18:1 Cholesteryl ester

18:1 cholesteryl ester is a lipid of Sterol Lipids (ST) class. The involved functions are known as Gene-Environment Interaction.

Cross Reference

Introduction

To understand associated biological information of 18:1 Cholesteryl ester, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with 18:1 Cholesteryl ester?

There are no associated biomedical information in the current reference collection.

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with 18:1 Cholesteryl ester

MeSH term MeSH ID Detail
Hypothyroidism D007037 32 associated lipids
Starvation D013217 47 associated lipids
Niemann-Pick Diseases D009542 25 associated lipids
Hypertension, Malignant D006974 4 associated lipids
Total 4

PubChem Associated disorders and diseases

What pathways are associated with 18:1 Cholesteryl ester

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with 18:1 Cholesteryl ester?

There are no associated biomedical information in the current reference collection.

What functions are associated with 18:1 Cholesteryl ester?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with 18:1 Cholesteryl ester?

There are no associated biomedical information in the current reference collection.

What genes are associated with 18:1 Cholesteryl ester?

There are no associated biomedical information in the current reference collection.

What common seen animal models are associated with 18:1 Cholesteryl ester?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with 18:1 Cholesteryl ester

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Authors Title Published Journal PubMed Link
Merkel M et al. Lysosomal acid lipase. Assay and purification. 1999 Methods Mol. Biol. pmid:9918015
Chang CC et al. Recombinant acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) purified to essential homogeneity utilizes cholesterol in mixed micelles or in vesicles in a highly cooperative manner. 1998 J. Biol. Chem. pmid:9857049
Weinmann P et al. Quantitative analysis of cholesterol and cholesteryl esters in human atherosclerotic plaques using near-infrared Raman spectroscopy. 1998 Atherosclerosis pmid:9733218
Versluis AJ et al. Synthesis of a lipophilic daunorubicin derivative and its incorporation into lipidic carriers developed for LDL receptor-mediated tumor therapy. 1998 Pharm. Res. pmid:9587947
Shamburek RD et al. Intracellular trafficking of the free cholesterol derived from LDL cholesteryl ester is defective in vivo in Niemann-Pick C disease: insights on normal metabolism of HDL and LDL gained from the NP-C mutation. 1997 J. Lipid Res. pmid:9458266
Boer JM et al. Interactions between lifestyle-related factors and the ApoE polymorphism on plasma lipids and apolipoproteins. The EARS Study. European Atherosclerosis Research Study. 1997 Arterioscler. Thromb. Vasc. Biol. pmid:9327762
Lohse P et al. Human lysosomal acid lipase/cholesteryl ester hydrolase and human gastric lipase: site-directed mutagenesis of Cys227 and Cys236 results in substrate-dependent reduction of enzymatic activity. 1997 J. Lipid Res. pmid:9323599
Weaver AM et al. LDL receptor family-dependent and -independent pathways for the internalization and digestion of lipoprotein lipase-associated beta-VLDL by rat vascular smooth muscle cells. 1997 J. Lipid Res. pmid:9323593
Benoist F et al. Cholesteryl ester transfer protein mediates selective uptake of high density lipoprotein cholesteryl esters by human adipose tissue. 1997 J. Biol. Chem. pmid:9295295
Harrison EH et al. Size of the catalytically active unit of rat hepatic carboxylester lipase in the presence and absence of bile salt. 1997 Biochim. Biophys. Acta pmid:9295161