MOAP1

Modulator of apoptosis 1, also known as MOAP1, is a human gene.cite web | title = Entrez Gene: MOAP1 modulator of apoptosis 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64112| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene was identified by its interaction with apoptosis regulator BAX protein. This protein contains a Bcl-2 homology 3 (BH3)-like motif, which is required for the association with BAX. When overexpressed, this gene has been shown to mediate caspase-dependent apoptosis.cite web | title = Entrez Gene: MOAP1 modulator of apoptosis 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64112| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Tan KO, Tan KM, Chan SL, "et al." |title=MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains. |journal=J. Biol. Chem. |volume=276 |issue= 4 |pages= 2802–7 |year= 2001 |pmid= 11060313 |doi= 10.1074/jbc.M008955200
*cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=
*cite journal | author=Simpson JC, Wellenreuther R, Poustka A, "et al." |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058
*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=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Wiemann S, Arlt D, Huber W, "et al." |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704
*cite journal | author=Baksh S, Tommasi S, Fenton S, "et al." |title=The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death. |journal=Mol. Cell |volume=18 |issue= 6 |pages= 637–50 |year= 2005 |pmid= 15949439 |doi= 10.1016/j.molcel.2005.05.010
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Vos MD, Dallol A, Eckfeld K, "et al." |title=The RASSF1A tumor suppressor activates Bax via MOAP-1. |journal=J. Biol. Chem. |volume=281 |issue= 8 |pages= 4557–63 |year= 2006 |pmid= 16344548 |doi= 10.1074/jbc.M512128200
*cite journal | author=Mehrle A, Rosenfelder H, Schupp I, "et al." |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139
*cite journal | author=Lim J, Hao T, Shaw C, "et al." |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032
*cite journal | author=Fu NY, Sukumaran SK, Yu VC |title=Inhibition of ubiquitin-mediated degradation of MOAP-1 by apoptotic stimuli promotes Bax function in mitochondria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 24 |pages= 10051–6 |year= 2007 |pmid= 17535899 |doi= 10.1073/pnas.0700007104

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