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@ARTICLE{Pagani:845105,
      author       = {Pagani, Giulia and Gohlke, Holger},
      title        = {{O}n the contributing role of the transmembrane domain for
                      subunit-specific sensitivity of integrin activation},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2018-02424},
      pages        = {5733},
      year         = {2018},
      abstract     = {Integrins are α/β heterodimeric transmembrane adhesion
                      receptors. Evidence exists that their transmembrane domain
                      (TMD) separates upon activation. Subunit-specific
                      differences in activation sensitivity of integrins were
                      reported. However, whether sequence variations in the TMD
                      lead to differential TMD association has remained elusive.
                      Here, we show by molecular dynamics simulations and
                      association free energy calculations on TMDs of integrin
                      αIIbβ3, αvβ3, and α5β1 that αIIbβ3 TMD is most
                      stably associated; this difference is related to interaction
                      differences across the TMDs. The order of TMD association
                      stability is paralleled by the basal activity of these
                      integrins, which suggests that TMD differences can have a
                      decisive effect on integrin conformational free energies. We
                      also identified a specific order of clasp disintegration
                      upon TMD dissociation, which suggests that the closed state
                      of integrins may comprise several microstates. Our results
                      provide unprecedented insights into a possibly contributing
                      role of TMD towards subunit-specific sensitivity of integrin
                      activation.},
      cin          = {JSC / NIC / ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / 551 - Functional Macromolecules and Complexes
                      (POF3-551) / 553 - Physical Basis of Diseases (POF3-553) /
                      Structure, energetics, and dynamics of integrin inside-out
                      signaling $(hdd11_20131101)$},
      pid          = {G:(DE-HGF)POF3-511 / G:(DE-HGF)POF3-551 /
                      G:(DE-HGF)POF3-553 / $G:(DE-Juel1)hdd11_20131101$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29636500},
      UT           = {WOS:000429679900013},
      doi          = {10.1038/s41598-018-23778-5},
      url          = {https://juser.fz-juelich.de/record/845105},
}