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

Structural and functional properties of the 154-171 wild-type and variant peptides of human lecithin-cholesterol acyltransferase.

European journal of biochemistry - 1 Nov 1997

Peelman F, Goethals M, Vanloo B, Labeur C, Brasseur R, Vandekerckhove J, Rosseneu M

Abstract excerpt

The 154-171 segment of the human lecithin-cholesterol acyltransferase (LCAT) enzyme was identified as the most stable amphipathic helix in the LCAT sequence. Its mean hydrophobicity, hydrophobic moment and its orientation at a lipid/water interface are similar to those of some of the helical repeats of apolipoprotein A-IV and E. This domain was therefore proposed as a candidate peptide accounting for 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 Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Microscopy, Electron

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Peptide Fragments

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 9395317
DOI: 10.1111/j.1432-1033.1997.t01-2-00708.x

Genes

LCAT

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

Structural and functional properties of the 154-171 wild-type and variant peptides of human lecithin-cholesterol acyltransferase.PMID 9395317Read ↗

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

Lipid-interacting properties of the N-terminal domain of human apolipoprotein C-III.Semantic proximity Read ↗

Mechanistic insights into the activation of lecithin-cholesterol acyltransferase in therapeutic nanodiscs composed of apolipoprotein A-I mimetic peptides and phospholipidsSemantic proximity Read ↗

Role of the lid hydrophobicity pattern in pancreatic lipase activity.Semantic proximity Read ↗

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

Structure and stability of apolipoprotein a-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation.Semantic proximity Read ↗

Conserved Amphipathic Helices Mediate Lipid Droplet Targeting of Perilipins 1-3.Semantic proximity Read ↗

An amphipathic helical region of the N-terminal barrel of phospholipid transfer protein is critical for ABCA1-dependent cholesterol efflux.Semantic proximity Read ↗

The beta 5' loop of the pancreatic lipase C2-like domain plays a critical role in the lipase-lipid interactions.Semantic proximity Read ↗

Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles.Semantic proximity Read ↗

Engineering a compact non-native state of intestinal fatty acid-binding protein.Semantic proximity Read ↗

Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease.Semantic proximity Read ↗

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