article Open AccessTop 1% cited
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Nature Structural & Molecular Biology · 2010 · Vol. 17(5) · pp. 561–567
Mahiuddin Ahmed✉(Stony Brook University)Judianne Davis(Stony Brook University)Darryl Aucoin(Stony Brook University)Takeshi Sato(Protein Research Foundation)Shivani Ahuja(Stony Brook University)Saburo Aimoto(Osaka University)James I. Elliott(Yale University)William E. Van Nostrand(Stony Brook University)Steven O. Smith(Stony Brook University)
Alzheimer's disease research and treatmentsSupramolecular Self-Assembly in MaterialsGraph theory and applicationsFibrilChemistryAmyloid (mycology)BiophysicsOligomerPeptideCrystallographyBeta sheetAmyloid betaAmyloid fibril
MeSH terms
Alzheimer DiseaseAmino Acid SequenceAnimalsCell SurvivalCells, CulturedCold TemperatureModels, MolecularMolecular Sequence DataNeuronsPeptide FragmentsSaltsAmyloid beta-PeptidesProtein Structure, SecondaryNuclear Magnetic Resonance, BiomolecularMice
Funding
- National Science Foundation
Citations
1,085
FWCI
31.44
field-weighted impact
References
46
Percentile
100%
vs. same field & year
Citations per year
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References
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Science · 2002 · 13,715 citations
P<scp>ROTOFIBRILS</scp>, P<scp>ORES</scp>, F<scp>IBRILS, AND</scp> N<scp>EURODEGENERATION</scp>: Separating the Responsible Protein Aggregates from The Innocent Bystanders
Annual Review of Neuroscience · 2003 · 1,643 citations
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Nature Neuroscience · 2004 · 1,667 citations
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