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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

Nature Structural & Molecular Biology · 2016 · Vol. 23(5) · pp. 409–415
Marcus D. TuttleGemma ComellasAndrew J. NieuwkoopDustin J. CovellDominik BertholdKathryn D. KloepperJoseph M. CourtneyJae Kwang KimAlexander M. BarclayAmy KendallWilliam WanGerald StubbsCharles D. SchwietersVirginia M.‐Y. LeeJulia M. GeorgeChad M. Rienstra
Parkinson's Disease Mechanisms and TreatmentsAdvanced NMR Techniques and ApplicationsAdvanced Neuroimaging Techniques and ApplicationsFibrilChemistrySolid-state nuclear magnetic resonanceCrystallographySalt bridgeProtein foldingAmyloid (mycology)Alpha-synucleinBiophysicsAmyloid fibril

MeSH terms

Protein DomainsAmino Acid SequenceAmyloidAnimalsCells, CulturedHumansHydrogen BondingNeuronsParkinson DiseaseLewy BodiesProtein Structure, SecondaryProtein FoldingNuclear Magnetic Resonance, BiomolecularProtein Structure, QuaternaryMice

Funding

  • National Science Foundation
  • U.S. Department of Energy
  • National Institutes of Health
  • University of Illinois at Urbana-Champaign
  • Division of Materials Research
  • Center for Information Technology
  • National Center for Research Resources
  • Basic Energy Sciences
  • Biological and Environmental Research
  • Brookhaven National Laboratory
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