ArticlePloS one2026
Monitoring of Cd and GSH contents and Bn-OASTL expression in transgenic tobacco seedlings in response to Cd stress.
Article in PloS one, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cadmium (Cd) pollution threatens agricultural productivity and food safety. O-acetylserine(thiol)lyase (OASTL) genes have been tied to plant responses to heavy metal stress, yet their roles in heterologous systems, particularly in Cd accumulation and tolerance, remain unclear. Here, we isolated a novel OASTL gene, BnaOASTL, from the high-Cd-accumulating oilseed rape cultivar Brassica napus "Nanyou 868" and expressed it in tobacco (Nicotiana benthamiana). Transgenic lines were exposed to Cd stress, and Cd content, glutathione (GSH) level, and BnaOASTL expression were evaluated. The full-length BnaOASTL cDNA (969 bp) encoded a cytoplasmic/nuclear protein of 322 amino acids. Under Cd stress, Bn-OASTL expression was significantly upregulated in transgenic plants, particularly in roots. However, compared with wild-type, transgenic lines showed no improvement in Cd tolerance or accumulation and no significant changes in GSH levels. The findings suggest that although BnaOASTL is transcriptionally responsive to Cd stress, its overexpression alone does not confer altered Cd tolerance or accumulation in tobacco. The study highlights the complexity of Cd response mechanisms and suggests that BnaOASTL functions within a broader, species-specific regulatory network.
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