M. Stefani
Molecular Biology · 2002–2003
A researcher in the Science corpus: 3 papers; trusts 2 researchers and is trusted by 15 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 32 citations into it; #3,287 of 17,773 by trust here, #4,657 by citations
- Cell Biology — 8 citations into it; #374 of 2,073 by trust here, #1,265 by citations
- Materials Chemistry — 5 citations into it
Whom M. Stefani trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts M. Stefani overall
- Christopher M. Dobson
- Wilke Drummond
- Ò. Conchillo-Solé
- R. Winter
- D. A. Drummond
- Natalia Sanchez de Groot
- D. Lopes
- Pietro Sormanni
- Claus O. Wilke
- Fabrizio Chiti
Papers from M. Stefani's perspective
Ordered by how strongly the researchers M. Stefani trusts endorse each paper. Same corpus, a different order for every researcher.
- The structural basis of protein folding and its links with human disease. (Philosophical transactions of the Royal Society of London. Series B, Biological sciences)
- Amyloid fibrils from muscle myoglobin (Nature)
- A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly* (Journal of Biological Chemistry)
- Aggresomes, inclusion bodies and protein aggregation. (Trends in Cell Biology)
- Natively unfolded proteins: A point where biology waits for physics (Protein Science)
- Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo (Nature)
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis (Science)
- Intrinsically disordered protein.
- Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein (Proceedings of the National Academy of Sciences of the United States of America)
- Opposing Activities Protect Against Age-Onset Proteotoxicity (Science)
Their papers
- Rationalization of the effects of mutations on peptide andprotein aggregation rates (2003) — 1,049 citations
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002) — 2,483 citations
- Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution (2003) — 1,657 citations