Fabrizio Chiti

Molecular Biology · 2002–2017

A researcher in the Science corpus: 7 papers; trusts 17 researchers and is trusted by 23 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 79 citations into it; #2,040 of 17,773 by trust here, #2,599 by citations
• Physiology — 76 citations into it; #108 of 2,276 by trust here, #233 by citations
• Neurology — 41 citations into it
• Cell Biology — 17 citations into it
• Biomaterials — 12 citations into it
• Cellular and Molecular Neuroscience — 10 citations into it
• Materials Chemistry — 10 citations into it
• Spectroscopy — 9 citations into it

Whom Fabrizio Chiti trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. Christopher M. Dobson
2. Vladimir N Uversky
3. G. Zandomeneghi
4. Tuomas P. J. Knowles
5. A. Paravastu
6. Wai-Ming Yau
7. D. Selkoe
8. Richard Leapman
9. R. Tycko
10. M. Krebs

Who trusts Fabrizio Chiti overall

1. Christopher M. Dobson
2. Ò. Conchillo-Solé
3. E. K. Kim
4. Tuomas P. J. Knowles
5. S. Loveday
6. Pietro Sormanni
7. Yongdae Shin
8. Michele Vendruscolo
9. F. Hartl
10. Natalia Sanchez de Groot

Papers from Fabrizio Chiti's perspective

Ordered by how strongly the researchers Fabrizio Chiti trusts endorse each paper. Same corpus, a different order for every researcher.

1. 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)
2. Protein misfolding, functional amyloid, and human disease. (Annual Review of Biochemistry)
3. An Analytical Solution to the Kinetics of Breakable Filament Assembly (Science)
4. Amyloid fibrils from muscle myoglobin (Nature)
5. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (Nature)
6. The structural basis of protein folding and its links with human disease. (Philosophical transactions of the Royal Society of London. Series B, Biological sciences)
7. Nucleated conformational conversion and the replication of conformational information by a prion determinant. (Science)
8. Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques (Proceedings of the National Academy of Sciences of the United States of America)
9. Intrinsically disordered protein.
10. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. (Biochemistry)

Their papers

• Rationalization of the effects of mutations on peptide andprotein aggregation rates (2003) — 1,049 citations
• Protein misfolding, functional amyloid, and human disease. (2006) — 6,175 citations
• Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. (2005) — 596 citations
• Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002) — 2,483 citations
• Amyloid formation by globular proteins under native conditions. (2009) — 829 citations
• Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017) — 2,248 citations
• Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers (2017) — 622 citations