Evidence map›Paper›PMID 26707925›Full record

ReviewTrends in pharmacological sciences2016

Protein S-Nitrosylation as a Therapeutic Target for Neurodegenerative Diseases.

Tomohiro Nakamura, Stuart A Lipton

Open access · greenAbstract readReview
In one paragraph

Review in Trends in pharmacological sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
10.6field-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

93 citing papers in PubMed, 157 citations in OpenAlex.

  1. Review
  2. Gas entrapping materials for damage control.Advanced drug delivery reviews · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Stress-induced nuclear GAPDH: Scientific update and clinical application.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  9. Review
  10. Review
  11. Article
  12. Hydrogen Sulfide (HInternational journal of molecular sciences · 2025
    Review
  13. Article
  14. Nitric Oxide Signaling and Sensing in Age-Related Diseases.Antioxidants (Basel, Switzerland) · 2024
    Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Review

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

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

2 authors at 2 institutions in 1 country.

Tomohiro NakamuraScintillon Institute, San Diego, CA 92121, USA. Electronic address: tnakamura@scintillon.org.
Stuart A LiptonScintillon Institute, San Diego, CA 92121, USA; Department of Neurosciences, University of California, San Diego School of Medicine, La Jolla, CA 92039, USA. Electronic address: slipton@ucsd.edu.
Scintillon Institute · USUniversity of California, San Diego · US

Funding

PROJECT III - GENETIC APPROACH TO EXCITATORY TRANSMISSIONP01HD029587 · NICHD · SCINTILLON INSTITUTE FOR PHOTOBIOLOGY · PI LIPTON, STUART A · 1992 to 2016
$21.9M
Novel Proteomics Approach to HIV-Associated Neurocognitive Disorder & Drug AbuseDP1DA041722 · NIDA · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2016 to 2020
$7.0M
Modeling Parkinson's Disease with Isogenic hiPSC-Derived Dopaminergic NeuronsR01NS086890 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2014 to 2018
$2.1M
NICHD NIH HHS P01 HD029587NIDA NIH HHS DP1 DA041722NINDS NIH HHS R01 NS086890
6 · The paper itself

Abstract

At physiological levels, nitric oxide (NO) contributes to the maintenance of normal neuronal activity and survival, thus serving as an important regulatory mechanism in the central nervous system. By contrast, accumulating evidence suggests that exposure to environmental toxins or the normal aging process can trigger excessive production of reactive oxygen/nitrogen species (such as NO), contributing to the etiology of several neurodegenerative diseases. We highlight here protein S-nitrosylation, resulting from covalent attachment of an NO group to a cysteine thiol of the target protein, as a ubiquitous effector of NO signaling in both health and disease. We review our current understanding of this redox-dependent post-translational modification under neurodegenerative conditions, and evaluate how targeting dysregulated protein S-nitrosylation can lead to novel therapeutics.

Indexed as

Glyceraldehyde-3-Phosphate DehydrogenasesHumansNeurodegenerative DiseasesNitric OxideNitrosationProtein Processing, Post-TranslationalReactive Nitrogen SpeciesReceptors, N-Methyl-D-AspartateSecond Messenger SystemsS-NitrosothiolsGlyceraldehyde-3-Phosphate DehydrogenasesNitric OxideReactive Nitrogen SpeciesReceptors, N-Methyl-D-AspartateS-NitrosothiolsAlzheimer's diseasedenitrosylationNitroMemantineParkinson's diseaseprotein S-nitrosylationtransnitrosylation

Identifiers

PMID26707925
PMCPMC4698225
OpenAlexW2197855706

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.