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@ARTICLE{Weiergrber:911654,
      author       = {Weiergräber, Oliver H. and Petrović, Dušan and Kislat,
                      Andreas and Pattky, Martin and Fabig, Judith and
                      Batra-Safferling, Renu and Schulte am Esch, Jan and Hänel,
                      Karen and Huhn, Carolin and Strodel, Birgit and Homey,
                      Bernhard and Willbold, Dieter},
      title        = {{S}tructure and {D}ynamics of {H}uman {C}hemokine
                      {CCL}16—{I}mplications for {B}iological {A}ctivity},
      journal      = {Biomolecules},
      volume       = {12},
      number       = {11},
      issn         = {2218-273X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2022-04909},
      pages        = {1588 -},
      year         = {2022},
      abstract     = {Human C-C motif ligand 16 (CCL16) is a chemokine that is
                      distinguished by a large cleavable C-terminal extension of
                      unknown significance. Conflicting data have been reported
                      concerning its tissue distribution and modulation of
                      expression, rendering the biological function of CCL16
                      enigmatic. Here, we report an integrated approach to the
                      characterisation of this chemokine, including a
                      re-assessment of its expression characteristics as well as a
                      biophysical investigation with respect to its structure and
                      dynamics. Our data indicate that CCL16 is chiefly
                      synthesised by hepatocytes, without an appreciable response
                      to mediators of inflammation, and circulates in the blood as
                      a full-length protein. While the crystal structure of CCL16
                      confirms the presence of a canonical chemokine domain,
                      molecular dynamics simulations support the view that the
                      C-terminal extension impairs the accessibility of the
                      glycosaminoglycan binding sites and may thus serve as an
                      intrinsic modulator of biological activity.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / SFB 974 A11 - Kommunikation und Systemrelevanz
                      bei Leberschädigung und Regeneration (190586431)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)190586431},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36358937},
      UT           = {WOS:000880888200001},
      doi          = {10.3390/biom12111588},
      url          = {https://juser.fz-juelich.de/record/911654},
}