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Journal ArticleDOI

The role of lipid-protein interactions in amyloid-type protein fibril formation.

TLDR
The present review summarizes the principal factors responsible for the enhancement of fibril formation in a membrane environment, viz. structural transformation of polypeptide chain into a partially folded conformation, increase of the local concentration of a protein upon its membrane binding, and aggregation-favoring orientation of the bound protein.
About
This article is published in Chemistry and Physics of Lipids.The article was published on 2006-06-01. It has received 267 citations till now. The article focuses on the topics: Protein tertiary structure & Protein structure.

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Citations
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Journal ArticleDOI

The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization.

TL;DR: The γ-secretase complex and its cell surface localization, in the absence of an effect on Notch, is studied to avoid side-effects caused by EP2 receptor.
Journal ArticleDOI

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

TL;DR: This review will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality.
Journal ArticleDOI

Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide

TL;DR: It is shown that extracellular soluble Aβ at concentrations as low as 1 nM was taken up by murine cortical neurons and neuroblastoma cells but not by human embryonic kidney (HEK293) cells, and then concentrated into endosomes/lysosomes.
References
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Journal ArticleDOI

Natively unfolded proteins: a point where biology waits for physics.

TL;DR: Results of this analysis showed that intrinsically unstructured proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity, and the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globule, premolten globules, and random coils) is discussed.
Journal ArticleDOI

Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes

TL;DR: It is reported that α-synuclein binds to small unilamellarospholipid vesicles containing acidic phospholipids, but not to vesicular charges with a net neutral charge, consistent with a role in vesicle function at the presynaptic terminal.
Book ChapterDOI

Molten globule and protein folding.

TL;DR: It is predicted and confirmed experimentally that the molten globule state can exist in a living cell and plays an important role in a number of physiological processes.
Journal ArticleDOI

How lipids affect the activities of integral membrane proteins

TL;DR: The role of non-annular, or 'co-factor' lipids, tightly bound to membrane proteins, is described, as well as the effects of charged lipids on ion concentrations close to the surface of the bilayer.
Journal ArticleDOI

Protein aggregation: folding aggregates, inclusion bodies and amyloid

TL;DR: 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.
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