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@ARTICLE{Covaceuszach:293437,
      author       = {Covaceuszach, Sonia and Konarev, Petr V. and Cassetta,
                      Alberto and Paoletti, Francesca and Svergun, Dmitri I. and
                      Lamba, Doriano and Cattaneo, Antonino},
      title        = {{T}he {C}onundrum of the {H}igh-{A}ffinity {NGF} {B}inding
                      {S}ite {F}ormation {U}nveiled?},
      journal      = {Biophysical journal},
      volume       = {108},
      number       = {3},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {PUBDB-2016-00526},
      pages        = {687 - 697},
      year         = {2015},
      note         = {(c) by the Biophysical Society},
      abstract     = {The homodimer NGF (nerve growth factor) exerts its neuronal
                      activity upon binding to either or both distinct
                      transmembrane receptors TrkA and $p75^{NTR}$. Functionally
                      relevant interactions between NGF and these receptors have
                      been proposed, on the basis of binding and signaling
                      experiments. Namely, a ternary $TrkA/NGF/p75^{NTR}$ complex
                      is assumed to be crucial for the formation of the so-called
                      high-affinity NGF binding sites. However, the existence, on
                      the cell surface, of direct extracellular interactions is
                      still a matter of controversy. Here, supported by a
                      small-angle x-ray scattering solution study of human NGF, we
                      propose that it is the oligomerization state of the secreted
                      NGF that may drive the formation of the ternary
                      heterocomplex. Our data demonstrate the occurrence in
                      solution of a concentration-dependent distribution of dimers
                      and dimer of dimers. A head-to-head molecular assembly
                      configuration of the NGF dimer of dimers has been validated.
                      Overall, these findings prompted us to suggest a new, to our
                      knowledge, model for the transient ternary heterocomplex,
                      i.e., a $TrkA/NGF/p75^{NTR}$ ligand/receptors molecular
                      assembly with a (2:4:2) stoichiometry. This model would
                      neatly solve the problem posed by the unconventional
                      orientation of $p75^{NTR}$ with respect to TrkA, as being
                      found in the crystal structures of the TrkA/NGF and
                      $p75^{NTR}/NGF$ complexes.},
      cin          = {EMBL / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101 / EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000348758600027},
      pubmed       = {pmid:25650935},
      doi          = {10.1016/j.bpj.2014.11.3485},
      url          = {https://bib-pubdb1.desy.de/record/293437},
}