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| Home > Publications database > The low resolution structure of ApoA1 in spherical high density lipoprotein revealed by small angle neutron scattering > print |
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| 024 | 7 | _ | |2 pmc |a pmc:PMC3069452 |
| 024 | 7 | _ | |2 DOI |a 10.1074/jbc.M110.209130 |
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| 041 | _ | _ | |a eng |
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| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Wu, Z. |b 0 |
| 245 | _ | _ | |a The low resolution structure of ApoA1 in spherical high density lipoprotein revealed by small angle neutron scattering |
| 260 | _ | _ | |a Bethesda, Md. |b Soc. |c 2011 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 3091 |a Journal of Biological Chemistry |v 286 |x 0021-9258 |y 12495 - 12508 |
| 500 | _ | _ | |a This work was supported, in whole or in part, by National Institutes of Health Grants P01 HL098055, P01 HL076491-055328, and P01 HL087018-02001. This work was also supported in part by a grant from the Foundation Leducq. |
| 520 | _ | _ | |a Spherical high density lipoprotein (sHDL), a key player in reverse cholesterol transport and the most abundant form of HDL, is associated with cardiovascular diseases. Small angle neutron scattering with contrast variation was used to determine the solution structure of protein and lipid components of reconstituted sHDL. Apolipoprotein A1, the major protein of sHDL, forms a hollow structure that cradles a central compact lipid core. Three apoA1 chains are arranged within the low resolution structure of the protein component as one of three possible global architectures: (i) a helical dimer with a hairpin (HdHp), (ii) three hairpins (3Hp), or (iii) an integrated trimer (iT) in which the three apoA1 monomers mutually associate over a portion of the sHDL surface. Cross-linking and mass spectrometry analyses help to discriminate among the three molecular models and are most consistent with the HdHp overall architecture of apoA1 within sHDL. |
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| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Apolipoprotein A-I: chemistry |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Lipoproteins, HDL: chemistry |
| 650 | _ | 2 | |2 MeSH |a Mass Spectrometry |
| 650 | _ | 2 | |2 MeSH |a Neutrons |
| 650 | _ | 2 | |2 MeSH |a Protein Multimerization |
| 650 | _ | 2 | |2 MeSH |a Scattering, Small Angle |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Apolipoprotein A-I |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Lipoproteins, HDL |
| 650 | _ | 7 | |2 WoSType |a J |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Gogonea, V. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Lee, X. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a May, R.P. |b 3 |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Wagner, M.A. |b 5 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Undurti, A. |b 6 |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a DiDonato, J.A. |b 11 |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Hazen, S.L. |b 13 |
| 773 | _ | _ | |0 PERI:(DE-600)1474604-9 |a 10.1074/jbc.M110.209130 |g Vol. 286 |q 286 |t The @journal of biological chemistry |v 286 |x 0021-9258 |y 2011 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3069452 |
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