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David M. Dias
Researcher at University of Oxford
Publications - 15
Citations - 596
David M. Dias is an academic researcher from University of Oxford. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Human serum albumin. The author has an hindex of 10, co-authored 14 publications receiving 459 citations. Previous affiliations of David M. Dias include University of Coimbra & University of Cambridge.
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Journal ArticleDOI
Structure-Guided Design and Optimization of Small Molecules Targeting the Protein-Protein Interaction between the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase and the Hypoxia Inducible Factor (HIF) Alpha Subunit with in Vitro Nanomolar Affinities.
Carles Galdeano,M.S. Gadd,P. Soares,Salvatore Scaffidi,Inge Van Molle,Ipek Birced,Sarah Hewitt,David M. Dias,Alessio Ciulli,Alessio Ciulli +9 more
TL;DR: The design and optimization, guided by X-ray crystal structures, of a ligand series with nanomolar binding affinities of the pVHL:HIF-1α interaction is reported.
Journal ArticleDOI
Local unfolding of the HSP27 monomer regulates chaperone activity.
T. Reid Alderson,T. Reid Alderson,Julien Roche,Julien Roche,Heidi Y. Gastall,David M. Dias,Iva Pritišanac,Jinfa Ying,Ad Bax,Justin L. P. Benesch,Andrew Baldwin +10 more
TL;DR: While HSP27 assembles into oligomers, it is shown that the monomers formed upon reduction are highly active chaperones in vitro, but are susceptible to self-aggregation.
Journal ArticleDOI
NMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexes.
David M. Dias,Alessio Ciulli +1 more
TL;DR: Current state-of-the-art in the portfolio of available NMR-based experiments that are used to aid early-stage lead discovery of multi-protein complexes as targets and how NMR spectroscopy allows studying of interactions within the high molecular weight assemblies that make up a vast fraction of the yet untargeted proteome are described.
Journal ArticleDOI
Is NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein-Protein Interactions?
David M. Dias,Inge Van Molle,Matthias G. J. Baud,Carles Galdeano,Carlos F. G. C. Geraldes,Alessio Ciulli +5 more
TL;DR: The requirements for ligand-based NMR techniques to detect rule-of-three compliant fragments that form part of known high-affinity inhibitors of the PPI between the von Hippel–Lindau protein and the alpha subunit of hypoxia-inducible factor 1 (pVHL:HIF-1α) are investigated.
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Interaction of PiB-derivative metal complexes with beta-amyloid peptides: selective recognition of the aggregated forms.
André F. Martins,David M. Dias,Jean-François Morfin,Sara Lacerda,Douglas V. Laurents,Éva Tóth,Carlos F. G. C. Geraldes +6 more
TL;DR: Time-dependent circular dichroism, dynamic light scattering, and TEM investigations of the secondary structure and of the aggregation of Aβ1-40 in the presence of increasing amounts of the metal complexes provide coherent data showing that, despite their structural similarity, the two complexes affect Aβ fibril formation distinctly.