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Showing 1–19 of 19 results
Advanced filters: Author: Duilio Cascio Clear advanced filters

  • A short segment of α-synuclein called NACore (residues 68–78) is responsible for the formation of amyloid aggregates responsible for cytotoxicity in Parkinson disease; here the nanocrystal structure of this invisible-to-optical-microscopy segment is determined using micro-electron diffraction, offering insight into its function and simultaneously demonstrating the first use of micro-electron diffraction to solve a previously unknown protein structure.

    • Jose A. Rodriguez
    • Magdalena I. Ivanova
    • David S. Eisenberg
    Research
    Nature
    Volume: 525, P: 486-490

  • An environmentally safe means of mosquito control is the application of Bacillus thuringiensis israelensis, which produces a cocktail of four naturally crystalline proteins exclusively toxic to mosquito. Here the authors report the atomic-resolution structures of Bti Cry11Aa and related Btj Cry11Ba solved de novo through Serial Femtosecond Crystallography on naturally-occurring nanocrystals.

    • Guillaume Tetreau
    • Michael R. Sawaya
    • Jacques-Philippe Colletier
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • Combined use of microcrystal electron diffraction and genome mining for biosynthetic gene clusters enables the rapid structural elucidation of natural products, including a newly discovered 2-pyridone compound and a revised structure of fischerin.

    • Lee Joon Kim
    • Masao Ohashi
    • Hosea M. Nelson
    Research
    Nature Chemical Biology
    Volume: 17, P: 872-877

  • hnRNPA2 is involved in RNA metabolism and can form both functional amyloid-like fibrils in membraneless organelles, and pathogenic fibrils in neurodegenerative conditions. Here, the authors present the cryo-EM fibril structure of the wild-type hnRNPA2 low-complexity domain (LCD) and the crystal structure of a LCD segment with the disease causing D290V variant and discuss how mutations can transform fibril structure from a functional to a pathogenic form.

    • Jiahui Lu
    • Qin Cao
    • David S. Eisenberg
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • In patients with sporadic Alzheimer’s disease part of the Asp23 residues are isomerized to L-isoaspartate (L-isoAsp23). Here the authors present the MicroED structures of wild-type and L-isoAsp23 Aβ 20–34 amyloid fibrils that both form tightly packed cores and self-associate through two distinct interfaces with one of these interfaces being strengthened by the isoaspartyl modification.

    • Rebeccah A. Warmack
    • David R. Boyer
    • Steven G. Clarke
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • Structural analysis of the human MePCE methyltransferase domain in complex with 7SK in the presence of SAH or SAM reveals that MePCE has higher affinity for capped 7SK and holds it for subsequent assembly of 7SK RNP.

    • Yuan Yang
    • Catherine D. Eichhorn
    • Juli Feigon
    Research
    Nature Chemical Biology
    Volume: 15, P: 132-140

  • Bacillus thuringiensis israelensis (Bti) produces the naturally-crystalline proteinaceous toxin Cyt1Aa that is toxic to mosquito larvae. Here the authors grow recombinant nanocrystals of the Cyt1Aa protoxin in vivo and use serial femtosecond crystallography to determine its structure at different redox and pH conditions and by combining their structural data with further biochemical, toxicological and biophysical analyses provide mechanistic insights into the Cyt1Aa bioactivation cascade.

    • Guillaume Tetreau
    • Anne-Sophie Banneville
    • Jacques-Philippe Colletier
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16

  • The structure of the bacterial toxin BinAB, which is used to combat mosquito-borne diseases, reveals pH-sensitive switches and carbohydrate-binding modules that may contribute to the larvicidal function of the toxin.

    • Jacques-Philippe Colletier
    • Michael R. Sawaya
    • David S. Eisenberg
    Research
    Nature
    Volume: 539, P: 43-47

  • Prions can adopt a transmissible β-sheet-rich conformation and also form strains with different structural and biological properties. Polymorphic crystal structures of peptides from prion- and other amyloid-forming proteins suggest the structural basis for prion strains, revealing two potential mechanisms: packing and segmental polymorphism.

    • Jed J W Wiltzius
    • Meytal Landau
    • David Eisenberg
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 973-978

  • A computational method to design cyclic protein homo-oligomers has been developed. Using this approach, a series of idealized repeat proteins incorporating designed interfaces that direct their assembly into complexes possessing cyclic symmetry were fabricated. 15 out of 96 oligomers that were characterized experimentally were shown to be consistent with the computational model.

    • Jorge A. Fallas
    • George Ueda
    • David Baker
    Research
    Nature Chemistry
    Volume: 9, P: 353-360