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@ARTICLE{Mojr:474132,
      author       = {Mojr, Viktor and Roghanian, Mohammad and Tamman, Hedvig and
                      Do Pham, Duy Dinh and Petrová, Magdalena and Pohl, Radek
                      and Takada, Hiraku and Van Nerom, Katleen and Ainelo, Hanna
                      and Caballero-Montes, Julien and Jimmy, Steffi and
                      Garcia-Pino, Abel and Hauryliuk, Vasili and Rejman, Dominik},
      title        = {{N}onhydrolysable {A}nalogues of (p)pp{G}pp and (p)pp{A}pp
                      {A}larmone {N}ucleotides as {N}ovel {M}olecular {T}ools},
      journal      = {ACS chemical biology},
      volume       = {16},
      number       = {9},
      issn         = {1554-8929},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PUBDB-2022-00522},
      pages        = {1680 - 1691},
      year         = {2021},
      note         = {Waiting for fulltext},
      abstract     = {While alarmone nucleotides
                      guanosine-3′,5′-bisdiphosphate (ppGpp) and
                      guanosine-5′-triphosphate-3′-diphosphate (pppGpp) are
                      archetypical bacterial second messengers, their adenosine
                      analogues ppApp (adenosine-3′,5′-bisdiphosphate) and
                      pppApp (adenosine-5′-triphosphate-3′-diphosphate) are
                      toxic effectors that abrogate bacterial growth. The
                      alarmones are both synthesized and degraded by the members
                      of the RelA-SpoT Homologue (RSH) enzyme family. Because of
                      the chemical and enzymatic liability of (p)ppGpp and
                      (p)ppApp, these alarmones are prone to degradation during
                      structural biology experiments. To overcome this limitation,
                      we have established an efficient and straightforward
                      procedure for synthesizing nonhydrolysable (p)ppNuNpp
                      analogues starting from 3′-azido-3′-deoxyribonucleotides
                      as key intermediates. To demonstrate the utility of
                      (p)ppGNpp as a molecular tool, we show that (i) as an HD
                      substrate mimic, ppGNpp competes with ppGpp to inhibit the
                      enzymatic activity of human MESH1 Small Alarmone Hyrolase,
                      SAH; and (ii) mimicking the allosteric effects of (p)ppGpp,
                      (p)ppGNpp acts as a positive regulator of the synthetase
                      activity of long ribosome-associated RSHs Rel and RelA.
                      Finally, by solving the structure of the N-terminal domain
                      region (NTD) of T. thermophilus Rel complexed with pppGNpp,
                      we show that as an HD substrate mimic, the analogue serves
                      as a bona fide orthosteric regulator that promotes the same
                      intra-NTD structural rearrangements as the native
                      substrate.},
      cin          = {CSSB-DESY-HS},
      ddc          = {540},
      cid          = {I:(DE-H253)CSSB-DESY-HS-20210521},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34477366},
      UT           = {WOS:000697343400008},
      doi          = {10.1021/acschembio.1c00398},
      url          = {https://bib-pubdb1.desy.de/record/474132},
}