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@ARTICLE{Wu:18200,
      author       = {Wu, Z. and Gogonea, V. and Lee, X. and May, R.P. and
                      Pipich, V. and Wagner, M.A. and Undurti, A. and Tallant,
                      T.C. and Baleanu-Gogonea, C. and Charlton, F. and Ioffe, A.
                      and DiDonato, J.A. and Rye, K--A. and Hazen, S.L.},
      title        = {{T}he low resolution structure of {A}po{A}1 in spherical
                      high density lipoprotein revealed by small angle neutron
                      scattering},
      journal      = {The journal of biological chemistry},
      volume       = {286},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-18200},
      year         = {2011},
      note         = {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.},
      abstract     = {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.},
      keywords     = {Apolipoprotein A-I: chemistry / Humans / Lipoproteins, HDL:
                      chemistry / Mass Spectrometry / Neutrons / Protein
                      Multimerization / Scattering, Small Angle / Apolipoprotein
                      A-I (NLM Chemicals) / Lipoproteins, HDL (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
                      Science JCNS (München) ; JCNS-FRM-II / JCNS-1 / JCNS-2 /
                      Jülich Centre for Neutron Science JCNS (JCNS) ; JCNS /
                      PGI-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106 /
                      I:(DE-Juel1)JCNS-20121112 / I:(DE-Juel1)PGI-4-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Großgeräte für die Forschung
                      mit Photonen, Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21292766},
      pmc          = {pmc:PMC3069452},
      UT           = {WOS:000289077500063},
      doi          = {10.1074/jbc.M110.209130},
      url          = {https://juser.fz-juelich.de/record/18200},
}