Instituto de Física de Partículas y del Cosmos (IPARCOS)
Centro/Instituto
Michele
Vendruscolo
Publicaciones en las que colabora con Michele Vendruscolo (31)
2022
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An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients
Chemical Science, Vol. 13, Núm. 46, pp. 13815-13828
2021
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Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease
Frontiers in Cell and Developmental Biology, Vol. 9
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Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures
Frontiers in Neuroscience, Vol. 15
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Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis
Cell Chemical Biology, Vol. 28, Núm. 1, pp. 70-77.e5
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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, Vol. 118, Núm. 38
2020
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A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease
Scientific Reports, Vol. 10, Núm. 1
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Rational design of a conformation-specific antibody for the quantification of Aβ oligomers
Proceedings of the National Academy of Sciences of the United States of America, Vol. 117, Núm. 24, pp. 13509-13518
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Rationally designed antibodies as research tools to study the structure–toxicity relationship of amyloid-β oligomers
International Journal of Molecular Sciences, Vol. 21, Núm. 12, pp. 1-18
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Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease
Science Advances, Vol. 6, Núm. 45
2019
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Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
Nature Communications, Vol. 10, Núm. 1
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Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression
Acta neuropathologica communications, Vol. 7, Núm. 1, pp. 120
2018
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A rationally designed Hsp70 variant rescues the aggregation-associated toxicity of human IAPP in cultured pancreatic islet β-cells
International Journal of Molecular Sciences, Vol. 19, Núm. 5
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Automated behavioral analysis of large c. Elegans populations using a wide field-of-view tracking platform
Journal of Visualized Experiments, Vol. 2018, Núm. 141
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Cooperative Assembly of Hsp70 Subdomain Clusters
Biochemistry, Vol. 57, Núm. 26, pp. 3641-3649
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Erratum to: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation (Scientific Reports, (2017), 7, 1, (9039), 10.1038/s41598-017-08324-z)
Scientific Reports
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Third generation antibody discovery methods:: In silico rational design
Chemical Society Reviews, Vol. 47, Núm. 24, pp. 9137-9157
2017
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Delivery of Native Proteins into C. Elegans Using a Transduction Protocol Based on Lipid Vesicles
Scientific Reports, Vol. 7, Núm. 1
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Methods of probing the interactions between small molecules and disordered proteins
Cellular and Molecular Life Sciences, Vol. 74, Núm. 17, pp. 3225-3243
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Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method
Science Advances, Vol. 3, Núm. 6
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Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide
Journal of Molecular Biology, Vol. 429, Núm. 18, pp. 2772-2779