Results 11 to 20 of about 737,709 (296)

Increased Aggregation Is More Frequently Associated to Human Disease-Associated Mutations Than to Neutral Polymorphisms. [PDF]

open access: yesPLoS Computational Biology, 2015
Protein aggregation is a hallmark of over 30 human pathologies. In these diseases, the aggregation of one or a few specific proteins is often toxic, leading to cellular degeneration and/or organ disruption in addition to the loss-of-function resulting ...
Greet De Baets   +3 more
doaj   +1 more source

A Conceptual Framework for Integrating Cellular Protein Folding, Misfolding and Aggregation

open access: yesLife, 2021
How proteins properly fold and maintain solubility at the risk of misfolding and aggregation in the cellular environments still remains largely unknown.
Seong Il Choi, Baik L. Seong
doaj   +1 more source

α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies

open access: yesNeural Regeneration Research, 2023
The misfolding and aggregation of α-synuclein is the general hallmark of a group of devastating neurodegenerative pathologies referred to as synucleinopathies, such as Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy.
Alessandra Bigi   +2 more
doaj   +1 more source

Protein aggregation and bioprocessing [PDF]

open access: yesThe AAPS Journal, 2006
Protein aggregation is a common issue encountered during manufacture of biotherapeutics. It is possible to influence the amount of aggregate produced during the cell culture and purification process by carefully controlling the environment (eg, media components) and implementing appropriate strategies to minimize the extent of aggregation.
Mary E M, Cromwell   +2 more
openaire   +2 more sources

Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]

open access: yes, 2015
The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio   +9 more
core   +2 more sources

Aggregation of polyQ proteins is increased upon yeast aging and affected by Sir2 and Hsf1: novel quantitative biochemical and microscopic assays. [PDF]

open access: yesPLoS ONE, 2012
Aging-related neurodegenerative disorders, such as Parkinson's, Alzheimer's and Huntington's diseases, are characterized by accumulation of protein aggregates in distinct neuronal cells that eventually die. In Huntington's disease, the protein huntingtin
Aviv Cohen   +3 more
doaj   +1 more source

Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]

open access: yes, 2015
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection.
Carver, John A.   +3 more
core   +1 more source

Non-Arrhenius Protein Aggregation [PDF]

open access: yesThe AAPS Journal, 2013
Protein aggregation presents one of the key challenges in the development of protein biotherapeutics. It affects not only product quality but also potentially impacts safety, as protein aggregates have been shown to be linked with cytotoxicity and patient immunogenicity.
Wei, Wang, Christopher J, Roberts
openaire   +2 more sources

Aggregation is a Context-Dependent Constraint on Protein Evolution

open access: yesFrontiers in Molecular Biosciences, 2021
Solubility is a requirement for many cellular processes. Loss of solubility and aggregation can lead to the partial or complete abrogation of protein function. Thus, understanding the relationship between protein evolution and aggregation is an important
Michele Monti   +9 more
doaj   +1 more source

Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Caenorhabditis elegans Lysates [PDF]

open access: yes, 2018
Protein aggregation is a hallmark of several neurodegenerative diseases and is associated with impaired protein homeostasis. This imbalance is caused by the loss of the protein's native conformation, which ultimately results in its aggregation or ...
Mata Cabana, Alejandro   +3 more
core   +2 more sources

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