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Editing of messenger RNA precursors and of tRNAs by adenosine to inosine conversion.
Keller W, Wolf J, Gerber A. Keller W, et al. Among authors: gerber a. FEBS Lett. 1999 Jun 4;452(1-2):71-6. doi: 10.1016/s0014-5793(99)00590-6. FEBS Lett. 1999. PMID: 10376681 Review.
ADAR1 and ADAR2 have similar sequence features, including double-stranded RNA binding domains (dsRBDs) and a deaminase domain. The tRNA-specific adenosine deaminases Tad1p and Tad2p/Tad3p modify A 37 in tRNA-Ala1 of eukaryotes and the first nucleotide of the anticod …
ADAR1 and ADAR2 have similar sequence features, including double-stranded RNA binding domains (dsRBDs) and a deaminase domain. The tR …
Purification of human double-stranded RNA-specific editase 1 (hRED1) involved in editing of brain glutamate receptor B pre-mRNA.
O'Connell MA, Gerber A, Keller W. O'Connell MA, et al. Among authors: gerber a. J Biol Chem. 1997 Jan 3;272(1):473-8. doi: 10.1074/jbc.272.1.473. J Biol Chem. 1997. PMID: 8995285
Here, we report the purification of a 90-kDa double-stranded RNA-specific adenosine deaminase from HeLa cell nuclear extract that specifically edits the glutamine codon at position 586 in the pre-mRNA of the glutamate receptor B subunit. ...Recently, a gene encoding …
Here, we report the purification of a 90-kDa double-stranded RNA-specific adenosine deaminase from HeLa cell nuclear extract that spe …
Two forms of human double-stranded RNA-specific editase 1 (hRED1) generated by the insertion of an Alu cassette.
Gerber A, O'Connell MA, Keller W. Gerber A, et al. RNA. 1997 May;3(5):453-63. RNA. 1997. PMID: 9149227 Free PMC article.
We cloned human RED1 (hRED1/hADAR2) cDNAs from a brain cDNA library. The human enzyme is 95% identical to the rat homologue. ...
We cloned human RED1 (hRED1/hADAR2) cDNAs from a brain cDNA library. The human enzyme is 95% identical to the rat homologue. ...
Purification of native and recombinant double-stranded RNA-specific adenosine deaminases.
O'Connell MA, Gerber A, Keegan LP. O'Connell MA, et al. Among authors: gerber a. Methods. 1998 May;15(1):51-62. doi: 10.1006/meth.1998.0605. Methods. 1998. PMID: 9614652
ADAR1 and ADAR2 are members of a family of enzymes that catalyze the conversion of adenosine to inosine in double-stranded RNA. ...
ADAR1 and ADAR2 are members of a family of enzymes that catalyze the conversion of adenosine to inosine in double-stranded RNA. ...
Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2.
Gerber A, Grosjean H, Melcher T, Keller W. Gerber A, et al. EMBO J. 1998 Aug 17;17(16):4780-9. doi: 10.1093/emboj/17.16.4780. EMBO J. 1998. PMID: 9707437 Free PMC article.
Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes.
Maas S, Gerber AP, Rich A. Maas S, et al. Among authors: gerber ap. Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8895-900. doi: 10.1073/pnas.96.16.8895. Proc Natl Acad Sci U S A. 1999. PMID: 10430867 Free PMC article.
It represents the functional homologue of the recently identified yeast protein Tad1p [Gerber, A., Grosjean, H., Melcher, T. & Keller, W. (1998) EMBO J. 17, 4780-4789]. ...The anticodon stem-loop of tRNA(Ala) alone is not a functional substrate for hADAT1 …
It represents the functional homologue of the recently identified yeast protein Tad1p [Gerber, A., Grosjean, H., Melcher, T. & …
An adenosine deaminase that generates inosine at the wobble position of tRNAs.
Gerber AP, Keller W. Gerber AP, et al. Science. 1999 Nov 5;286(5442):1146-9. doi: 10.1126/science.286.5442.1146. Science. 1999. PMID: 10550050
The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification.
Keegan LP, Gerber AP, Brindle J, Leemans R, Gallo A, Keller W, O'Connell MA. Keegan LP, et al. Among authors: gerber ap. Mol Cell Biol. 2000 Feb;20(3):825-33. doi: 10.1128/mcb.20.3.825-833.2000. Mol Cell Biol. 2000. PMID: 10629039 Free PMC article.
An adenosine deaminase acting on tRNAs, scTad1p (also known as scADAT1), cloned from Saccharomyces cerevisiae has a deaminase domain related to the ADARs but lacks dsRNA-binding domains. ...The enzyme has no activity on dsRNA substrates but is a tRNA deaminase with …
An adenosine deaminase acting on tRNAs, scTad1p (also known as scADAT1), cloned from Saccharomyces cerevisiae has a deaminase domain …
Patterns of developmental expression of the RNA editing enzyme rADAR2.
Paupard M-C, O'Connell MA, Gerber AP, Zukin RS. Paupard M-C, et al. Among authors: gerber ap. Neuroscience. 2000;95(3):869-79. doi: 10.1016/s0306-4522(99)00431-5. Neuroscience. 2000. PMID: 10670454
In rodents, ADAR2 undergoes alternative RNA splicing, giving rise to two splice variants that differ by the presence or absence of a 10-amino-acid insert in the carboxy-terminal catalytic domain. ...In summary, our study shows that ADAR2 messenger RNA expression is regulat …
In rodents, ADAR2 undergoes alternative RNA splicing, giving rise to two splice variants that differ by the presence or absence of a
RNA editing by base deamination: more enzymes, more targets, new mysteries.
Gerber AP, Keller W. Gerber AP, et al. Trends Biochem Sci. 2001 Jun;26(6):376-84. doi: 10.1016/s0968-0004(01)01827-8. Trends Biochem Sci. 2001. PMID: 11406411 Review.
The recent identification of tRNA-specific adenosine deaminases (ADATs) has led to the suggestion that these enzymes, as well as the cytidine and adenosine deaminases acting on pre-mRNAs (CDARs and ADARs), belong to a superfamily of RNA-dependent deaminases. ...
The recent identification of tRNA-specific adenosine deaminases (ADATs) has led to the suggestion that these enzymes, as well as the cytidin …
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