Evidence map›Paper›PMID 37277371›Full record

ArticleNature communications2023

FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions.

Guochen Qin, Menghuan Qu, Bei Jia, Wei Wang, Zhuojun Luo, Chun-Peng Song, W Andy Tao, Pengcheng Wang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 23 citations in OpenAlex.

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  12. ANAC044 orchestrates mitochondrial stress signaling to trigger iron-induced stem cell death in root meristems.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Guochen QinShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.ORCID 0000-0002-2048-8571
Menghuan QuShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.
Bei JiaShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.
Wei WangState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, 475004, Kaifeng, China.
Zhuojun LuoDepartment of Biochemistry, Purdue University, West Lafayette, IN, 47907, USA.
Chun-Peng SongState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, 475004, Kaifeng, China.ORCID 0000-0001-8774-4309
W Andy TaoDepartment of Biochemistry, Purdue University, West Lafayette, IN, 47907, USA.ORCID 0000-0002-5535-5517
Pengcheng WangInstitute of Advanced Biotechnology and School of Life Sciences, Southern University of Science and Technology, 518055, Shenzhen, China. wangpc@sustech.edu.cn.ORCID 0000-0001-6043-4132
Chinese Academy of Sciences · CNHenan University · CNPurdue University West Lafayette · USSouthern University of Science and Technology · CN

Funding

Dissecting signaling pathways and seeking EV phosphoproteins as novel biomarkers for Alzheimer's DiseaseRF1AG064250 · NIA · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2020 to 2021
$1.7M
NIA NIH HHS RF1 AG064250
6 · The paper itself

Abstract

Reversible protein S-nitrosylation regulates a wide range of biological functions and physiological activities in plants. However, it is challenging to quantitively determine the S-nitrosylation targets and dynamics in vivo. In this study, we develop a highly sensitive and efficient fluorous affinity tag-switch (FAT-switch) chemical proteomics approach for S-nitrosylation peptide enrichment and detection. We quantitatively compare the global S-nitrosylation profiles in wild-type Arabidopsis and gsnor1/hot5/par2 mutant using this approach, and identify 2,121 S-nitrosylation peptides in 1,595 protein groups, including many previously unrevealed S-nitrosylated proteins. These are 408 S-nitrosylated sites in 360 protein groups showing an accumulation in hot5-4 mutant when compared to wild type. Biochemical and genetic validation reveal that S-nitrosylation at Cys337 in ER OXIDOREDUCTASE 1 (ERO1) causes the rearrangement of disulfide, resulting in enhanced ERO1 activity. This study offers a powerful and applicable tool for S-nitrosylation research, which provides valuable resources for studies on S-nitrosylation-regulated ER functions in plants.

Indexed as

ArabidopsisArabidopsis ProteinsCysteineNitric OxideArabidopsis ProteinsCysteineNitric Oxide

Identifiers

PMID37277371
PMCPMC10241878
OpenAlexW4379467857

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.