Evidence map›Paper›PMID 25064181›Full record

ReviewNitric oxide : biology and chemistry2014

Nitrosothiol signaling and protein nitrosation in cell death.

Anand Krishnan V Iyer, Yon Rojanasakul, Neelam Azad

Abstract readReview
In one paragraph

Review in Nitric oxide : biology and chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Nitric Oxide: Physiological Functions, Delivery, and Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  6. Article
  7. Article
  8. Dietary supplements and vascular function in hypertensive disorders of pregnancy.Pflugers Archiv : European journal of physiology · 2023
    Review
  9. Review
  10. Article
  11. Biological Mechanisms ofAntioxidants (Basel, Switzerland) · 2021
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. 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

3 authors at 2 institutions in 1 country.

Anand Krishnan V IyerDepartment of Pharmaceutical Sciences, Hampton University, Hampton, VA 23668, USA. Electronic address: anand.iyer@hamptonu.edu.
Yon RojanasakulDepartment of Pharmaceutical Sciences, West Virginia University, Morgantown, WV 26505, USA.
Neelam AzadDepartment of Pharmaceutical Sciences, Hampton University, Hampton, VA 23668, USA.
Hampton University · USWest Virginia University · US

Funding

Anti-Tumorigenic Potential of Novel Digitoxin AnaloguesSC1CA173069 · NCI · HAMPTON UNIVERSITY · PI IYER, ANAND K. · 2012 to 2016
$1.3M
Impact of Oxidative Stress-Regulated Angiogenesis in Pulmonary FibrosisSC1HL112630 · NHLBI · HAMPTON UNIVERSITY · PI AZAD, NEELAM · 2011 to 2015
$1.3M
NCI NIH HHS SC1 CA173069NHLBI NIH HHS SC1 HL112630
6 · The paper itself

Abstract

Nitric oxide, a reactive free radical, is an important signaling molecule that can lead to a plethora of cellular effects affecting homeostasis. A well-established mechanism by which NO manifests its effect on cellular functions is the post-translational chemical modification of cysteine thiols in substrate proteins by a process known as S-nitrosation. Studies that investigate regulation of cellular functions through NO have increasingly established S-nitrosation as the primary modulatory mechanism in their respective systems. There has been a substantial increase in the number of reports citing various candidate proteins undergoing S-nitrosation, which affects cell-death and -survival pathways in a number of tissues including heart, lung, brain and blood. With an exponentially growing list of proteins being identified as substrates for S-nitrosation, it is important to assimilate this information in different cell/tissue systems in order to gain an overall view of protein regulation of both individual proteins and a class of protein substrates. This will allow for broad mapping of proteins as a function of S-nitrosation, and help delineate their global effects on pathophysiological responses including cell death and survival. This information will not only provide a much better understanding of overall functional relevance of NO in the context of various disease states, it will also facilitate the generation of novel therapeutics to combat specific diseases that are driven by NO-mediated S-nitrosation.

Indexed as

Cell DeathSignal TransductionNitroso CompoundsProteinsSulfhydryl CompoundsNitroso CompoundsProteinsSulfhydryl CompoundsApoptosisCancerCell deathNitrosationS-nitrosylationSurvival

Identifiers

PMID25064181
PMCPMC4258442
OpenAlexW2082110706

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.