
35490011Kinetic profiling of therapeutic strategies for inhibiting the formation of amyloid oligomers.J Chem Phys2022
35625644Conformational Entropy as a Potential Liability of Computationally Designed Antibodies.Biomolecules2022
35815989Are casein micelles extracellular condensates formed by liquid-liquid phase separation?FEBS Lett2022
36544716An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients.Chem Sci2022
36341999Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates.Biochemistry2022
35905186ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.Sci Adv2022
36138006Protein condensation diseases: therapeutic opportunities.Nat Commun2022
36367941Fragment-based computational design of antibodies targeting structured epitopes.Sci Adv2022
35901206Adsorption free energy predicts amyloid protein nucleation rates.Proc Natl Acad Sci U S A2022
36230002Characterization of full-length p53 aggregates and their kinetics of formation.Biophys J2022
36127374Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease.Nat Commun2022
36030306Misfolded protein oligomers induce an increase of intracellular Ca<sup>2+</sup> causing an escalation of reactive oxidative species.Cell Mol Life Sci2022
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Collaborators

University of Cambridge
Co-authored papers 196
University of Melbourne, The Royal Children's Hospital
Co-authored papers 19
Institut Pasteur, Universite Paris Cite, CNRS UMR 8
Co-authored papers 15
Institut fur Physikalische Biologie, Heinrich-Heine-Universitat Dusseldorf
Co-authored papers 13
Harvard University
Co-authored papers 11
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Co-authored papers 10
University of Toronto
Co-authored papers 7
Cambridge Institute for Medical Research, University of Cambridge
Co-authored papers 5
Cambridge Institute for Medical Research, University of Cambridge
Co-authored papers 4
University of Connecticut Health Center
Co-authored papers 4
University of Padova
Co-authored papers 4
Co-authored papers 3
Leicester Institute of Structural and Chemical Biology, University of Leicester
Co-authored papers 3
Bijvoet Center for Biomolecular Research, Utrecht University
Co-authored papers 3
University of Cambridge
Co-authored papers 3
VIB-VUB Center for Structural Biology
Co-authored papers 3
University of California
Co-authored papers 2
Hospital for Sick Children
Co-authored papers 2
Co-authored papers 2
Institute of Bioengineering of Catalonia (IBEC)
Co-authored papers 2
Max Planck Institute of Molecular Plant Physiology
Co-authored papers 2
National Institutes of Health
Co-authored papers 2
University of Texas Southwestern Medical Center
Co-authored papers 2
Morsani College of Medicine, University of South Florida
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Center for Integrated Protein Science, Technische Universitat Munchen
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Zernike Institute for Advanced Materials, University of Groningen
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Rutgers University
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