Publicacions en què col·labora amb Michele Vendruscolo (31)

2022

  1. 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

  1. 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

  2. Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures

    Frontiers in Neuroscience, Vol. 15

  3. 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

  4. 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

  1. 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

  2. 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

  3. 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

  4. Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease

    Science Advances, Vol. 6, Núm. 45

2019

  1. Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

    Nature Communications, Vol. 10, Núm. 1

  2. 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

  1. 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

  2. Automated behavioral analysis of large c. Elegans populations using a wide field-of-view tracking platform

    Journal of Visualized Experiments, Vol. 2018, Núm. 141

  3. Cooperative Assembly of Hsp70 Subdomain Clusters

    Biochemistry, Vol. 57, Núm. 26, pp. 3641-3649

  4. 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

  5. Third generation antibody discovery methods:: In silico rational design

    Chemical Society Reviews, Vol. 47, Núm. 24, pp. 9137-9157

2017

  1. Delivery of Native Proteins into C. Elegans Using a Transduction Protocol Based on Lipid Vesicles

    Scientific Reports, Vol. 7, Núm. 1

  2. Methods of probing the interactions between small molecules and disordered proteins

    Cellular and Molecular Life Sciences, Vol. 74, Núm. 17, pp. 3225-3243

  3. Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method

    Science Advances, Vol. 3, Núm. 6

  4. 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