Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain (DD)-containing adapter molecules and members of the ICE/CED-3 protease family. Caspases-8 (FLICE) and -10 (FLICE2) are two pivotal members in the ICE/CED-3 protease family. FLICE-inhibitory proteins were identified in virus and human and designated v-FLIPs and c-FLIPs, respectively1,2. The human FLIPs were also cloned by several labs independently and termed Casper , I-FLICE, FLAME-1, CASH, CLARP and usurpin3-7. FLIP contains two death effector domains (DEDs) and a caspase-like domain. FLIP interacts with adapter protein FADD and caspase-8 and 10, and potently inhibits apoptosis induced by all known death receptors CD95, DR3, TRAIL-R and TNFR1. Four splice variants of c-FLIPs have been identified and termed FLIPalpha, beta, gamma, and delta, respectively (8).
Related Pathway
Apoptosis
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Western blot analysis of FLIP in total cell lysates from HeLa (H), Jurkat (J), THP-1 (T), A431 (A), K562 (K) and NIH3T3 (N) cells with FLIP antibody at 1:1000 dilution.
