ArticleBiochemistry2013
The conformation of lipid-free human apolipoprotein A-I in solution.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- The Structural and Functional Journey of Apolipoprotein A-I Through the Human Body.Current atherosclerosis reports · 2026Review
- Foam fractionation studies of recombinant human apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2024Article
- The role of C-terminal ionic residues in self-association of apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2023Article
- The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta.The Journal of biological chemistry · 2022Article
- First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation.PloS one · 2020Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Interleukin-17 Drives Interstitial Entrapment of Tissue Lipoproteins in Experimental Psoriasis.Cell metabolism · 2019Article
- Charged Residues in the C-Terminal Domain of Apolipoprotein A-I Modulate Oligomerization.Biochemistry · 2018Article
- Decreased pretherapy serum apolipoprotein A-I is associated with extent of metastasis and poor prognosis of non-small-cell lung cancer.OncoTargets and therapy · 2018Article
- A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state.Nature structural & molecular biology · 2017Article
- Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity.Biochimica et biophysica acta. Biomembranes · 2017Article
- High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation.Biochemistry · 2016Article
- Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.Journal of lipid research · 2016Article
- An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding.The Journal of biological chemistry · 2016Article
- Microdomains, Inflammation, and Atherosclerosis.Circulation research · 2016Review
- Spectroscopic Characterization of Structural Changes in Membrane Scaffold Proteins Entrapped within Mesoporous Silica Gel Monoliths.ACS applied materials & interfaces · 2015Article
- Structural Insights into High Density Lipoprotein: Old Models and New Facts.Frontiers in pharmacology · 2015Review
- An experimentally robust model of monomeric apolipoprotein A-I created from a chimera of two X-ray structures and molecular dynamics simulations.Biochemistry · 2014Article
- Binding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia.Journal of lipid research · 2014Article
- Analysis of lipid phase behavior and protein conformational changes in nanolipoprotein particles upon entrapment in sol-gel-derived silica.Langmuir : the ACS journal of surfaces and colloids · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Apolipoprotein AI (apoA-I) is the principal acceptor of lipids from ATP-binding cassette transporter A1, a process that yields nascent high density lipoproteins. Analysis of lipidated apoA-I conformation yields a belt or twisted belt in which two strands of apoA-I lie antiparallel to one another. In contrast, biophysical studies have suggested that a part of lipid-free apoA-I was arranged in a four-helix bundle. To understand how lipid-free apoA-I opens from a bundle to a belt while accepting lipid it was necessary to have a more refined model for the conformation of lipid-free apoA-I. This study reports the conformation of lipid-free human apoA-I using lysine-to-lysine chemical cross-linking in conjunction with disulfide cross-linking achieved using selective cysteine mutations. After proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is compact with roughly four helical regions, amino acids 44-186, bundled together. C- and N-terminal ends, amino acids 1-43 and 187-243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example, lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
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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.