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Journal ArticleDOI

Role of the cell membrane interface in modulating production and uptake of Alzheimer's beta amyloid protein.

TLDR
The aim of this review is to highlight and summarize recent literature that have contributed insight into the implications of altered membrane composition on amyloid precursor protein (APP) proteolysis, production of Aβ, its internalization in to cells via permeabilization and receptor mediated uptake.
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This article is published in Biochimica et Biophysica Acta.The article was published on 2018-09-01. It has received 45 citations till now. The article focuses on the topics: Amyloid precursor protein & Protein aggregation.

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Plasma membrane integrity in health and disease: significance and therapeutic potential

TL;DR: In this paper, the authors focus on the existence of membrane disruptions and repair mechanisms in both physiological and pathological conditions, and across multiple cell types, albeit to different degrees, and emphasise the widespread potential of targeting plasma membrane repair mechanisms for therapeutic purposes.
Journal ArticleDOI

Amylin and beta amyloid proteins interact to form amorphous heterocomplexes with enhanced toxicity in neuronal cells.

TL;DR: It is demonstrated that hIAPP promotes Aβ oligomerization and formation of small oligomer and large aggregate heterocomplexes, and rIAPP exhibited reductions in Aβ induced neuronal cell death that was independent of its ability to interact with Aβ and form heterocom complex; suggesting mediation by other pathways.
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Plasmalogen-Based Liquid Crystalline Multiphase Structures Involving Docosapentaenoyl Derivatives Inspired by Biological Cubic Membranes

TL;DR: In this article, the spontaneous self-assembly of bio-inspired, custom-produced docosapentaenoyl (DPA) plasmenyl (ether) and ester phospholipids in aqueous environment (pH 7) by synchrotron small-angle X-ray scattering (SAXS) and cryogenic transmission electron microscopy (cryo-TEM).
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Role of Cholesterol on Binding of Amyloid Fibrils to Lipid Bilayers.

TL;DR: It is shown that electrostatic interactions play an important role in fibril-bilayer binding and cholesterol modulates this interaction, and the interaction between positive residues and lipid head groups becomes more favorable in the presence of cholesterol.
References
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Journal ArticleDOI

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

TL;DR: An apparently full-length complementary DNA clone coding for the A4 polypeptide is isolated and sequenced and suggests that the cerebral amyloid deposited in Alzheimer's disease and aged Down's syndrome is caused by aberrant catabolism of a cell-surface receptor.
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The MARTINI force field : Coarse grained model for biomolecular simulations

TL;DR: An improved and extended version of the coarse grained lipid model is presented, coined the MARTINI force field, based on the reproduction of partitioning free energies between polar and apolar phases of a large number of chemical compounds to reproduce the free energies of these chemical building blocks.
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Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide.

TL;DR: Findings in other neurodegenerative diseases indicate that a broadly similar process of neuronal dysfunction is induced by diffusible oligomers of misfolded proteins.
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Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

TL;DR: It is shown that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomer regardless of sequence, suggesting they share a common mechanism of toxicity.
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Update of the CHARMM All-Atom Additive Force Field for Lipids: Validation on Six Lipid Types

TL;DR: The presented lipid FF is developed and applied to phospholipid bilayers with both choline and ethanolamine containing head groups and with both saturated and unsaturated aliphatic chains and is anticipated to be of utility for simulations of pure lipid systems as well as heterogeneous systems including membrane proteins.
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