% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Bogdanow:601641,
      author       = {Bogdanow, Boris and Gruska, Iris and Mühlberg, Lars and
                      Protze, Jonas and Hohensee, Svea and Vetter, Barbara and
                      Bosse, Jens B. and Lehmann, Martin and Sadeghi, Mohsen and
                      Wiebusch, Lüder and Liu, Fan},
      title        = {{S}patially resolved protein map of intact human
                      cytomegalovirus virions},
      journal      = {Nature microbiology},
      volume       = {8},
      number       = {9},
      issn         = {2058-5276},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {PUBDB-2024-00334},
      pages        = {1732 - 1747},
      year         = {2023},
      abstract     = {Herpesviruses assemble large enveloped particles that are
                      difficult to characterize structurally due to their size,
                      fragility and complex multilayered proteome with partially
                      amorphous nature. Here we used crosslinking mass
                      spectrometry and quantitative proteomics to derive a
                      spatially resolved interactome map of intact human
                      cytomegalovirus virions. This enabled the de novo allocation
                      of 32 viral proteins into four spatially resolved virion
                      layers, each organized by a dominant viral scaffold protein.
                      The viral protein UL32 engages with all layers in an
                      N-to-C-terminal radial orientation, bridging nucleocapsid to
                      viral envelope. We observed the layer-specific incorporation
                      of 82 host proteins, of which 39 are selectively recruited.
                      We uncovered how UL32, by recruitment of PP-1 phosphatase,
                      antagonizes binding to 14-3-3 proteins. This mechanism
                      assures effective viral biogenesis, suggesting a perturbing
                      role of UL32-14-3-3 interaction. Finally, we integrated
                      these data into a coarse-grained model to provide global
                      insights into the native configuration of virus and host
                      protein interactions inside herpesvirions.},
      cin          = {CSSB-MHH-JB},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-MHH-JB-20210520},
      pnm          = {899 - ohne Topic (POF4-899) / DFG project 390874280 - EXC
                      2155: RESIST - Resolving Infection Susceptibility
                      (390874280) / SFB 958 A04 - Raumzeitliches Modell neuronaler
                      Signaltransduktion und ihrer Regulation durch
                      Präsynaptische Membrangerüste (A04) (202189827) / SFB 1114
                      C03/Erg. - Anomale Michaelis-Menten-Kinetik in
                      dichtgepackter, heterogener Umgebung (C03/Erg.) (355497160)},
      pid          = {G:(DE-HGF)POF4-899 / G:(GEPRIS)390874280 /
                      G:(GEPRIS)202189827 / G:(GEPRIS)355497160},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37550507},
      UT           = {WOS:001043678400003},
      doi          = {10.1038/s41564-023-01433-8},
      url          = {https://bib-pubdb1.desy.de/record/601641},
}