Results 41 to 50 of about 7,628,689 (242)

Protein aggregation in silico [PDF]

open access: yesTrends in Biotechnology, 2007
Protein aggregation is a challenge to the successful manufacture of protein therapeutics; it can impose severe limitations on purification yields and compromise formulation stability. Advances in computer power, and the wealth of computational studies pertaining to protein folding, have facilitated the development of molecular simulation as a tool to ...
Troy, Cellmer   +3 more
openaire   +2 more sources

Neuroinflammation and protein aggregation co-localize across the frontotemporal dementia spectrum

open access: yesBrain : a journal of neurology, 2020
Bevan-Jones, Cope et al. report that neuroinflammation co-localizes with protein aggregation in all major types of frontotemporal dementia, both in vivo with positron emission tomography, and at post mortem. In vivo neuroinflammation patterns are disease-
W. R. Bevan-Jones   +18 more
semanticscholar   +1 more source

Lipid oxidation in foods and its implications on proteins

open access: yesFrontiers in Nutrition, 2023
Lipids in foods are sensitive to various environmental conditions. Under light or high temperatures, free radicals could be formed due to lipid oxidation, leading to the formation of unstable food system.
Lianxin Geng   +3 more
doaj   +1 more source

Detergent-mediated protein aggregation [PDF]

open access: yesChemistry and Physics of Lipids, 2013
Because detergents are commonly used to solvate membrane proteins for structural evaluation, much attention has been devoted to assessing the conformational bias imparted by detergent micelles in comparison to the native environment of the lipid bilayer.
Chris, Neale   +5 more
openaire   +2 more sources

Liquid-Liquid Phase Separation and its Mechanistic Role in Pathological Protein Aggregation.

open access: yesJournal of Molecular Biology, 2020
Liquid-liquid phase separation (LLPS) of proteins underlies the formation of membrane-less organelles. While it has been recognized for some time that these organelles are of key importance for normal cellular functions, a growing number of recent ...
W. M. Babinchak, W. Surewicz
semanticscholar   +1 more source

An in vivo platform to select and evolve aggregation-resistant proteins

open access: yesNature Communications, 2020
Protein aggregation remains a significant challenge for manufacturing of protein biopharmaceuticals. Here, the authors demonstrate the use of directed evolution and an assay for in vivo innate protein aggregation-propensity to generate aggregation ...
Jessica S. Ebo   +14 more
doaj   +1 more source

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]

open access: yes, 2017
The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M   +2 more
core   +2 more sources

Protein aggregation and neurodegeneration [PDF]

open access: yesMethods, 2011
In 1997 Carrell and Lomas put forth the concept that many disorders, which appeared to be unlinked, arose from the same general mechanism that involved the abnormal unfolding and aggregation of various underlying proteins [1]. The flux of proteins through pathways for formation of amyloid-like aggregates was proposed to be the mechanism for ...
Katie J, Mayo, Douglas M, Cyr
openaire   +2 more sources

A3DyDB: exploring structural aggregation propensities in the yeast proteome

open access: yesMicrobial Cell Factories, 2023
Background The budding yeast Saccharomyces cerevisiae (S. cerevisiae) is a well-established model system for studying protein aggregation due to the conservation of essential cellular structures and pathways found across eukaryotes.
Javier Garcia-Pardo   +6 more
doaj   +1 more source

O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease. [PDF]

open access: yes, 2015
Several aggregation-prone proteins associated with neurodegenerative diseases can be modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-synuclein, is a toxic aggregating protein associated with synucleinopathies ...
Ambroso, Mark R   +8 more
core   +2 more sources

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