Zobrazeno 1 - 7 of 7 pro vyhledávání: '"Banafsheh Mehrazma"'
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Akademický článek
d-Amino Acid Pseudopeptides as Potential Amyloid-Beta Aggregation Inhibitors
Autor: Banafsheh Mehrazma, Stanley Opare, Anahit Petoyan, Arvi Rauk
Publikováno v: Molecules, Vol 23, Iss 9, p 2387 (2018)
A causative factor for neurotoxicity associated with Alzheimer’s disease is the aggregation of the amyloid-β (Aβ) peptide into soluble oligomers. Two all d-amino acid pseudo-peptides, SGB1 and SGD1, were designed to stop the aggregation. Molecula
Externí odkaz: https://doaj.org/article/2248a087b9104551bdaec3ee63e6d0e9
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3
A Unique Conformational Distortion Mechanism Drives Lipocalin 2 Binding to Bacterial Siderophores
Autor: Xiaojing Huang, Sladjana Slavkovic, Philip E. Johnson, Gary Sweeney, Derek J. Wilson, Banafsheh Mehrazma, Amy Botta, Cristina Lento, Erfei Song
Publikováno v: ACS Chemical Biology. 15:234-242
Lcn2 is a host defense protein induced via the innate immune response to sequester iron-loaded bacterial siderophores. However, excess or prolonged elevation of Lcn2 levels can induce adverse cellular effects, including oxidative stress and inflammat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::519ab21bfae92cdecb33cc7556c226ec
https://doi.org/10.1021/acschembio.9b00820
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4
Pseudo-peptide amyloid-β blocking inhibitors: molecular dynamics and single molecule force spectroscopy study
Autor: Anahit Petoyan, Banafsheh Mehrazma, Arvi Rauk, Jennifer Lou, Stanley K.A. Opare, Francis T. Hane, Zoya Leonenko, Morgan Robinson
Publikováno v: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865:1707-1718
By combining MD simulations and AFS experimental technique, we demonstrated a powerful approach for rational design and single molecule testing of novel inhibitor molecules which can block amyloid-amyloid binding - the first step of toxic amyloid oli
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e464367fa9bc9dbd0d1ea5ac9d2c5c9
https://doi.org/10.1016/j.bbapap.2017.07.022
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5
Pseudopeptide Amyloid Aggregation Inhibitors: In Silico, Single Molecule and Cell Viability Studies
Autor: Michael A. Beazely, Zoya Leonenko, Banafsheh Mehrazma, Arvi Rauk, Jennifer Lou, Morgan Robinson
Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 3
International Journal of Molecular Sciences, Vol 22, Iss 1051, p 1051 (2021)
Neurodegeneration in Alzheimer&rsquo
s disease (AD) is defined by pathology featuring amyloid-&beta
(A&beta
) deposition in the brain. A&beta
monomers themselves are generally considered to be nontoxic, but misfold into &beta
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e50a86665cca054eed05dedec80c026c
https://doi.org/10.3390/ijms22031051
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6
Interaction of the N-AcAβ(13–23)NH2 segment of the beta amyloid peptide with beta-sheet-blocking peptides: site and edge specificity
Autor: Arvi Rauk, Anahit Petoyan, Banafsheh Mehrazma, Stanley K.A. Opare
Publikováno v: Canadian Journal of Chemistry. 94:583-592
The region encompassing residues 13–23 of the amyloid beta peptide (Aβ(13–23)) of Alzheimer’s disease is the self-recognition site that initiates toxic oligomerization and fibrillization and also is the site of interaction of Aβ with many oth
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0b7332217e7c200a12e055091fa2d8ba
https://doi.org/10.1139/cjc-2016-0033
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7
Molecular dynamics study of the monomers and dimers of N-AcAβ(13–23)NH2: on the effect of pH on the aggregation of the amyloid beta peptide of Alzheimer’s disease
Autor: Anahit Petoyan, Banafsheh Mehrazma, Arvi Rauk, Stanley K.A. Opare
Publikováno v: Canadian Journal of Chemistry. 94:273-281
The region encompassed by residues 13–23 of the amyloid beta peptide (Aβ(13–23)) of Alzheimer’s disease is the self-recognition site that initiates toxic oligomerization and fibrillization and also is the site of interaction of Aβ with many o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80e0094a07b7d45ebf1faf0a87cf82c9
https://doi.org/10.1139/cjc-2015-0036
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