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@ARTICLE{Xiong:289139,
      author       = {Y. Xiong and H. Greschik and C. Johansson and L. Seifert
                      and V. Gamble and K.-S. Park and V. Fagan and F. Li and I.
                      Chau and M. Vedadi and C. H. Arrowsmith and P. Brennan and
                      O. Fedorov and M. Jung$^*$ and G. Farnie and J. Liu and U.
                      Oppermann and R. Schüle and J. Jin},
      title        = {{D}iscovery of a {P}otent, {S}elective, and {C}ell-{A}ctive
                      {SPIN}1 {I}nhibitor.},
      journal      = {Journal of medicinal chemistry},
      volume       = {67},
      number       = {7},
      issn         = {0095-9065},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {DKFZ-2024-00606},
      pages        = {5837-5853},
      year         = {2024},
      note         = {2024 Apr 11;67(7):5837-5853},
      abstract     = {The methyl-lysine reader protein SPIN1 plays important
                      roles in various human diseases. However, targeting
                      methyl-lysine reader proteins has been challenging. Very few
                      cellularly active SPIN1 inhibitors have been developed. We
                      previously reported that our G9a/GLP inhibitor UNC0638
                      weakly inhibited SPIN1. Here, we present our comprehensive
                      structure-activity relationship study that led to the
                      discovery of compound 11, a dual SPIN1 and G9a/GLP
                      inhibitor, and compound 18 (MS8535), a SPIN1 selective
                      inhibitor. We solved the cocrystal structure of SPIN1 in
                      complex with 11, confirming that 11 occupied one of the
                      three Tudor domains. Importantly, 18 displayed high
                      selectivity for SPIN1 over 38 epigenetic targets, including
                      G9a/GLP, and concentration dependently disrupted the
                      interactions of SPIN1 and H3 in cells. Furthermore, 18 was
                      bioavailable in mice. We also developed 19 (MS8535N), which
                      was inactive against SPIN1, as a negative control of 18.
                      Collectively, these compounds are useful chemical tools to
                      study biological functions of SPIN1.},
      cin          = {FR01},
      ddc          = {610},
      cid          = {I:(DE-He78)FR01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38533580},
      doi          = {10.1021/acs.jmedchem.4c00121},
      url          = {https://inrepo02.dkfz.de/record/289139},
}