% 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{Kugele:906750,
      author       = {Kugele, Anandi and Uzun, Buket and Müller, Lena and
                      Schott-Verdugo, Stephan and Gohlke, Holger and Groth, Georg
                      and Drescher, Malte},
      title        = {{M}apping the helix arrangement of the reconstituted {ETR}1
                      ethylene receptor transmembrane domain by {EPR}
                      spectroscopy},
      journal      = {RSC Advances},
      volume       = {12},
      issn         = {2046-2069},
      address      = {London},
      publisher    = {RSC Publishing},
      reportid     = {FZJ-2022-01668},
      pages        = {7352 - 7356},
      year         = {2022},
      abstract     = {The plant ethylene receptor ETR1 is a key player in the
                      perception of the phytohormone and subsequent downstream
                      ethylene signal transmission, crucial for processes such as
                      ripening, senescence and abscission. However, to date, there
                      is sparse structural knowledge about the transmembrane
                      sensor domain (TMD) of ETR1 that is responsible for the
                      binding of the plant hormone and initiates the downstream
                      signal transmission. Sequence information and ab initio
                      modelling suggest that the TMD consists of three
                      transmembrane helices. Here, we combined site-directed spin
                      labelling with electron paramagnetic resonance spectroscopy
                      and obtained distance restraints for liposome-reconstituted
                      $ETR1_TMD$ on the orientation and arrangement of the
                      transmembrane helices. We used these data to scrutinize
                      different computational structure predictions of the TMD.},
      cin          = {JSC / NIC / IBI-7 / IBG-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBG-4-20200403},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217) /
                      2172 - Utilization of renewable carbon and energy sources
                      and engineering of ecosystem functions (POF4-217) /
                      Forschergruppe Gohlke $(hkf7_20200501)$ / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
                      G:(DE-HGF)POF4-2172 / $G:(DE-Juel1)hkf7_20200501$ /
                      G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000764246300001},
      doi          = {10.1039/D2RA00604A},
      url          = {https://juser.fz-juelich.de/record/906750},
}