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A:

В классе SomeActivity есть метод onStop

@Override
public void onStop() {
super.onStop();
Log.v(“Hello”, “onStop”);
}

на этом методе убивается обработка завершения потока в onPause()
Для примера
protected void onPause() {
Log.v(“Hello”, “onPause”);
super.onPause();
}

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A:

В классе SomeActivity есть метод onStop

@Override
public void onStop() {
super.onStop();
Log.v(“Hello”, “onStop”);
}

на этом методе убивается обработка завершения потока в onPause()
Для примера
protected void onPause() {
Log.v(“Hello”, “onPause”);
super.onPause();
}

Some cIAP family members interact with STING, the mammalian adaptor protein in cytosolic DNA sensing.
The cellular inhibitor of apoptosis (cIAP) family proteins are critical for the caspase-8-dependent apoptosis pathway and the NF-kappaB pathway. However, cIAP family members have multiple functions in the immune responses, and the regulatory mechanisms involved in cIAP family members are not fully understood. Here we report that the v-IAP (Birc2) subfamily members inhibit cytokine- and pathogen-mediated activation of NF-kappaB. cIAP1 and cIAP2 (Birc3/Rbx1) inhibit TNF-alpha and IL-1beta responses in RAW264.7 macrophages. A gene knockdown approach shows that cIAP1 and cIAP2 are important for NF-kappaB activation induced by TNF-alpha, IL-1beta, LPS, poly(I:C), and Sendai virus. Genetic and biochemical approaches suggest that cIAP1 and cIAP2 suppress cytokine- and pathogen-mediated activation of the protein kinase TBK1 by directly binding to the adaptor molecule STING (stimulator of interferon genes). STING becomes activated by cytokine- and pathogen-triggered DNA changes in the cytosol. Our findings demonstrate that the cIAP family members regulate STING-mediated NF-kappaB signaling and suggest that the cIAP family may be involved in the innate immune responses by regulating the recruitment of TBK1 for