Matthew Biancalana
Molecular Biology · 2010–2013
A researcher in the Science corpus: 2 papers; trusts 2 researchers and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 25 citations into it
- Physiology — 11 citations into it
- Materials Chemistry — 5 citations into it
Whom Matthew Biancalana trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Papers from Matthew Biancalana's perspective
Ordered by how strongly the researchers Matthew Biancalana trusts endorse each paper. Same corpus, a different order for every researcher.
- Amyloid formation by globular proteins under native conditions. (Nature Chemical Biology)
- Protein folding and misfolding
- The binding of thioflavin-T to amyloid fibrils: localisation and implications. (Journal of Structural Biology)
- Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B (Annals of Neurology)
- Atomic structures of amyloid cross-beta spines reveal varied steric zippers. (Nature)
- Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation (Proceedings of the National Academy of Sciences of the United States of America)
- Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status (Journal of chemical biology)
- Mechanism of thioflavin T binding to amyloid fibrils. (Journal of Structural Biology)
- Conformation of twisted beta-pleated sheets in proteins.
- Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism (Chemical Biology and Drug Design)
Their papers
- Dominant-Activating, Germline Mutations in Phosphoinositide 3-Kinase p110δ Cause T Cell Senescence and Human Immunodeficiency (2013) — 637 citations
- Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010) — 1,982 citations