The nuclear poly(A) binding protein, PABP2, forms an oligomeric particle covering the length of the poly(A) tail
- 31 March 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 297 (3), 569-583
- https://doi.org/10.1006/jmbi.2000.3572
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitroNucleic Acids Research, 1999
- Pre-mRNP particles: From gene to nuclear poreCurrent Biology, 1999
- Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machineryThe EMBO Journal, 1999
- Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophyNature Genetics, 1998
- Mechanism and regulation of mRNA polyadenylationGenes & Development, 1997
- Novel Drosophila melanogaster genes encoding RRM-type RNA-binding proteins identified by a degenerate PCR strategyGene, 1995
- Degradation of mRNA in eukaryotesCell, 1995
- Interactions of Escherichia coli transcription termination factor rho with RNA: II. Electron microscopy and nuclease protection experimentsJournal of Molecular Biology, 1988
- Correlation of hnRNP structure and nascent transcript cleavageCell, 1981
- The Role of the Poly(A) Sequence in Mammalian Messenger RNCritical Reviews in Biochemistry, 1981