Publicaciones en colaboración con investigadores/as de Imperial College London (22)

2024

  1. A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF

    Alzheimer's Research and Therapy, Vol. 16, Núm. 1

2023

  1. Natural Inhibitors of Amyloid Aggregation

    International Journal of Molecular Sciences

  2. Site-Specific 68Ga Radiolabeling of Trastuzumab Fab via Methionine for ImmunoPET Imaging

    Bioconjugate Chemistry, Vol. 34, Núm. 10, pp. 1802-1810

  3. The ALS/FTD-related C9orf72 hexanucleotide repeat expansion forms RNA condensates through multimolecular G-quadruplexes

    Nature Communications, Vol. 14, Núm. 1

  4. Unveiling the Rational Development of Stimuli-Responsive Silk Fibroin-Based Ionogel Formulations

    Chemistry of Materials, Vol. 35, Núm. 15, pp. 5798-5808

  5. α-Synuclein Aggregation Is Triggered by Oligomeric Amyloid-β 42 via Heterogeneous Primary Nucleation

    Journal of the American Chemical Society, Vol. 145, Núm. 33, pp. 18276-18285

2022

  1. A Chemical Mutagenesis Approach to Insert Post-translational Modifications in Aggregation-Prone Proteins

    ACS Chemical Neuroscience, Vol. 13, Núm. 12, pp. 1714-1718

  2. A Facile Method to Produce N-Terminally Truncated α-Synuclein

    Frontiers in Neuroscience, Vol. 16

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. Man does not live by intrinsically unstructured proteins alone: The role of structured regions in aggregation

    BioEssays, Vol. 43, Núm. 11

  3. Modulation of amyloid-β aggregation by metal complexes with a dual binding mode and their delivery across the blood-brain barrier using focused ultrasound

    Chemical Science, Vol. 12, Núm. 27, pp. 9485-9493

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

    Frontiers in Neuroscience, Vol. 15

  5. 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

  6. 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

  7. The diagnostic potential of amyloidogenic proteins

    International Journal of Molecular Sciences, Vol. 22, Núm. 8

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. 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

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

    Science Advances, Vol. 6, Núm. 45

2017

  1. 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

2015

  1. Structure and dynamics of the integrin LFA-1 I-domain in the inactive state underlie its inside-out/outside-in signaling and allosteric mechanisms

    Structure, Vol. 23, Núm. 4, pp. 745-753