ArticleBiochemical and biophysical research communications2007
Alternative polyadenylation sites of human endothelial nitric oxide synthase mRNA.
Article in Biochemical and biophysical research communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- Poly(A) polymerase (PAP) diversity in gene expression--star-PAP vs canonical PAP.FEBS letters · 2014Review
- A family of splice variants of CstF-64 expressed in vertebrate nervous systems.BMC molecular biology · 2009Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The mRNA 3'-untranslated region (3'-UTR) has been shown to have important roles in the regulation of mRNA function. In this study, we investigated the human endothelial nitric oxide synthase (eNOS) 3'-UTR to evaluate its potential regulatory role. 3'-RACE analysis revealed that the human eNOS mRNA has multiple alternative polyadenylation sites. Apart from the proximal site (418bp downstream of the stop codon), we identified two additional distal sites approximately 770 and 1478bp downstream of the stop codon. In addition, Northern analysis showed that the usage of these sites differed among human tissues. Further, amounts of these eNOS mRNAs were changed during growth of cultured human aortic endothelial cells; mRNAs with long 3'-UTRs decreased more rapidly than total mRNA, as cells approached confluency. Thus, the 3'-UTRs of human eNOS results from alternative polyadenylation sites and differ across tissues and during cell growth.
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