Zobrazeno 1 - 10
of 118
pro vyhledávání: '"Ari Gafni"'
Autor:
Chun-Chieh Chang, John Christian Althaus, Cynthia J L Carruthers, Michael A Sutton, Duncan G Steel, Ari Gafni
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e82139 (2013)
Two amyloid-β peptides (Aβ40 and Aβ42) feature prominently in the extracellular brain deposits associated with Alzheimer's disease. While Aβ40 is the prevalent form in the cerebrospinal fluid, the fraction of Aβ42 increases in the amyloid deposi
Externí odkaz:
https://doaj.org/article/40eaee1b217641fe864128e163a21b12
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23970 (2011)
Understanding how amyloid-β peptide interacts with living cells on a molecular level is critical to development of targeted treatments for Alzheimer's disease. Evidence that oligomeric Aβ interacts with neuronal cell membranes has been provided, bu
Externí odkaz:
https://doaj.org/article/6187aad09a20494fb1a395ae9ddd34b4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860:1616-1624
The amyloid-β peptides (Aβ40 and Aβ42) feature prominently in the synaptic dysfunction and neuronal loss associated with Alzheimer's disease (AD). This has been proposed to be due either to interactions between Aβ and cell surface receptors affec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec8125a0f7303001152bcd4c4199dd13
https://doi.org/10.1016/j.bbamem.2018.03.017
https://doi.org/10.1016/j.bbamem.2018.03.017
Publikováno v:
Protein Science. 23:869-883
Amyloid-β peptide (Aβ) oligomers may represent the proximal neurotoxin in Alzheimer's disease. Single-molecule microscopy (SMM) techniques have recently emerged as a method for overcoming the innate difficulties of working with amyloid-β, includin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::087740b214e2b5b8fbfe9c9a8d59f5ac
https://doi.org/10.1002/pro.2479
https://doi.org/10.1002/pro.2479
Autor:
John Christian Althaus, Michael A. Sutton, Chun-Chieh Chang, Kathleen Wisser, Robin D. Johnson, Cynthia J. L. Carruthers, Duncan G. Steel, Joseph A. Schauerte, Ari Gafni
Publikováno v:
Biophysical Journal. 104:894-903
Soluble oligomers of the amyloid-β peptide have been implicated as proximal neurotoxins in Alzheimer’s disease. However, the identity of the neurotoxic aggregate(s) and the mechanisms by which these species induce neuronal dysfunction remain uncer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e916c0a15f178822d2d523823fe3a908
https://doi.org/10.1016/j.bpj.2012.12.051
https://doi.org/10.1016/j.bpj.2012.12.051
β-Amyloid (1–40) Peptide Interactions with Supported Phospholipid Membranes: A Single-Molecule Study
Publikováno v:
Biophysical Journal. 103(7):1500-1509
Recent evidence supports the hypothesis that the oligomers formed by the β-amyloid peptide early in its aggregation process are neurotoxic and may feature in Alzheimer’s disease. Although the mechanism underlying this neurotoxicity remains unclear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3dae6c87d6efb5338ab1a945947d1153
Autor:
Jeffrey R. Brender, Ayyalusamy Ramamoorthy, Ari Gafni, Duncan G. Steel, Edgar L. Lee, Kevin Hartman, Pamela T. Wong
Publikováno v:
Biophysical Journal. 100(3):685-692
Type II diabetes, in its late stages, is often associated with the formation of extracellular islet amyloid deposits composed of islet amyloid polypeptide (IAPP or amylin). IAPP is stored before secretion at millimolar concentrations within secretory
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e779d547c541a73452e0277c7f4cfaa2
Publikováno v:
Biochemistry. 49:3031-3039
The extracellular senile plaques prevalent in brain tissue in Alzheimer's disease (AD) are composed of amyloid fibrils formed by the Abeta peptide. These fibrils have been traditionally believed to be featured in neurotoxicity; however, numerous rece
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc95eb81de62d184a64490b79c537957
https://doi.org/10.1021/bi901444w
https://doi.org/10.1021/bi901444w
Publikováno v:
Biophysical Journal. 97(3):912-921
Amyloid diseases are traditionally characterized by the appearance of inter- and intracellular fibrillar protein deposits, termed amyloid. Historically, these deposits have been thought to be the etiology of the disease. However, recent evidence sugg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ba25e35fee0a0382d47eed3248cee68
Autor:
Ayyalusamy Ramamoorthy, Duncan G. Steel, Ari Gafni, Marchello A. Cavitt, Jeffrey R. Brender, Edgar L. Lee
Publikováno v:
Journal of the American Chemical Society. 130:6424-6429
Aggregation of Islet Amyloid Polypeptide (IAPP) has been implicated in the development of type II diabetes. Because IAPP is a highly amyloidogenic peptide, it has been suggested that the formation of IAPP amyloid fibers causes disruption of the cellu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::847cb38493cd151681e6ed1a03bbd00b
https://doi.org/10.1021/ja710484d
https://doi.org/10.1021/ja710484d