ArticleThe Journal of biological chemistry2011
Structure of apolipoprotein A-I N terminus on nascent high density lipoproteins.
Article in The Journal of biological chemistry, 2011. 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.
- Molecular Simulation of the Binding of Amyloid Beta to Apolipoprotein A-I in High-Density Lipoproteins.International journal of molecular sciences · 2025Article
- An atomistic characterization of high-density lipoproteins and the conserved "LN" region of apoA-I.Biophysical journal · 2024Article
- Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Tertiary structure of apolipoprotein A-I in nascent high-density lipoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Synchrotron radiation circular dichroism spectroscopy reveals structural divergences in HDL-bound apoA-I variants.Scientific reports · 2017Article
- 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
- A novel truncated form of apolipoprotein A-I transported by dense LDL is increased in diabetic patients.Journal of lipid research · 2015Article
- Small-angle X-ray scattering of the cholesterol incorporation into human ApoA1-POPC discoidal particles.Biophysical journal · 2015Article
- Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development.Archives of medical research · 2015Review
- Conservation of apolipoprotein A-I's central domain structural elements upon lipid association on different high-density lipoprotein subclasses.Biochemistry · 2013Article
- The secondary structure of apolipoprotein A-I on 9.6-nm reconstituted high-density lipoprotein determined by EPR spectroscopy.The FEBS journal · 2013Article
- Discoidal HDL and apoA-I-derived peptides improve glucose uptake in skeletal muscle.Journal of lipid research · 2013Article
- Crystal structure of Δ(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt buckle, double hairpin and trefoil/tetrafoil.Journal of molecular biology · 2013Article
- Article
- Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Role of apolipoprotein A-II in the structure and remodeling of human high-density lipoprotein (HDL): protein conformational ensemble on HDL.Biochemistry · 2012Article
- The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.Biochemistry · 2012Review
- The low resolution structure of ApoA1 in spherical high density lipoprotein revealed by small angle neutron scattering.The Journal of biological chemistry · 2011Article
- EPR assessment of protein sites for incorporation of Gd(III) MRI contrast labels.Contrast media & molecular imagingArticle
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Authors and funding
6 authors.
Funding
Abstract
Apolipoprotein A-I (apoA-I) is the major protein component of high density lipoproteins (HDL) and a critical element of cholesterol metabolism. To better elucidate the role of the apoA-I structure-function in cholesterol metabolism, the conformation of the apoA-I N terminus (residues 6-98) on nascent HDL was examined by electron paramagnetic resonance (EPR) spectroscopic analysis. A series of 93 apoA-I variants bearing single nitroxide spin label at positions 6-98 was reconstituted onto 9.6-nm HDL particles (rHDL). These particles were subjected to EPR spectral analysis, measuring regional flexibility and side chain solvent accessibility. Secondary structure was elucidated from side-chain mobility and molecular accessibility, wherein two major α-helical domains were localized to residues 6-34 and 50-98. We identified an unstructured segment (residues 35-39) and a β-strand (residues 40-49) between the two helices. Residues 14, 19, 34, 37, 41, and 58 were examined by EPR on 7.8, 8.4, and 9.6 nm rHDL to assess the effect of particle size on the N-terminal structure. Residues 14, 19, and 58 showed no significant rHDL size-dependent spectral or accessibility differences, whereas residues 34, 37, and 41 displayed moderate spectral changes along with substantial rHDL size-dependent differences in molecular accessibility. We have elucidated the secondary structure of the N-terminal domain of apoA-I on 9.6 nm rHDL (residues 6-98) and identified residues in this region that are affected by particle size. We conclude that the inter-helical segment (residues 35-49) plays a role in the adaptation of apoA-I to the particle size of HDL.
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