| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1949555 | Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids | 2011 | 6 Pages |
Abstract
âºS55P mutation had a modest effect on the stability of the bundle structure of apoA-I. âºS55P/Î190-243 apoA-I restored the lipid binding despite the C-terminal truncation. âºDestabilized N-terminal helix bundle promoted lipid solubilization. âºAlterations in the stability of apoA-I appear to influence the production of HDL.
Keywords
Proline substitutionGdnHClTrp8-anilino-1-naphthalenesulfonic aciddimyristoylphosphatidylcholineHDLITCdMPCABCA1ATP-binding cassette transporter A1high-density lipoproteinAmphipathic α-helixapoapolipoproteinApolipoprotein A-ILipid bindinghydrogen–deuterium exchangeTryptophancircular dichroismANSphosphatidylcholineSUVwild-typeIsothermal titration calorimetrySmall unilamellar vesicleGuanidine hydrochloride
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Authors
Masafumi Tanaka, Padmaja Dhanasekaran, David Nguyen, Margaret Nickel, Yuki Takechi, Sissel Lund-Katz, Michael C. Phillips, Hiroyuki Saito,