DTL, the Drosophila Homolog of PIMT/Tgs1 Nuclear Receptor Coactivator-interacting Protein/RNA Methyltransferase, Has an Essential Role in Development
Open Access
- 1 April 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (13) , 12397-12404
- https://doi.org/10.1074/jbc.m409251200
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Specificity and Mechanism of RNA Cap Guanine-N2 Methyltransferase (Tgs1)Published by Elsevier ,2005
- Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylaseNucleic Acids Research, 2003
- Interaction of PIMT with Transcriptional Coactivators CBP, p300, and PBP Differential Role in Transcriptional RegulationPublished by Elsevier ,2002
- Hypermethylation of the Cap Structure of Both Yeast snRNAs and snoRNAs Requires a Conserved Methyltransferase that Is Localized to the NucleolusMolecular Cell, 2002
- Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP functionProceedings of the National Academy of Sciences, 2001
- Tat as a transcriptional activator and a potential therapeutic target for HIV-IPublished by Elsevier ,2000
- Biochemical and Functional Interactions between HIV-1 Tat Protein and TAR RNAArchives of Biochemistry and Biophysics, 1999
- Selection of RNA-binding peptides in vivoNature, 1996
- Vectors for Drosophila P-element-mediated transformation and tissue culture transfectionGene, 1988
- Signals for ribosomal frameshifting in the rous sarcoma virus gag-pol regionCell, 1988