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

Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity.

Proceedings of the National Academy of Sciences of the United States of America - 1 May 1990

Beg O U, Meng M S, Skarlatos S I, Previato L, Brunzell J D, Brewer H B, Fojo S S

Abstract excerpt

The molecular defect that leads to a deficiency of lipoprotein lipase (LPL) activity in the proband from a Bethesda kindred has been identified. The pre- and post-heparin plasma LPL mass in the proband was elevated when compared to controls; however, there was no detectable LPL activity, indicating the presence of a defective enzyme (termed LPLBethesda). Analysis of the patient's post-heparin plasma by...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Share to Polymerase Chain Reaction

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 2110364
DOI: 10.1073/pnas.87.9.3474
PMCID: PMC53923

Genes

LPL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity.PMID 2110364Read ↗

The molecular defects in lipoprotein lipase deficient patients.Semantic proximity Read ↗

Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome.Semantic proximity Read ↗

Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase.Semantic proximity Read ↗

Missense mutation (Gly----Glu188) of human lipoprotein lipase imparting functional deficiency.Semantic proximity Read ↗

Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene.Semantic proximity Read ↗

Identification and characterization of two novel mutations in the LPL gene causing type I hyperlipoproteinemia.Semantic proximity Read ↗

A compound heterozygote for hepatic lipase gene mutations Leu334-->Phe and Thr383-->Met: correlation between hepatic lipase activity and phenotypic expression.Semantic proximity Read ↗

A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia).Semantic proximity Read ↗

Molecular studies on primary lipoprotein lipase (LPL) deficiency. One base deletion (G916) in exon 5 of LPL gene causes no detectable LPL protein due to the absence of LPL mRNA transcript.Semantic proximity Read ↗

A missense mutation Pro157 Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity.Semantic proximity Read ↗

Lipoprotein lipase: recent contributions from molecular biology.Semantic proximity Read ↗

What is the phenotype of heterozygous lipoprotein lipase deficiency?Semantic proximity Read ↗

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