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@ARTICLE{Geiger:601616,
      author       = {Geiger, Michael and Brown, Chris and Wichers, Jan Stephan
                      and Strauss, Jan and Lill, Andrés and Thünauer, Roland and
                      Liffner, Benjamin and Wilcke, Louisa and Lemcke, Sarah and
                      Heincke, Dorothee and Pazicky, Samuel and Bachmann, Anna and
                      Loew, Christian and Wilson, Danny and Filarsky, Michael and
                      Burda, Paul-Christian and Zhang, Kun and Junop, Murray and
                      Gilberger, Tim},
      title        = {{S}tructural {I}nsights {I}nto {P}f{ARO} and
                      {C}haracterization of its {I}nteraction {W}ith {P}f{AIP}},
      journal      = {Journal of molecular biology},
      volume       = {432},
      number       = {4},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-00309},
      pages        = {878 - 896},
      year         = {2020},
      abstract     = {Apicomplexan parasites contain rhoptries, which are
                      specialized secretory organelles that coordinate host cell
                      invasion. During the process of invasion, rhoptries secrete
                      their contents to facilitate interaction with, and entry
                      into, the host cell. Here, we report the crystal structure
                      of the rhoptry protein Armadillo Repeats-Only (ARO) from the
                      human malaria parasite, Plasmodium falciparum (PfARO). The
                      structure of PfARO comprises five tandem Armadillo-like
                      (ARM) repeats, with adjacent ARM repeats stacked in a
                      head-to-tail orientation resulting in PfARO adopting an
                      elongated curved shape. Interestingly, the concave face of
                      PfARO contains two distinct patches of highly conserved
                      residues that appear to play an important role in
                      protein-protein interaction. We functionally characterized
                      the P. falciparum homolog of ARO interacting protein (PfAIP)
                      and demonstrate that it localizes to the rhoptries. We show
                      that conditional mislocalization of PfAIP leads to deficient
                      red blood cell invasion. Guided by the structure, we
                      identified mutations of PfARO that lead to mislocalization
                      of PfAIP. Using proximity-based biotinylation we probe into
                      PfAIP interacting proteins.},
      cin          = {CSSB-BNITM-TG / CSSB-EMBL-CL / CSSB-CF-ALFM / CSSB-UHH-MF},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-BNITM-TG-20210520 /
                      I:(DE-H253)CSSB-EMBL-CL-20210806 /
                      I:(DE-H253)CSSB-CF-ALFM-20210629 /
                      I:(DE-H253)CSSB-UHH-MF-20210701},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31877322},
      UT           = {WOS:000518867100008},
      doi          = {10.1016/j.jmb.2019.12.024},
      url          = {https://bib-pubdb1.desy.de/record/601616},
}