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Sterol

About: Sterol is a research topic. Over the lifetime, 8117 publications have been published within this topic receiving 309926 citations. The topic is also known as: sterols & sterol lipids.


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Journal ArticleDOI
TL;DR: Daily consumption of 1.6 g PS in low-fat FM efficiently lowers LDL cholesterol in subjects with moderate hypercholesterolemia without deleterious effects on biomarkers of oxidative stress.

115 citations

Journal ArticleDOI
TL;DR: It is concluded that the CoA-dependent esterification rate of cholesterol is at least 60 times greater than that of beta-sitosterol.

115 citations

01 Jan 2005
TL;DR: In this paper, the authors provide a brief review of cholesterol-dependent cytolytic activity of cholesterol dependent cytolysins, commonly known as thiol-activated toxins.
Abstract: Cholesterol, which is required for viability and cell proliferation, is a major sterol of mammalian cells. More than 90% of cellular cholesterol is located at the plasma membrane. Several microorganisms and bacterial products target lipid rafts, membrane microdomains of eukaryotic cells enriched in cholesterol, sphingolipids, and certain proteins. Cholesterol confined in lipid rafts is a crucial component required by microorganisms, directly or indirectly, to enter or exit the intracellular compartment. It is also required for cytolytic activity of cholesterol-dependent cytolysins formerly known as thiol-activated toxins. The object of this review is to provide a brief

115 citations

Journal ArticleDOI
01 Oct 2011-Traffic
TL;DR: It is concluded that the role of Osh proteins in non‐vesicular sterol transport between the PM, ER and lipid droplets is either minimal, or subsumed by other mechanisms and that Osh proteins regulate the organization of sterols at the PM.
Abstract: Sterol transport between the endoplasmic reticulum (ER) and plasma membrane (PM) occurs by an ATP-dependent, non-vesicular mechanism that is presumed to require sterol transport proteins (STPs). In Saccharomyces cerevisiae, homologues of the mammalian oxysterol-binding protein (Osh1–7) have been proposed to function as STPs. To evaluate this proposal we took two approaches. First we used dehydroergosterol (DHE) to visualize sterol movement in living cells by fluorescence microscopy. DHE was introduced into the PM under hypoxic conditions and observed to redistribute to lipid droplets on growing the cells aerobically. Redistribution required ATP and the sterol acyltransferase Are2, but did not require PM-derived transport vesicles. DHE redistribution occurred robustly in a conditional yeast mutant (oshΔ osh4-1ts) that lacks all functional Osh proteins at 37°C. In a second approach we used a pulse-chase protocol to analyze the movement of metabolically radiolabeled ergosterol from the ER to the PM. Arrival of radiolabeled ergosterol at the PM was assessed in isolated PM-enriched fractions as well by extracting sterols from intact cells with methyl-β-cyclodextrin. These experiments revealed that whereas ergosterol is transported effectively from the ER to the PM in Osh-deficient cells, the rate at which it moves within the PM to equilibrate with the methyl-β-cyclodextrin extractable sterol pool is slowed. We conclude (i) that the role of Osh proteins in nonvesicular sterol transport between the PM, ER and lipid droplets is either minimal, or subsumed by other mechanisms and (ii) that Osh proteins regulate the organization of sterols at the PM.

115 citations

Journal ArticleDOI
TL;DR: It is demonstrated that the structure of membrane-inserted PFO at low and neutral pH was similar as judged by the effect of phospholipid and sterol structure upon PFO properties and membrane interaction, however, low pH enhanced PFO membrane binding, oligomerization, and pore formation.

115 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023104
2022250
2021131
2020154
2019151
2018117