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@ARTICLE{Bi:626512,
      author       = {Bi, Chunyang and Mirza, Salahuddin and Baburi, Helay and
                      Schäkel, Laura and Winzer, Riekje and Moschütz, Susanne
                      and Keetz, Kilian and Lopez, Vittoria and Pelletier, Julie
                      and Sévigny, Jean and Schulze zur Wiesch, Julian and Claff,
                      Tobias and Tolosa, Eva and Namasivayam, Vigneshwaran and
                      Straeter, Norbert and Müller, Christa E.},
      title        = {{S}ynthesis, {C}haracterization, {I}nteractions, and
                      {I}mmunomodulatory {F}unction of {E}ctonucleotidase
                      {CD}39/{CD}73 {I}nhibitor 8-{B}utylthioadenosine
                      5′-{M}onophosphate},
      journal      = {ACS pharmacology $\&$ translational science},
      volume       = {8},
      number       = {5},
      issn         = {2575-9108},
      address      = {Washington, DC},
      publisher    = {ACS Publications},
      reportid     = {PUBDB-2025-01465},
      pages        = {1401 - 1415},
      year         = {2025},
      note         = {waiting for fulltext},
      abstract     = {Ectonucleoside triphosphate diphosphohydrolase-1 (NTPDase1,
                      CD39) catalyzes the extracellular hydrolysis of ATP
                      generating AMP, while ecto-5′-nucleotidase (CD73) further
                      hydrolyzes AMP yielding immunosuppressive adenosine.
                      8-Butylthioadenosine 5′-monophosphate (8-BuS-AMP) was
                      described as a CD39 inhibitor but has been poorly
                      characterized. The standard CD39 antagonist ARL 67156 is not
                      suitable for in vivo studies due to metabolic instability.
                      In the present study, we optimized and upscaled the
                      synthesis of 8-BuS-AMP and performed a comprehensive
                      investigation of its properties. It behaves as a competitive
                      inhibitor at human and mouse CD39, and additionally inhibits
                      CD73. Docking studies using a homology model of human CD39
                      and determination of an atomic-resolution (1.06 Å)
                      cocrystal structure with human CD73 indicated the
                      inhibitor’s interactions within the substrate binding
                      pockets and explained the compound’s stability toward
                      hydrolysis. 8-BuS-AMP is metabolically highly stable in
                      human and mouse liver microsomes. It inhibited ε-adenosine
                      formation from ε-ATP and ε-AMP in human synovial fluid and
                      enhanced activation and proliferation of peripheral human T
                      lymphocytes. Thus, 8-BuS-AMP is a recommended tool compound
                      for studying purinergic signaling in vitro and in vivo,
                      being superior to the standard CD39 inhibitor ARL 67156.
                      Moreover, it may serve as a lead structure to develop drugs
                      for the immunotherapy of cancer.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)335447717 - SFB 1328: Adeninnukleotide in
                      Immunität und Entzündung (335447717)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)335447717},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40370983},
      UT           = {WOS:001458665100001},
      doi          = {10.1021/acsptsci.5c00126},
      url          = {https://bib-pubdb1.desy.de/record/626512},
}