Výsledky vyhledávání

N-Terminal Modified Aβ Variants Enable Modulations to the Structures and Cytotoxicity Levels of Wild-Type Aβ Fibrils through Cross-Seeding

Autor: Liliya Vugmeyster, Letticia Cruceta, Wei Qiang, Dan Fai Au, Zhi-Wen Hu

Publikováno v: ACS Chem Neurosci

Post-translational modifications (PTMs) of β-amyloid (Aβ) peptides are considered as triggering factors in sporadic Alzheimer's disease. However, studies to show the influence of pre-existing PTM-Aβ fibrils on wild-type Aβ peptides, which directl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3582227c5714e8effe1d01e88b231d48
https://doi.org/10.1021/acschemneuro.0c00316

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Comparative hydrophobic core dynamics between wild-type amyloid-β fibrils, glutamate-3 truncation, and serine-8 phosphorylation

Autor: Dan Fai Au, Liliya Vugmeyster, Matthew C. Smith, Dmitry Ostrovsky

Publikováno v: Chemphyschem

Post-translational modifications (PTMs) of amyloid-β (Aβ) species are implicated in the modulation of overall toxicities and aggregation propensities. We investigated the internal dynamics in the hydrophobic core of the truncated ΔE3 mutant fibril

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::133287145ec3797160eed56d35b09577
https://europepmc.org/articles/PMC9484291/

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Molecular structure of an N-terminal phosphorylated β-amyloid fibril

Autor: Dan Fai Au, Zhi-Wen Hu, Yan Sun, Wei Qiang, Dmitry Ostrovsky, Liliya Vugmeyster

Publikováno v: Proceedings of the National Academy of Sciences. 116:11253-11258

The structural polymorphism in β-amyloid (Aβ) plaques from Alzheimer disease (AD) has been recognized as an important pathological factor. Plaques from sporadic AD patients contain fibrillar deposits of various amyloid proteins/peptides, including

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7142376db9d067cf86f243c8b5588e5d
https://doi.org/10.1073/pnas.1818530116

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Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils

Autor: Dan Fai Au, Dmitry Ostrovsky, Riqiang Fu, Liliya Vugmeyster

Publikováno v: Journal of Biological Chemistry. 294:5840-5853

Amyloid fibril deposits observed in Alzheimer's disease comprise amyloid-β (Aβ) protein possessing a structured hydrophobic core and a disordered N-terminal domain (residues 1–16). The internal flexibility of the disordered domain is likely essen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2311ba856b800f572bd2284f500f29fd
https://doi.org/10.1074/jbc.ra118.006559

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Deuteron Solid-State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-Terminal Domain of Amyloid-β Fibrils

Autor: Liliya Vugmeyster, Dan Fai Au, Riqiang Fu, Dmitry Ostrovsky

Publikováno v: Chemphyschem

We employed deuterium solid-state NMR techniques under static conditions to discern the details of the μs-ms timescale motions in the flexible N-terminal subdomain of Aβ(1-40) amyloid fibrils, which spans residues 1–16. In particular, we utilized

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a776d316672bb8063f44da0ebafcc81
https://pubmed.ncbi.nlm.nih.gov/31087613

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Akademický článek

Molecular structure of an N-terminal phosphorylated β-amyloid fibril.

Autor: Zhi-Wen Hu, Vugmeyster, Liliya, Dan Fai Au, Ostrovsky, Dmitry, Yan Sun, Wei Qiang

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America; 6/4/2019, Vol. 116 Issue 23, p11253-11258, 6p

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