Mutational Analysis of Baculovirus Capping Enzyme Lef4 Delineates an Autonomous Triphosphatase Domain and Structural Determinants of Divalent Cation Specificity
Open Access
- 1 December 2001
- journal article
- Published by Elsevier
- Vol. 276 (49) , 45522-45529
- https://doi.org/10.1074/jbc.m107615200
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- A yeast-like mRNA capping apparatus in Plasmodium falciparumProceedings of the National Academy of Sciences, 2001
- RNA Triphosphatase Component of the mRNA Capping Apparatus of Paramecium bursaria Chlorella Virus 1Journal of Virology, 2001
- Characterization of Schizosaccharomyces pombe RNA triphosphataseNucleic Acids Research, 2001
- Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active siteNucleic Acids Research, 2000
- Structure, mechanism, and evolution of the mRNA capping apparatusProgress in Nucleic Acid Research and Molecular Biology, 2000
- Mutational Analyses of Yeast RNA Triphosphatases Highlight a Common Mechanism of Metal-dependent NTP Hydrolysis and a Means of Targeting Enzymes to Pre-mRNAs in Vivo by Fusion to the Guanylyltransferase Component of the Capping ApparatusJournal of Biological Chemistry, 1999
- Yeast and Viral RNA 5′ Triphosphatases Comprise a New Nucleoside Triphosphatase FamilyJournal of Biological Chemistry, 1998
- Phylogeny of mRNA capping enzymesProceedings of the National Academy of Sciences, 1997
- X-Ray Crystallography Reveals a Large Conformational Change during Guanyl Transfer by mRNA Capping EnzymesCell, 1997
- Domain structure of vaccinia DNA ligaseNucleic Acids Research, 1997