Evidence map›Paper›PMID 23719160›Full record

ReviewNeuron2013

Aberrant protein s-nitrosylation in neurodegenerative diseases.

Tomohiro Nakamura, Shichun Tu, Mohd Waseem Akhtar, Carmen R Sunico, Shu-Ichi Okamoto, Stuart A Lipton

Open access · bronzeAbstract readReview
In one paragraph

Review in Neuron, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 191 papers.

0numbers the graph read from it
0cells of the map it votes in
191citing papers in PubMed
17.5field-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

191 citing papers in PubMed, 347 citations in OpenAlex.

  1. Review
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  13. Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  14. Redox modulation of the complement cascade contributes to synapse loss in Alzheimer's disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. S-Nitrosylation of CRTC1 in Alzheimer's disease impairs CREB-dependent gene expression induced by neuronal activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Review
  20. Article

131 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

6 authors at 1 institution in 1 country.

Tomohiro NakamuraDel E. Web Center for Neuroscience, Aging, and Stem Cell Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. tnakamura@sanfordburnham.org
Shichun Tu
Mohd Waseem Akhtar
Carmen R Sunico
Shu-Ichi Okamoto
Stuart A Lipton
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

PROJECT III - GENETIC APPROACH TO EXCITATORY TRANSMISSIONP01HD029587 · NICHD · SCINTILLON INSTITUTE FOR PHOTOBIOLOGY · PI LIPTON, STUART A · 1992 to 2016
$21.9M
Project 4: A Developmental Perspective to Nitrosative/Oxidative SusceptibilityP01ES016738 · NIEHS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LIPTON, STUART A · 2008 to 2012
$8.5M
Project-002P30NS076411 · NINDS · SCINTILLON INSTITUTE FOR PHOTOBIOLOGY · PI LIPTON, STUART A · 2011 to 2016
$4.5M
Protection of Brain Injury from Cyanide Poisoning by Carnosic AcidR21NS080799 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LIPTON, STUART A · 2012 to 2013
$975k
NICHD NIH HHS P01 HD029587NICHD NIH HHS P01 HD29587NIEHS NIH HHS P01 ES01673NIEHS NIH HHS P01 ES016738NINDS NIH HHS P30 NS076411NINDS NIH HHS R21 NS080799
6 · The paper itself

Abstract

S-Nitrosylation is a redox-mediated posttranslational modification that regulates protein function via covalent reaction of nitric oxide (NO)-related species with a cysteine thiol group on the target protein. Under physiological conditions, S-nitrosylation can be an important modulator of signal transduction pathways, akin to phosphorylation. However, with aging or environmental toxins that generate excessive NO, aberrant S-nitrosylation reactions can occur and affect protein misfolding, mitochondrial fragmentation, synaptic function, apoptosis or autophagy. Here, we discuss how aberrantly S-nitrosylated proteins (SNO-proteins) play a crucial role in the pathogenesis of neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. Insight into the pathophysiological role of aberrant S-nitrosylation pathways will enhance our understanding of molecular mechanisms leading to neurodegenerative diseases and point to potential therapeutic interventions.

Indexed as

AnimalsBrainHumansNerve Tissue ProteinsNeurodegenerative DiseasesNitric OxideNitric Oxide SynthaseReactive Nitrogen SpeciesNerve Tissue ProteinsNitric OxideNitric Oxide SynthaseReactive Nitrogen Species

Identifiers

PMID23719160
PMCPMC3712898
OpenAlexW2164545630

What Socratic 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 Socratic graph.