User profiles for Francesco A. Aprile
Francesco Antonio AprileDepartment of Chemistry, Imperial College London Verified email at imperial.ac.uk Cited by 4458 |
[HTML][HTML] Targeting amyloid aggregation: an overview of strategies and mechanisms
Amyloids result from the aggregation of a set of diverse proteins, due to either specific
mutations or promoting intra- or extra-cellular conditions. Structurally, they are rich in …
mutations or promoting intra- or extra-cellular conditions. Structurally, they are rich in …
Third generation antibody discovery methods: in silico rational design
Owing to their outstanding performances in molecular recognition, antibodies are extensively
used in research and applications in molecular biology, biotechnology and medicine. …
used in research and applications in molecular biology, biotechnology and medicine. …
[HTML][HTML] Methods of probing the interactions between small molecules and disordered proteins
It is generally recognized that a large fraction of the human proteome is made up of proteins
that remain disordered in their native states. Despite the fact that such proteins play key …
that remain disordered in their native states. Despite the fact that such proteins play key …
[HTML][HTML] Direct observation of the interconversion of normal and toxic forms of α-synuclein
Here, we use single-molecule techniques to study the aggregation of α-synuclein, the protein
whose misfolding and deposition is associated with Parkinson's disease. We identify a …
whose misfolding and deposition is associated with Parkinson's disease. We identify a …
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
…, E Deas, M Ouberai, FA Aprile… - Proceedings of the …, 2015 - National Acad Sciences
We describe the isolation and detailed structural characterization of stable toxic oligomers of
α-synuclein that have accumulated during the process of amyloid formation. Our approach …
α-synuclein that have accumulated during the process of amyloid formation. Our approach …
The CamSol method of rational design of protein mutants with enhanced solubility
Protein solubility is often an essential requirement in biotechnological and biomedical
applications. Great advances in understanding the principles that determine this specific property …
applications. Great advances in understanding the principles that determine this specific property …
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
The self-assembly of α-synuclein is closely associated with Parkinson’s disease and related
syndromes. We show that squalamine, a natural product with known anticancer and antiviral …
syndromes. We show that squalamine, a natural product with known anticancer and antiviral …
[HTML][HTML] Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
…, P Flagmeier, C Hughes, FA Aprile… - Nature …, 2019 - nature.com
Protein aggregation is a complex process resulting in the formation of heterogeneous mixtures
of aggregate populations that are closely linked to neurodegenerative conditions, such as …
of aggregate populations that are closely linked to neurodegenerative conditions, such as …
Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method
Antibodies targeting Aβ42 are under intense scrutiny because of their therapeutic potential
for Alzheimer’s disease. To enable systematic searches, we present an “antibody scanning” …
for Alzheimer’s disease. To enable systematic searches, we present an “antibody scanning” …
Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins
P Sormanni, FA Aprile… - Proceedings of the …, 2015 - National Acad Sciences
Antibodies are powerful tools in life sciences research, as well as in diagnostic and
therapeutic applications, because of their ability to bind given molecules with high affinity and …
therapeutic applications, because of their ability to bind given molecules with high affinity and …