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@ARTICLE{Eid:294676,
author = {M. Eid$^*$ and U. Barayeu$^*$ and K. Sulková$^*$ and C.
Aranda-Vallejo$^*$ and T. Dick$^*$},
title = {{U}sing the heme peroxidase {APEX}2 to probe intracellular
{H}2{O}2 flux and diffusion.},
journal = {Nature Communications},
volume = {15},
number = {1},
issn = {2041-1723},
address = {[London]},
publisher = {Nature Publishing Group UK},
reportid = {DKFZ-2024-02411},
pages = {1239},
year = {2024},
note = {#EA:A160#LA:A160# / DKFZ-ZMBH Alliance},
abstract = {Currently available genetically encoded H2O2 probes report
on the thiol redox state of the probe, which means that they
reflect the balance between probe thiol oxidation and
reduction. Here we introduce the use of the engineered heme
peroxidase APEX2 as a thiol-independent chemogenetic H2O2
probe that directly and irreversibly converts H2O2 molecules
into either fluorescent or luminescent signals. We
demonstrate sensitivity, specificity, and the ability to
quantitate endogenous H2O2 turnover. We show how the probe
can be used to detect changes in endogenous H2O2 generation
and to assess the roles and relative contributions of
endogenous H2O2 scavengers. Furthermore, APEX2 can be used
to study H2O2 diffusion inside the cytosol. Finally, APEX2
reveals the impact of commonly used alkylating agents and
cell lysis protocols on cellular H2O2 generation.},
keywords = {Heme / Hydrogen Peroxide / Oxidation-Reduction /
Peroxidases: chemistry / Peroxidases: metabolism /
Sulfhydryl Compounds / Heme (NLM Chemicals) / Hydrogen
Peroxide (NLM Chemicals) / Peroxidases (NLM Chemicals) /
Sulfhydryl Compounds (NLM Chemicals)},
cin = {A160},
ddc = {500},
cid = {I:(DE-He78)A160-20160331},
pnm = {311 - Zellbiologie und Tumorbiologie (POF4-311) / Redox
Relays - Detecting, understanding and exploiting
intracellular redox signaling relays (742039)},
pid = {G:(DE-HGF)POF4-311 / G:(EU-Grant)742039},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:38336829},
pmc = {pmc:PMC10858230},
doi = {10.1038/s41467-024-45511-9},
url = {https://inrepo02.dkfz.de/record/294676},
}