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@ARTICLE{Brown:909359,
      author       = {Brown, Hawley and Chung, Mia and Üffing, Alina and
                      Batistatou, Nefeli and Tsang, Tiffany and Doskocil, Samantha
                      and Mao, Weiqun and Willbold, Dieter and Bast, Robert C. and
                      Lu, Zhen and Weiergräber, Oliver H. and Kritzer, Joshua A.},
      title        = {{S}tructure-{B}ased {D}esign of {S}tapled {P}eptides {T}hat
                      {B}ind {GABARAP} and {I}nhibit {A}utophagy},
      journal      = {Journal of the American Chemical Society},
      volume       = {144},
      number       = {32},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2022-03149},
      pages        = {14687 - 14697},
      year         = {2022},
      abstract     = {The LC3/GABARAP family of proteins are involved in nearly
                      every stage of autophagy. Inhibition of LC3/GABARAP proteins
                      is a promising approach to blocking autophagy, which
                      sensitizes advanced cancers to DNA-damaging chemotherapy.
                      Here, we report the structure-based design of stapled
                      peptides that inhibit GABARAP with nanomolar affinities.
                      Small changes in staple structure produced stapled peptides
                      with very different binding modes and functional differences
                      in LC3/GABARAP paralog selectivity, ranging from highly
                      GABARAP-specific to broad inhibition of both subfamilies.
                      The stapled peptides exhibited considerable cytosolic
                      penetration and resistance to biological degradation. They
                      also reduced autophagic flux in cultured ovarian cancer
                      cells and sensitized ovarian cancer cells to cisplatin.
                      These small, potent stapled peptides represent promising
                      autophagy-modulating compounds that can be developed as
                      novel cancer therapeutics and novel mediators of targeted
                      protein degradation.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / SFB 1208 B02 - Spezifische Rollen von Atg8s im
                      Vesikeltransport (B02) (289554527)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)289554527},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35917476},
      UT           = {WOS:000836234100001},
      doi          = {10.1021/jacs.2c04699},
      url          = {https://juser.fz-juelich.de/record/909359},
}