Evidence map›Paper›PMID 29358078›Full record

ArticleMolecular cell2018

A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation.

Divya Seth, Douglas T Hess, Alfred Hausladen, Liwen Wang, Ya-Juan Wang, Jonathan S Stamler

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Cysteine-S-nitrosylation inhibits Rop5-mediated immune evasion inbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Dysregulated ProteinCirculation research · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    Review
  12. Gases define redox signalling: NO, HNature metabolism · 2025
    Article
  13. Review
  14. Review
  15. GSNOR overexpression enhances CAR-T cell stemness and anti-tumor function by enforcing mitochondrial fitness.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  16. Hydrogen Sulfide (HBiomolecules · 2024
    Review
  17. Review
  18. Article
  19. Article
  20. Article

24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Divya SethInstitute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University School of Medicine and University Hospitals Cleveland Medical Center, Cleveland, OH 44106, USA.
Douglas T HessInstitute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University School of Medicine and University Hospitals Cleveland Medical Center, Cleveland, OH 44106, USA.
Alfred HausladenInstitute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University School of Medicine and University Hospitals Cleveland Medical Center, Cleveland, OH 44106, USA.
Liwen WangCenter for Proteomics and Bioinformatics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Ya-Juan WangCenter for Proteomics and Bioinformatics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Jonathan S StamlerInstitute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University School of Medicine and University Hospitals Cleveland Medical Center, Cleveland, OH 44106, USA; Harrington Discovery Institute, University Hospitals Cleveland Medical Center, Cleveland, OH 44106, USA. Electronic address: jonathan.stamler@case.edu.
University School · USCase Western Reserve University · USUniversity Hospitals of Cleveland · US

Funding

Identification of Novel DenitrosylasesR01GM099921 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI STAMLER, JONATHAN S. · 2013 to 2016
$1.4M
NIGMS NIH HHS R01 GM099921
6 · The paper itself

Abstract

S-nitrosylation, the oxidative modification of Cys residues by nitric oxide (NO) to form S-nitrosothiols (SNOs), modifies all main classes of proteins and provides a fundamental redox-based cellular signaling mechanism. However, in contrast to other post-translational protein modifications, S-nitrosylation is generally considered to be non-enzymatic, involving multiple chemical routes. We report here that endogenous protein S-nitrosylation in the model organism E. coli depends principally upon the enzymatic activity of the hybrid cluster protein Hcp, employing NO produced by nitrate reductase. Anaerobiosis on nitrate induces both Hcp and nitrate reductase, thereby resulting in the S-nitrosylation-dependent assembly of a large interactome including enzymes that generate NO (NO synthase), synthesize SNO-proteins (SNO synthase), and propagate SNO-based signaling (trans-nitrosylases) to regulate cell motility and metabolism. Thus, protein S-nitrosylation by NO in E. coli is essentially enzymatic, and the potential generality of the multiplex enzymatic mechanism that we describe may support a re-conceptualization of NO-based cellular signaling.

Indexed as

CysteineEscherichia coliEscherichia coli ProteinsNitric OxideNitrosationOxidation-ReductionProtein Processing, Post-TranslationalProteinsProteolysisProteomicsSignal TransductionS-NitrosothiolsCysteineEscherichia coli ProteinsNitric OxideProteinsS-Nitrosothiolsiron-sulfur clusternitrate reductasenitric oxideOxyRS-nitrosylaseS-nitrosylationtrans-nitrosylase

Identifiers

PMID29358078
PMCPMC5999318
OpenAlexW2785074274

What OpenQuestion holds

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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.