BCL2L10

BCL2-like 10 (apoptosis facilitator), also known as BCL2L10, is a human gene.cite web | title = Entrez Gene: BCL2L10 BCL2-like 10 (apoptosis facilitator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10017| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains conserved BH4, BH1 and BH2 domains. This protein can interact with other members of BCL-2 protein family including BCL2, BCL2L1/BCL-X(L), and BAX. Overexpression of this gene has been shown to suppress cell apoptosis possibly through the prevention of cytochrome C release from the mitochondria, and thus activating caspase-3 activation. The mouse counterpart of this protein is found to interact with Apaf1 and forms a protein complex with Caspase 9, which suggests the involvement of this protein in APAF1 and CASPASE 9 related apoptotic pathway.cite web | title = Entrez Gene: BCL2L10 BCL2-like 10 (apoptosis facilitator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10017| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=van Oirschot JT |title=Diva vaccines that reduce virus transmission. |journal=J. Biotechnol. |volume=73 |issue= 2-3 |pages= 195–205 |year= 1999 |pmid= 10486928 |doi=
*cite journal | author=Pan G, O'Rourke K, Dixit VM |title=Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5841–5 |year= 1998 |pmid= 9488720 |doi=
*cite journal | author=Inohara N, Gourley TS, Carrio R, "et al." |title=Diva, a Bcl-2 homologue that binds directly to Apaf-1 and induces BH3-independent cell death. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32479–86 |year= 1999 |pmid= 9829980 |doi=
*cite journal | author=Song Q, Kuang Y, Dixit VM, Vincenz C |title=Boo, a novel negative regulator of cell death, interacts with Apaf-1. |journal=EMBO J. |volume=18 |issue= 1 |pages= 167–78 |year= 1999 |pmid= 9878060 |doi= 10.1093/emboj/18.1.167
*cite journal | author=Ke N, Godzik A, Reed JC |title=Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12481–4 |year= 2001 |pmid= 11278245 |doi= 10.1074/jbc.C000871200
*cite journal | author=Naumann U, Weit S, Wischhusen J, Weller M |title=Diva/Boo is a negative regulator of cell death in human glioma cells. |journal=FEBS Lett. |volume=505 |issue= 1 |pages= 23–6 |year= 2001 |pmid= 11557035 |doi=
*cite journal | author=Aouacheria A, Arnaud E, Venet S, "et al." |title=Nrh, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor of apoptosis. |journal=Oncogene |volume=20 |issue= 41 |pages= 5846–55 |year= 2001 |pmid= 11593390 |doi= 10.1038/sj.onc.1204740
*cite journal | author=Zhang H, Holzgreve W, De Geyter C |title=Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks apoptosis in the mitochondria death pathway but not in the death receptor pathway. |journal=Hum. Mol. Genet. |volume=10 |issue= 21 |pages= 2329–39 |year= 2002 |pmid= 11689480 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Li Z, Takeuchi S, Ohara N, Maruo T |title=Paradoxically abundant expression of Bcl-2 and adrenomedullin in invasive cervical squamous carcinoma. |journal=Int. J. Clin. Oncol. |volume=8 |issue= 2 |pages= 83–9 |year= 2003 |pmid= 12720100 |doi= 10.1007/s101470300015
*cite journal | author=Kang Y, Lee DC, Han J, "et al." |title=NM23-H2 involves in negative regulation of Diva and Bcl2L10 in apoptosis signaling. |journal=Biochem. Biophys. Res. Commun. |volume=359 |issue= 1 |pages= 76–82 |year= 2007 |pmid= 17532299 |doi= 10.1016/j.bbrc.2007.05.090

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