Small molecule probes of protein aggregation
Understanding the mechanisms of amyloid formation and toxicity remain major challenges. Although substantial progress has been made in the development of methods able to identify the species formed during self-assembly and to describe the kinetic ...
Lydia M. Young, A. Ashcroft, S. Radford
semanticscholar +1 more source
Study of cosolvent-induced α-chymotrypsin fibrillogenesis: Does protein surface hydrophobicity trigger early stages of aggregation reaction? [PDF]
The misfolding of specific proteins is often associated with their assembly into fibrillar aggregates, commonly termed amyloid fibrils. Despite the many efforts expended to characterize amyloid formation in vitro, there is no deep knowledge about the ...
A Ahmad +66 more
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Visual Molecular Dynamics Investigations of the Impact of Hydrophobic Nanoparticles on Prognosis of Alzheimer’s Disease and Cancers [PDF]
The possible impact of hydrophobic lectin nanoparticles on the prognosis and progression of Alzheimer's disease (AD) and cancers was investigated by Visual Molecular Dynamics (VMD) computer modeling programs available from the Beckmann Advanced ...
I. C. Baianu, M Charles, V. I. Prisecaru
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Protein aggregation: folding aggregates, inclusion bodies and amyloid
Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve beta sheets.
openaire +2 more sources
ER stress causes widespread protein aggregation and prion formation
Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER stress. This activates the unfolded protein response (UPR), which alters the expression of many genes involved in ER quality control.
Norfadilah Hamdan +2 more
semanticscholar +1 more source
Polysorbates, peroxides, protein aggregation, and immunogenicity – a growing concern
Aggregation can have a number of deleterious effects on biotherapeutics including the loss of efficacy, the induction of unwanted immunogenicity, altered pharmacokinetics, and reduced shelf life. Aggregation is ameliorated by the inclusion of surfactants
Edward T. Maggio
doaj
Protein folding, protein structure and the origin of life: Theoretical methods and solutions of dynamical problems [PDF]
Theoretical methods and solutions of the dynamics of protein folding, protein aggregation, protein structure, and the origin of life are discussed. The elements of a dynamic model representing the initial stages of protein folding are presented.
Weaver, D. L.
core +1 more source
The proteome of Plasmodium falciparum exhibits a marked propensity for aggregation. This characteristic results from the parasite’s AT-rich genome, which encodes numerous proteins with long asparagine-rich stretches and low structural complexity, which ...
Yunuen Avalos-Padilla +14 more
doaj +1 more source
Investigation on the surface hydrophobicity and aggregation kinetics of human calprotectin in the presence of calcium [PDF]
Calcium and zinc binding protein, calprotectin is a multifunctional protein with broad spectrum antimicrobial and antitumoural activity. It was purified from human neutrophil, using a two-step ion exchange chromatography.
امانی, مجتبی +5 more
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