D. Hamada
2002
A researcher in the Science corpus: 1 paper; trusts 1 researcher and is trusted by 0 researchers here, as inferred from the citation graph.
Whom D. Hamada trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Papers from D. Hamada's perspective
Ordered by how strongly the researchers D. Hamada trusts endorse each paper. Same corpus, a different order for every researcher.
- Amyloid fibrils from muscle myoglobin (Nature)
- The structural basis of protein folding and its links with human disease. (Philosophical transactions of the Royal Society of London. Series B, Biological sciences)
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (Nature)
- Structural and kinetic characterization of early folding events in β-lactoglobulin (Nature Structural Biology)
- A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. (Proceedings of the National Academy of Sciences of the United States of America)
- The protofilament structure of insulin amyloid fibrils (Proceedings of the National Academy of Sciences of the United States of America)
- Aggresomes, inclusion bodies and protein aggregation. (Trends in Cell Biology)
- A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly* (Journal of Biological Chemistry)
- Impairment of the ubiquitin-proteasome system by protein aggregation. (Science)
- The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia (Annals of Neurology)
Their papers
- A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea (2002) — 248 citations