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@ARTICLE{Prazak:613733,
      author       = {Prazak, Vojtech and Mironova, Yuliia and Vasishtan, Daven
                      and Hagen, Christoph and Laugks, Ulrike and Jensen, Yannick
                      and Sanders, Saskia and Heumann, John M. and Bosse, Jens
                      Bernhard and Klupp, Barbara G. and Mettenleiter, Thomas C.
                      and Grange, Michael and Gruenewald, Kay},
      title        = {{M}olecular plasticity of herpesvirus nuclear egress
                      analysed in situ},
      journal      = {Nature microbiology},
      volume       = {9},
      number       = {7},
      issn         = {2058-5276},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {PUBDB-2024-05621},
      pages        = {1842-1855},
      year         = {2024},
      note         = {Waiting for fulltext},
      abstract     = {The viral nuclear egress complex (NEC) allows herpesvirus
                      capsids to escape from the nucleus without compromising the
                      nuclear envelope integrity. The NEC lattice assembles on the
                      inner nuclear membrane and mediates the budding of nascent
                      nucleocapsids into the perinuclear space and their
                      subsequent release into the cytosol. Its essential role
                      makes it a potent antiviral target, necessitating structural
                      information in the context of a cellular infection. Here we
                      determined structures of NEC–capsid interfaces in situ
                      using electron cryo-tomography, showing a substantial
                      structural heterogeneity. In addition, while the capsid is
                      associated with budding initiation, it is not required for
                      curvature formation. By determining the NEC structure in
                      several conformations, we show that curvature arises from an
                      asymmetric assembly of disordered and hexagonally ordered
                      lattice domains independent of pUL25 or other viral capsid
                      vertex components. Our results advance our understanding of
                      the mechanism of nuclear egress in the context of a living
                      cell.},
      cin          = {CSSB-LIV-KG / CSSB-MHH-JB / CSSB-CF-CRYO},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-LIV-KG-20220525 /
                      I:(DE-H253)CSSB-MHH-JB-20210520 /
                      I:(DE-H253)CSSB-CF-CRYO-20210520},
      pnm          = {899 - ohne Topic (POF4-899) / DFG project
                      G:(GEPRIS)390874280 - EXC 2155: RESIST - Resolving Infection
                      Susceptibility (390874280) / GRK 2771 - GRK 2771: Mensch und
                      Mikrobe: Reorganisation von Zellkompartimenten und
                      Molekülkomplexen während der Infektion (453548970)},
      pid          = {G:(DE-HGF)POF4-899 / G:(GEPRIS)390874280 /
                      G:(GEPRIS)453548970},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38918469},
      UT           = {WOS:001254317500003},
      doi          = {10.1038/s41564-024-01716-8},
      url          = {https://bib-pubdb1.desy.de/record/613733},
}