ArticlePlant signaling & behavior2018
Evidence that thiol-based redox state is critical for xylem vessel cell differentiation.
Article in Plant signaling & behavior, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 11 citations in OpenAlex.
- Excess nitric oxide alters cellular pH to restrict salicylic acid movement and systemic immunity.Science advances · 2026Article
- Role of protein S-nitrosylation in plant growth and development.Plant cell reports · 2024Review
- NAC domain transcription factors VNI2 and ATAF2 form protein complexes and regulate leaf senescence.Plant direct · 2023Article
- VND-INTERACTING2 effectively inhibits transcriptional activities of VASCULAR-RELATED NAC-DOMAIN7 through a conserved sequence.Plant biotechnology (Tokyo, Japan) · 2022Article
- Histone Deacetylation Controls Xylem Vessel Cell DifferentiationFrontiers in plant science · 2021Article
- Isolation of dominant ArabidopsisPlant biotechnology (Tokyo, Japan) · 2020Article
- The Progression of Xylem Vessel Cell Differentiation is Dependent on the Activity Level of VND7 inPlants (Basel, Switzerland) · 2019Article
- Creating vessel elements in vitro: Towards a comprehensive understanding of the molecular basis of xylem vessel element differentiation.Plant biotechnology (Tokyo, Japan) · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitric oxide (NO), which plays essential roles in a variety of cell signaling processes, is the precursor of a family of NO-derived molecules, including toxic reactive nitrogen species. The NO-based regulation of cellular activity is mediated by the reversible modification of cysteine thiol groups in redox-sensitive proteins. One such modification is protein S-nitrosylation, i.e., the addition of an NO moiety to a cysteine thiol, and this S-nitrosylation is regulated by enzymes such as S-nitrosoglutathione reductase (GSNOR). Recently, we reported a novel loss-of-function allele of gsnor1, named suppressor of ectopic vessel cell differentiation induced by VND7-1 (seiv1), based on the VND7-inducible system, in which almost all cell types are transdifferentiated into xylem vessel cells upon activation of the NAC transcription factor VND7. We also found that VND7 can be S-nitrosylated and that the target cysteine residues for S-nitrosylation are critical for VND7 transactivation activity. Here, we further discuss roles for GSNOR1 in xylem vessel cell differentiation, and provide additional data on the effects of cellular NO level on VND7 activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.