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Xian-Cheng Jiang

Researcher at SUNY Downstate Medical Center

Publications -  185
Citations -  12216

Xian-Cheng Jiang is an academic researcher from SUNY Downstate Medical Center. The author has contributed to research in topics: Phospholipid transfer protein & Cholesterol. The author has an hindex of 56, co-authored 181 publications receiving 11124 citations. Previous affiliations of Xian-Cheng Jiang include Fudan University & Columbia University.

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Cholesterol Efflux and Atheroprotection Advancing the Concept of Reverse Cholesterol Transport

TL;DR: High-density lipoprotein has been proposed to have several antiatherosclerotic properties, including the ability to mediate macrophage cholesterol efflux, antioxidant capacity, antiinflammatory properties, nitric oxide–promoting activity, and ability to transport proteins with their own intrinsic biological activities.
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Targeted mutation of plasma phospholipid transfer protein gene markedly reduces high-density lipoprotein levels

TL;DR: Reduced plasma PLTP activity causes markedly decreased HDL lipid and apoprotein, demonstrating the importance of transfer of surface components of TRL in the maintenance of HDL levels.
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Plasma Sphingomyelin Level as a Risk Factor for Coronary Artery Disease

TL;DR: Plasma SM levels could be a marker for atherogenic remnant lipoprotein accumulation and may predict lipop protein susceptibility to arterial wall sphingomyelinase, and the findings indicate that human plasma SM levels are positively and independently related to CAD.
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Ceramide is a cardiotoxin in lipotoxic cardiomyopathy

TL;DR: In this paper, de novo ceramide biosynthesis was inhibited pharmacologically by myriocin and genetically by heterozygous deletion of LCB1, a subunit of serine palmitoyltransferase (SPT).
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Secretory Sphingomyelinase, a Product of the Acid Sphingomyelinase Gene, Can Hydrolyze Atherogenic Lipoproteins at Neutral pH IMPLICATIONS FOR ATHEROSCLEROTIC LESION DEVELOPMENT

TL;DR: It is shown that S-SMase can hydrolyze and aggregate native plasma LDL at pH 5.5 but not at pH 7.4, making this enzyme a leading candidate for the arterial wall SMase that hydrolyzes LDL-SM and causes subendothelial LDL aggregation.