FRANCESCO
APRILE
Ramón y Cajal
Imperial College London
Londres, Reino UnidoPublicaciones en colaboración con investigadores/as de Imperial College London (22)
2024
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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
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Natural Inhibitors of Amyloid Aggregation
International Journal of Molecular Sciences
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Site-Specific 68Ga Radiolabeling of Trastuzumab Fab via Methionine for ImmunoPET Imaging
Bioconjugate Chemistry, Vol. 34, Núm. 10, pp. 1802-1810
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The ALS/FTD-related C9orf72 hexanucleotide repeat expansion forms RNA condensates through multimolecular G-quadruplexes
Nature Communications, Vol. 14, Núm. 1
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Unveiling the Rational Development of Stimuli-Responsive Silk Fibroin-Based Ionogel Formulations
Chemistry of Materials, Vol. 35, Núm. 15, pp. 5798-5808
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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
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A Chemical Mutagenesis Approach to Insert Post-translational Modifications in Aggregation-Prone Proteins
ACS Chemical Neuroscience, Vol. 13, Núm. 12, pp. 1714-1718
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A Facile Method to Produce N-Terminally Truncated α-Synuclein
Frontiers in Neuroscience, Vol. 16
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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Man does not live by intrinsically unstructured proteins alone: The role of structured regions in aggregation
BioEssays, Vol. 43, Núm. 11
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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
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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
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The diagnostic potential of amyloidogenic proteins
International Journal of Molecular Sciences, Vol. 22, Núm. 8
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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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
2017
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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
2015
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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