Evidence map›Paper›PMID 27064847›Full record

ArticleBiochemistry2016

S-Nitrosation of Conserved Cysteines Modulates Activity and Stability of S-Nitrosoglutathione Reductase (GSNOR).

Damian Guerra, Keith Ballard, Ian Truebridge, Elizabeth Vierling

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 120 citations in OpenAlex.

  1. Review
  2. Integration of NO and HPlant communications · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. De-nitrosylation Coordinates Appressorium Function for Infection of the Rice Blast Fungus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Functions of NO and HMethods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Review
  14. Review
  15. Molecular dissection of a dedicated formaldehyde dehydrogenase from Mycobacterium smegmatis.Protein science : a publication of the Protein Society · 2022
    Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. PodocyteFrontiers in pharmacology · 2021
    Article
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

4 authors at 1 institution in 1 country.

Damian GuerraDepartment of Biochemistry and Molecular Biology, University of Massachusetts , 240 Thatcher Road, Amherst, Massachusetts 01003, United States.
Keith BallardDepartment of Biochemistry and Molecular Biology, University of Massachusetts , 240 Thatcher Road, Amherst, Massachusetts 01003, United States.
Ian TruebridgeDepartment of Biochemistry and Molecular Biology, University of Massachusetts , 240 Thatcher Road, Amherst, Massachusetts 01003, United States.
Elizabeth VierlingDepartment of Biochemistry and Molecular Biology, University of Massachusetts , 240 Thatcher Road, Amherst, Massachusetts 01003, United States.
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

The free radical nitric oxide (NO(•)) regulates diverse physiological processes from vasodilation in humans to gas exchange in plants. S-Nitrosoglutathione (GSNO) is considered a principal nitroso reservoir due to its chemical stability. GSNO accumulation is attenuated by GSNO reductase (GSNOR), a cysteine-rich cytosolic enzyme. Regulation of protein nitrosation is not well understood since NO(•)-dependent events proceed without discernible changes in GSNOR expression. Because GSNORs contain evolutionarily conserved cysteines that could serve as nitrosation sites, we examined the effects of treating plant (Arabidopsis thaliana), mammalian (human), and yeast (Saccharomyces cerevisiae) GSNORs with nitrosating agents in vitro. Enzyme activity was sensitive to nitroso donors, whereas the reducing agent dithiothreitol (DTT) restored activity, suggesting that catalytic impairment was due to S-nitrosation. Protein nitrosation was confirmed by mass spectrometry, by which mono-, di-, and trinitrosation were observed, and these signals were sensitive to DTT. GSNOR mutants in specific non-zinc-coordinating cysteines were less sensitive to catalytic inhibition by nitroso donors and exhibited reduced nitrosation signals by mass spectrometry. Nitrosation also coincided with decreased tryptophan fluorescence, increased thermal aggregation propensity, and increased polydispersity-properties reflected by differential solvent accessibility of amino acids important for dimerization and the shape of the substrate and coenzyme binding pockets as assessed by hydrogen-deuterium exchange mass spectrometry. Collectively, these data suggest a mechanism for NO(•) signal transduction in which GSNOR nitrosation and inhibition transiently permit GSNO accumulation.

Indexed as

Aldehyde OxidoreductasesAmino Acid SequenceArabidopsisCysteineCytosolHumansNitric OxideNitrosationProtein ConformationSaccharomyces cerevisiaeSequence Homology, Amino AcidSignal TransductionS-NitrosoglutathioneAldehyde OxidoreductasesCysteineformaldehyde dehydrogenase, glutathione-independentNitric OxideS-Nitrosoglutathione

Identifiers

PMID27064847
PMCPMC4974627
OpenAlexW2331965877

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.