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@ARTICLE{Kritsiligkou:285568,
      author       = {P. Kritsiligkou$^*$ and K. Bosch$^*$ and T.-K. Shen$^*$ and
                      M. Meurer$^*$ and M. Knop$^*$ and T. Dick$^*$},
      title        = {{P}roteome-wide tagging with an {H}2{O}2 biosensor reveals
                      highly localized and dynamic redox microenvironments.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {120},
      number       = {48},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DKFZ-2023-02434},
      pages        = {e2314043120},
      year         = {2023},
      note         = {DKFZ-ZMBH Alliance / #EA:A160#LA:A160# / 2023 Nov
                      28;120(48):e2314043120},
      abstract     = {Hydrogen peroxide (H2O2) sensing and signaling involves the
                      reversible oxidation of particular thiols on particular
                      proteins to modulate protein function in a dynamic manner.
                      H2O2 can be generated from various intracellular sources,
                      but their identities and relative contributions are often
                      unknown. To identify endogenous 'hotspots' of H2O2
                      generation on the scale of individual proteins and protein
                      complexes, we generated a yeast library in which the H2O2
                      sensor HyPer7 was fused to the C-terminus of all
                      protein-coding open reading frames (ORFs). We also generated
                      a control library in which a redox-insensitive mutant of
                      HyPer7 (SypHer7) was fused to all ORFs. Both libraries were
                      screened side-by-side to identify proteins located within
                      H2O2-generating environments. Screening under a variety of
                      different metabolic conditions revealed dynamic changes in
                      H2O2 availability highly specific to individual proteins and
                      protein complexes. These findings suggest that intracellular
                      H2O2 generation is much more localized and functionally
                      differentiated than previously recognized.},
      keywords     = {genetically encoded probes (Other) / hydrogen peroxide
                      (Other) / redox regulation (Other) / redox signaling
                      (Other)},
      cin          = {A160 / A260},
      ddc          = {500},
      cid          = {I:(DE-He78)A160-20160331 / I:(DE-He78)A260-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37991942},
      doi          = {10.1073/pnas.2314043120},
      url          = {https://inrepo02.dkfz.de/record/285568},
}