Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Liliya Vugmeyster"'
Publikováno v:
Magnetochemistry, Vol 9, Iss 1, p 33 (2023)
Protein methyl groups can participate in multiple motional modes on different time scales. Sub-nanosecond to nano-second time scale motions of methyl axes are particularly challenging to detect for small proteins in solutions. In this work we employ
Externí odkaz:
https://doaj.org/article/f94c805ab4b641e495120d4e21764be8
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
We utilized the 2H Chemical Exchange Saturation Transfer (CEST) technique under magic angle spinning (MAS) conditions to demonstrate the feasibility of the method for studies of slow motions in the solid state. For the quadrupolar anisotropic interac
Externí odkaz:
https://doaj.org/article/33d5e801b914487abeafcb204990cdd3
Publikováno v:
The Journal of Physical Chemistry B. 127:2887-2899
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f06bc64e2d4a82812c068b0eba495229
https://doi.org/10.1021/acs.jpcb.2c07817
https://doi.org/10.1021/acs.jpcb.2c07817
Publikováno v:
Journal of Magnetic Resonance. :107493
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bba3ab41a394294256d0f425923d251a
https://doi.org/10.1016/j.jmr.2023.107493
https://doi.org/10.1016/j.jmr.2023.107493
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
https://doi.org/10.1021/acschemneuro.0c00316
Publikováno v:
Chemphyschem
We provide an experimental and computational framework for (2)H quadrupolar chemical exchange saturation transfer NMR experiments (Q-CEST) under static solid-state conditions for the quantification of dynamics on μs-ms timescales. Simulations using
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f6b685c35258b79f1af8ab2e6fe4715
https://doi.org/10.1002/cphc.201901053
https://doi.org/10.1002/cphc.201901053
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/
https://europepmc.org/articles/PMC9484291/
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
We utilized the 2H Chemical Exchange Saturation Transfer (CEST) technique under magic angle spinning (MAS) conditions to demonstrate the feasibility of the method for studies of slow motions in the solid state. For the quadrupolar anisotropic interac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb6003a308b2e0c2755efc6e37c04ee2
https://www.frontiersin.org/articles/10.3389/fmolb.2021.705572/full
https://www.frontiersin.org/articles/10.3389/fmolb.2021.705572/full
Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus
Autor:
Brian Kierl, Zhi-Wen Hu, Dmitry Ostrovsky, Wei Qiang, Dan F. Au, Riqiang Fu, Liliya Vugmeyster
Publikováno v:
Biophys J
We investigate the variability in the dynamics of the disordered N-terminal domain of amyloid-β fibrils (Aβ), comprising residues 1–16 of Aβ(1–40), due to post-translational modifications and mutations in the β-bend regions known to modulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6429c2cb09938e6335b83bae4f8446b5
https://doi.org/10.1016/j.bpj.2019.09.004
https://doi.org/10.1016/j.bpj.2019.09.004
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
https://doi.org/10.1073/pnas.1818530116