ADAR

ADAR

Adenosine deaminase, RNA-specific, also known as ADAR, is a human gene.cite web | title = Entrez Gene: ADAR Adenosine Deaminase Acting on RNA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=103| accessdate = ]

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summary_text = This gene encodes the enzyme responsible for RNA editing by site-specific deamination of adenosines. This enzyme destabilizes double stranded RNA through conversion of adenosine to inosine. Mutations in this gene have been associated with dyschromatosis symmetrica hereditaria. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.cite web | title = Entrez Gene: ADAR adenosine deaminase, RNA-specific| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=103| accessdate = ]

References

Further reading

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citations =
*cite journal | author=Valenzuela A, Blanco J, Callebaut C, "et al." |title=HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26. |journal=Adv. Exp. Med. Biol. |volume=421 |issue= |pages= 185–92 |year= 1997 |pmid= 9330696 |doi=
*cite journal | author=Wathelet MG, Szpirer J, Nols CB, "et al." |title=Cloning and chromosomal location of human genes inducible by type I interferon. |journal=Somat. Cell Mol. Genet. |volume=14 |issue= 5 |pages= 415–26 |year= 1988 |pmid= 3175763 |doi=
*cite journal | author=Wang Y, Zeng Y, Murray JM, Nishikura K |title=Genomic organization and chromosomal location of the human dsRNA adenosine deaminase gene: the enzyme for glutamate-activated ion channel RNA editing. |journal=J. Mol. Biol. |volume=254 |issue= 2 |pages= 184–95 |year= 1996 |pmid= 7490742 |doi= 10.1006/jmbi.1995.0610
*cite journal | author=Patterson JB, Samuel CE |title=Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase. |journal=Mol. Cell. Biol. |volume=15 |issue= 10 |pages= 5376–88 |year= 1995 |pmid= 7565688 |doi=
*cite journal | author=Patterson JB, Thomis DC, Hans SL, Samuel CE |title=Mechanism of interferon action: double-stranded RNA-specific adenosine deaminase from human cells is inducible by alpha and gamma interferons. |journal=Virology |volume=210 |issue= 2 |pages= 508–11 |year= 1995 |pmid= 7618288 |doi= 10.1006/viro.1995.1370
*cite journal | author=O'Connell MA, Krause S, Higuchi M, "et al." |title=Cloning of cDNAs encoding mammalian double-stranded RNA-specific adenosine deaminase. |journal=Mol. Cell. Biol. |volume=15 |issue= 3 |pages= 1389–97 |year= 1995 |pmid= 7862132 |doi=
*cite journal | author=Kim U, Wang Y, Sanford T, "et al." |title=Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 24 |pages= 11457–61 |year= 1994 |pmid= 7972084 |doi=
*cite journal | author=Weier HU, George CX, Greulich KM, Samuel CE |title=The interferon-inducible, double-stranded RNA-specific adenosine deaminase gene (DSRAD) maps to human chromosome 1q21.1-21.2. |journal=Genomics |volume=30 |issue= 2 |pages= 372–5 |year= 1996 |pmid= 8586444 |doi= 10.1006/geno.1995.0034
*cite journal | author=Liu Y, George CX, Patterson JB, Samuel CE |title=Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4419–28 |year= 1997 |pmid= 9020165 |doi=
*cite journal | author=Valenzuela A, Blanco J, Callebaut C, "et al." |title=Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles. |journal=J. Immunol. |volume=158 |issue= 8 |pages= 3721–9 |year= 1997 |pmid= 9103436 |doi=
*cite journal | author=Herbert A, Alfken J, Kim YG, "et al." |title=A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8421–6 |year= 1997 |pmid= 9237992 |doi=
*cite journal | author=Liu Y, Herbert A, Rich A, Samuel CE |title=Double-stranded RNA-specific adenosine deaminase: nucleic acid binding properties. |journal=Methods |volume=15 |issue= 3 |pages= 199–205 |year= 1998 |pmid= 9735305 |doi= 10.1006/meth.1998.0624
*cite journal | author=George CX, Samuel CE |title=Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 8 |pages= 4621–6 |year= 1999 |pmid= 10200312 |doi=
*cite journal | author=Schwartz T, Rould MA, Lowenhaupt K, "et al." |title=Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. |journal=Science |volume=284 |issue= 5421 |pages= 1841–5 |year= 1999 |pmid= 10364558 |doi=
*cite journal | author=Schade M, Turner CJ, Kühne R, "et al." |title=The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 22 |pages= 12465–70 |year= 1999 |pmid= 10535945 |doi=
*cite journal | author=Blanco J, Valenzuela A, Herrera C, "et al." |title=The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression. |journal=FEBS Lett. |volume=477 |issue= 1-2 |pages= 123–8 |year= 2000 |pmid= 10899322 |doi=
*cite journal | author=Herrera C, Morimoto C, Blanco J, "et al." |title=Comodulation of CXCR4 and CD26 in human lymphocytes. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19532–9 |year= 2001 |pmid= 11278278 |doi= 10.1074/jbc.M004586200
*cite journal | author=Wong SK, Sato S, Lazinski DW |title=Substrate recognition by ADAR1 and ADAR2. |journal=RNA |volume=7 |issue= 6 |pages= 846–58 |year= 2001 |pmid= 11421361 |doi=
*cite journal | author=Eckmann CR, Neunteufl A, Pfaffstetter L, Jantsch MF |title=The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein. |journal=Mol. Biol. Cell |volume=12 |issue= 7 |pages= 1911–24 |year= 2001 |pmid= 11451992 |doi=

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