Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Computational analysis and enzyme assay of inhibitor response to disease single nucleotide polymorphisms (SNPs) in lipoprotein lipase.

Journal of bioinformatics and computational biology - 1 Oct 2016

He Deyong, Huang Ling, Xu Yaping, Pan Xiaoliang, Liu Lijun

Abstract excerpt

Lipoprotein lipase (LPL) is the rate-limiting enzyme for the hydrolysis of the triglyceride (TG) core of circulating TG-rich lipoproteins, chylomicrons, and very low-density lipoproteins. The enzyme has been established as an efficacious and safe therapeutic target for the management of obesity. Here, a systematic profile of the lipase inhibitor response of three anti-obesity agents (Orlistat, Lipstatin, and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Drug Evaluation, Preclinical
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lactones

Share to Lipoprotein Lipase

Share to Models, Molecular

Share to Mutation, Missense

Share to Obesity

Share to Protein Conformation

Source

Identifiers

PMID: 27427383
DOI: 10.1142/S0219720016500281

Genes

LPL

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computational analysis and enzyme assay of inhibitor response to disease single nucleotide polymorphisms (SNPs) in lipoprotein lipase.PMID 27427383Read ↗

Lipoprotein lipase: A bioinformatics criterion for assessment of mutations as a risk factor for cardiovascular disease.Semantic proximity Read ↗

Comprehensive in-silico analysis of deleterious SNPs in APOC2 and APOA5 and their differential expression in cancer and cardiovascular diseases conditions.Semantic proximity Read ↗

Genetic and structure-function studies of missense mutations in human endothelial lipase.Semantic proximity Read ↗

Pathogenic classification of LPL gene variants reported to be associated with LPL deficiency.Semantic proximity Read ↗

Clinical features and functions of a novel Lpl mutation C.986A>C (p.Y329S) in patient with hypertriglyceridemia.Semantic proximity Read ↗

Crystal structure of pathogenic Staphylococcus aureus lipase complex with the anti-obesity drug orlistat.Semantic proximity Read ↗

Mutational scanning pinpoints distinct binding sites of key ATGL regulators in lipolysisSemantic proximity Read ↗

Mutational scanning pinpoints distinct binding sites of key ATGL regulators in lipolysis.Semantic proximity Read ↗

Large‐scale functionalLIPAvariant characterization to improve birth prevalence estimates of lysosomal acid lipase deficiencySemantic proximity Read ↗

Unveiling clinically significant PPARγ mutations for thiazolidinedione treatment responsiveness through atomistic simulations.Semantic proximity Read ↗

Pathogenic mutations of the lipoprotein lipase gene in Chinese patients with hypertriglyceridemic type 2 diabetes.Semantic proximity Read ↗

Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.