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@ARTICLE{Gogonea:187412,
      author       = {Gogonea, V. and Gerstenecker, G. S. and Gerstenecker, G. S.
                      and Wu, Z. and Lee, X. and Topbas, C. and Wagner, M. A. and
                      Tallant, T. C. and Smith, J. D. and Callow, P. and Pipich,
                      V. and Malet, H. and Schoehn, G. and DiDonato, J. A. and
                      Hazen, S. L.},
      title        = {{T}he low-resolution structure of n{HDL} reconstituted with
                      {DMPC} with and without cholesterol reveals a mechanism for
                      particle expansion},
      journal      = {Journal of lipid research},
      volume       = {54},
      number       = {4},
      issn         = {0022-2275},
      address      = {Bethesda, Md.},
      publisher    = {ASBMB},
      reportid     = {PreJuSER-187412},
      pages        = {966 - 983},
      year         = {2013},
      note         = {Record converted 2014-10-14 05:10:08},
      abstract     = {Small-angle neutron scattering (SANS) with contrast
                      variation was used to obtain the low-resolution structure of
                      nascent HDL (nHDL) reconstituted with dimyristoyl
                      phosphatidylcholine (DMPC) in the absence and presence of
                      cholesterol, [apoA1:DMPC (1:80, mol:mol) and
                      apoA1:DMPC:cholesterol (1:86:9, mol:mol:mol)]. The overall
                      shape of both particles is discoidal with the low-resolution
                      structure of apoA1 visualized as an open, contorted, and out
                      of plane conformation with three arms in nascent
                      HDL/dimyristoyl phosphatidylcholine without cholesterol
                      (nHDL(DMPC)) and two arms in nascent HDL/dimyristoyl
                      phosphatidylcholine with cholesterol (nHDL(DMPC+Chol)). The
                      low-resolution shape of the lipid phase in both nHDL(DMPC)
                      and nHDL(DMPC+Chol) were oblate ellipsoids, and fit well
                      within their respective protein shapes. Modeling studies
                      indicate that apoA1 is folded onto itself in nHDL(DMPC),
                      making a large hairpin, which was also confirmed
                      independently by both cross-linking mass spectrometry and
                      hydrogen-deuterium exchange (HDX) mass spectrometry
                      analyses. In nHDL(DMPC+Chol), the lipid was expanded and no
                      hairpin was visible. Importantly, despite the overall
                      discoidal shape of the whole particle in both nHDL(DMPC) and
                      nHDL(DMPC+Chol), an open conformation (i.e., not a closed
                      belt) of apoA1 is observed. Collectively, these data show
                      that full length apoA1 retains an open architecture that is
                      dictated by its lipid cargo. The lipid is likely
                      predominantly organized as a bilayer with a micelle domain
                      between the open apoA1 arms. The apoA1 configuration
                      observed suggests a mechanism for accommodating changing
                      lipid cargo by quantized expansion of hairpin structures.},
      keywords     = {Apolipoprotein A-I: chemistry / Cholesterol: chemistry /
                      Dimyristoylphosphatidylcholine: chemistry / High-Density
                      Lipoproteins, Pre-beta: chemistry / Humans / Mass
                      Spectrometry / Scattering, Small Angle / Apolipoprotein A-I
                      (NLM Chemicals) / High-Density Lipoproteins, Pre-beta (NLM
                      Chemicals) / Cholesterol (NLM Chemicals) /
                      Dimyristoylphosphatidylcholine (NLM Chemicals)},
      cin          = {KWS1},
      ddc          = {540},
      cid          = {I:(DE-MLZ)4128},
      pnm          = {54G - JCNS (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-54G24},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23349207},
      pmc          = {pmc:PMC3606002},
      UT           = {WOS:000316462600011},
      doi          = {10.1194/jlr.M032763},
      url          = {https://juser.fz-juelich.de/record/187412},
}