Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Lea C Paslay"'
Autor:
Amit Kumar, Rebekah L Bullard, Pritesh Patel, Lea C Paslay, Dipti Singh, Ewa A Bienkiewicz, Sarah E Morgan, Vijayaraghavan Rangachari
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18759 (2011)
Amyloid-β (Aβ) peptide aggregation is known to play a central role in the etiology of Alzheimer's disease (AD). Among various aggregates, low-molecular weight soluble oligomers of Aβ are increasingly believed to be the primary neurotoxic agents re
Externí odkaz:
https://doaj.org/article/b5812ea5adbd470cb224556fe18cc419
Autor:
Daniel F. Lyons, Sarah E. Morgan, Lea C. Paslay, Amit Kumar, Vijayaraghavan Rangachari, John J. Correia
Publikováno v:
Journal of Biological Chemistry. 287:21253-21264
Aggregates of amyloid-β (Aβ) peptides have been implicated in the etiology of Alzheimer disease. Among the different forms of Aβ aggregates, low molecular weight species ranging between ~2- and 50-mers, also called "soluble oligomers," have emerge
Autor:
Sabine Heinhorst, Mohamed O. Elasri, Veena Koul, Charles L. McCormick, Brooks A. Abel, Sarah E. Exley, Veena Choudhary, Sarah E. Morgan, Tyler Brown, Gyan S. Sahukhal, Lea C. Paslay
Publikováno v:
Biomacromolecules, vol 16, iss 12
Naturally occurring antimicrobial peptides (AMPs) display the ability to eliminate a wide variety of bacteria, without toxicity to the host eukaryotic cells. Synthetic polymers containing moieties mimicking lysine and arginine components found in AMP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0df86630b21002538d7488179ebd6b3a
https://europepmc.org/articles/PMC4825813/
https://europepmc.org/articles/PMC4825813/
Publikováno v:
Polymer. 51:738-747
The effects of polymer conformation and degree of substitution on miscibility, morphology and mechanical properties of solution blended systems containing polyphenylsulfone and copolymers of phenylketone substituted p-phenylene with m-phenylene were
Autor:
Sarah E. Morgan, Gordon C. Cannon, Lea C. Paslay, Daniel A. Savin, Leo Falgout, Sabine Heinhorst
Publikováno v:
Biomacromolecules. 14(7)
Hydrophobins are small fungal proteins that self-assemble at hydrophobic/hydrophilic interfaces to form stable, amyloid membranes that are resistant to denaturation. Their remarkable surface activity has driven intense research for their potential ut
Autor:
Vijayaraghavan Rangachari, Lea C. Paslay, Ewa A. Bienkiewicz, Amit Kumar, Rebekah L. Rice, Sarah E. Morgan, Pritesh Patel, Dipti Singh
Publikováno v:
Biophysical Journal. 100(3)
In Alzheimer's disease (AD), soluble oligomers of amyloid-β (Aβ) are believed to be primary neurotoxic species responsible for early synaptic dysfunction and cognitive decline. The rate of Aβ aggregation is known to be significantly affected in th
Autor:
Lea C. Paslay, John J. Correia, Sarah E. Morgan, Vijayaraghavan Rangachari, Amit Kumar, Daniel F. Lyons
Publikováno v:
Biophysical Journal. 104:48a-49a
Aggregates of amyloid-β (Aβ) peptides have been implicated in the etiology of Alzheimer disease (AD). Among the different forms of Aβ aggregates, low molecular weight species ranging between 2- and 50-mers, also called “soluble oligomers,” hav
Autor:
Lea C. Paslay, Sarah E. Morgan, Ewa A. Bienkiewicz, Vijayaraghavan Rangachari, Rebekah L. Bullard, Dipti Singh, Amit Kumar, Pritesh Patel
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18759 (2011)
PLoS ONE
PLoS ONE
Amyloid-β (Aβ) peptide aggregation is known to play a central role in the etiology of Alzheimer's disease (AD). Among various aggregates, low-molecular weight soluble oligomers of Aβ are increasingly believed to be the primary neurotoxic agents re