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

Natural mutations of apolipoprotein A-I impairing activation of lecithin:cholesterol acyltransferase.

Biochimica et biophysica acta - 20 Feb 2003

Hoang Anh, Huang Wei, Sasaki Jun, Sviridov Dmitri

Abstract excerpt

Five natural mutations of apolipoprotein A-I (apoA-I), apoA-I(A95D), apoA-I(Y100H), apoA-I(E110K), apoA-I(V156E) and apoA-I(H162Q), were studied for their ability to activate lecithin:cholesterol acyltransferase (LCAT). Mutants apoA-I(E110K), apoA-I(V156E) and apoA-I(H162Q) had an impaired ability to activate LCAT. Combined with data on other apoA-I mutants this finding is consistent with the idea that the...

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 Apolipoprotein A-I
Share to Binding Sites

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

Share to Dose-Response Relationship, Drug

Share to Enzyme Activation

Share to Mutation

Share to Phosphatidylcholine-Sterol O-Acyltransferase

Share to Point Mutation

Source

Identifiers

PMID: 12573451
DOI: 10.1016/s1388-1981(02)00357-8

Genes

LCAT

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

Natural mutations of apolipoprotein A-I impairing activation of lecithin:cholesterol acyltransferase.PMID 12573451Read ↗

A novel homozygous missense mutation in the apo A-I gene with apo A-I deficiency.Semantic proximity Read ↗

Activation of Naturally Occurring Lecithin:Cholesterol Acyltransferase Mutants by a Novel Activator Compound.Semantic proximity Read ↗

LCAT can rescue the abnormal phenotype produced by the natural ApoA-I mutations (Leu141Arg)Pisa and (Leu159Arg)FIN.Semantic proximity Read ↗

The replacement of arginine by cysteine at residue 151 in apolipoprotein A-I produces a phenotype similar to that of apolipoprotein A-IMilano.Semantic proximity Read ↗

Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT gene.Semantic proximity Read ↗

Identification of specific amphipathic alpha-helical sequence of human apolipoprotein A-IV involved in lecithin:cholesterol acyltransferase activation.Semantic proximity Read ↗

An approach to the functional analysis of lecithin-cholesterol acyltransferase. Activation by recombinant normal and mutagenized apolipoprotein AI.Semantic proximity Read ↗

Two novel molecular defects in the LCAT gene are associated with fish eye disease.Semantic proximity Read ↗

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity.Semantic proximity Read ↗

Structure-function studies of apoA-I variants: site-directed mutagenesis and natural mutations.Semantic proximity Read ↗

Point mutations in apolipoprotein A-I mimic the phenotype observed in patients with classical lecithin:cholesterol acyltransferase deficiency.Semantic proximity Read ↗

Apolipoprotein A-IFIN (Leu159-->Arg) mutation affects lecithin cholesterol acyltransferase activation and subclass distribution of HDL but not cholesterol efflux from fibroblasts.Semantic proximity Read ↗

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