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- W2105342942 abstract "Oxidant stress influences many cellular processes, including cell growth, differentiation, and cell death. A well-recognized link between these processes and oxidant stress is via alterations in Ca2+ signaling. However, precisely how oxidants influence Ca2+ signaling remains unclear. Oxidant stress led to a phenotypic shift in Ca2+ mobilization from an oscillatory to a sustained elevated pattern via calcium release–activated calcium (CRAC)–mediated capacitive Ca2+ entry, and stromal interaction molecule 1 (STIM1)– and Orai1-deficient cells are resistant to oxidant stress. Functionally, oxidant-induced Ca2+ entry alters mitochondrial Ca2+ handling and bioenergetics and triggers cell death. STIM1 is S-glutathionylated at cysteine 56 in response to oxidant stress and evokes constitutive Ca2+ entry independent of intracellular Ca2+ stores. These experiments reveal that cysteine 56 is a sensor for oxidant-dependent activation of STIM1 and demonstrate a molecular link between oxidant stress and Ca2+ signaling via the CRAC channel." @default.
- W2105342942 created "2016-06-24" @default.
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- W2105342942 date "2010-08-02" @default.
- W2105342942 modified "2023-10-11" @default.
- W2105342942 title "S-glutathionylation activates STIM1 and alters mitochondrial homeostasis" @default.
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- W2105342942 doi "https://doi.org/10.1083/jcb.201004152" @default.
- W2105342942 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2922639" @default.
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- W2105342942 hasPublicationYear "2010" @default.
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