ArticleJournal of lipid research2016
Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.
Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Flipped C-Terminal Ends of APOA1 Promote ABCA1-Dependent Cholesterol Efflux by Small HDLs.Circulation · 2024Article
- Flipped C-Terminal Ends of APOA1 Promote ABCA1-dependent Cholesterol Efflux by Small HDLs.medRxiv : the preprint server for health sciences · 2023Article
- A Study on Multiple Facets of Apolipoprotein A1 Milano.Applied biochemistry and biotechnology · 2023Review
- The role of C-terminal ionic residues in self-association of apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2023Article
- Conformational flexibility of apolipoprotein A-I amino- and carboxy-termini is necessary for lipid binding but not cholesterol efflux.Journal of lipid research · 2022Article
- First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation.PloS one · 2020Article
- GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- N-terminal mutation of apoA-I and interaction with ABCA1 reveal mechanisms of nascent HDL biogenesis.Journal of lipid research · 2019Article
- Molecular Insights into Human Hereditary Apolipoprotein A-I Amyloidosis Caused by the Glu34Lys Mutation.Biochemistry · 2018Article
- Is ABCA1 a lipid transfer protein?Journal of lipid research · 2018Review
- Charged Residues in the C-Terminal Domain of Apolipoprotein A-I Modulate Oligomerization.Biochemistry · 2018Article
- A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state.Nature structural & molecular biology · 2017Article
Corrections and comments
- Erratum issuedERRATUM.2016
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
apoA-I plays important structural and functional roles in reverse cholesterol transport. We have described the molecular structure of the N-terminal domain, Δ(185-243) by X-ray crystallography. To understand the role of the C-terminal domain, constructs with sequential elongation of Δ(185-243), by increments of 11-residue sequence repeats were studied and compared with Δ(185-243) and WT apoA-I. Constructs up to residue 230 showed progressively decreased percent α-helix with similar numbers of helical residues, similar detergent and lipid binding affinity, and exposed hydrophobic surface. These observations suggest that the C-terminal domain is unstructured with the exception of the last 11-residue repeat (H10B). Similar monomer-dimer equilibrium suggests that the H10B region is responsible for nonspecific aggregation. Cholesterol efflux progressively increased with elongation up to ∼60% of full-length apoA-I in the absence of the H10B. In summary, the sequential repeats in the C-terminal domain are probably unstructured with the exception of H10B. This segment appears to be responsible for initiation of lipid binding and aggregation, as well as cholesterol efflux, and thus plays a vital role during HDL formation. Based on these observations and the Δ(185-243) crystal structure, we propose a lipid-free apoA-I structural model in solution and update the mechanism of HDL biogenesis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.