ArticleMolecular biology reports2009
RNAi-mediated knock-down of gene mN6A1 reduces cell proliferation and decreases protein translation.
Article in Molecular biology reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 5 citations in OpenAlex.
- Full-protein release assay in a reconstituted yeast translation system using GGQ-methylated eRF1.Frontiers in molecular biosciences · 2026Article
- N-6-adenine-specific DNA methyltransferase 1 (N6AMT1) polymorphisms and arsenic methylation in Andean women.Environmental health perspectives · 2013Article
- RNAi assay in primary cells: a new method for gene function analysis in marine bivalve.Molecular biology reports · 2012Article
- The role of cell cycle-dependent neuropathy target esterase in cell proliferation.Molecular biology reports · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methyltransferases play essential roles in modulating important cellular and metabolic processes. A mouse putative N6-DNA methyltransferase gene (GenBank No AY456393) is a novel gene named mN6amt1(mN6A1). To investigate its function in cell fate and protein translation, RNA interference (RNAi)-mediated knock-down method was established. Cell cycle analysis suggests that the cell proliferation decreases after RNAi with mN6A1. The expression plasmid of luciferase was used to detect protein translation, and the results showed that luciferase expression decreased after RNAi with mN6A1, whereas increased after over-expression of mN6A1 or/and eRF1. The binding between mN6A1 and eRF1 was identified by co-immunoprecipitation and pull-down experiments. It might be suggested that mN6A1 participates in protein translation through interaction with eRF1.
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