Serum uric acid and lipid profiles in sporadic Creutzfeldt–Jakob disease

Chen, Shuai; He, Shuang; Shang, Junkui; Ma, Mingming; Xu, Chao; Shi, Xiaohong; Zhang, Jiewen

doi:10.1016/j.clinbiochem.2015.09.017

Cited by 4 publications

(1 citation statement)

References 14 publications

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“…Furthermore, the damage of proteins, lipids and DNA by reactive oxygen species (ROS) precede the appearance of a major hallmark of these pathologies, amyloid fibril formation by specific proteins, Aβ peptide (AD), α-synuclein (PD), prion protein (CJD), lysozyme (SA), etc. [1][2][3][4]. To exemplify, Aβ peptide interactions with transition metal ions (viz.…”

Section: Introductionmentioning

confidence: 99%

Fluorescence study of the effect of the oxidized phospholipids on amyloid fibril formation by the apolipoprotein A-I N-terminal fragment

Vus

Girych

Trusova

et al. 2017

Chemical Physics Letters

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The effects of the oxidized phospholipids (oxPLs) on amyloid fibril formation by the apolipoprotein A-I variant 1-83/G26R have been investigated using Thioflavin T fluorescence assay. All types of the PoxnoPC assemblies (premicellar aggregates, micelles, lipid bilayer vesicles) induced the enhancement the 1-83/G26R fibrillization, although PazePC micelles completely prevented protein aggregation at low proteinto-lipid molar ratios. Furthermore, 1-83/G26R fibrillization in the presence of the oxPLs was accompanied by the retardation of amyloid nucleation and elongation. Notably, the ability of PazePC to inhibit the formation of 1-83/G26R fibrils was explained by the protein-lipidelectrostatic interactions, stabilizing the α-helical structure of membrane/micelle-associated 1-83/G26R.

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Section: Introductionmentioning

confidence: 99%