Evidence map›Paper›PMID 36243209›Full record

ReviewFree radical biology & medicine2022

Hidden networks of aberrant protein transnitrosylation contribute to synapse loss in Alzheimer's disease.

Stuart A Lipton

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Redox organization of living systems.Free radical biology & medicine · 2024
    Review
  6. Review
  7. Review
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

1 author at 1 institution in 1 country.

Stuart A LiptonNeurodegeneration New Medicines Center and Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, USA; Department of Neurosciences, University of California, San Diego, School of Medicine, La Jolla, CA, 92093, USA; Department of Neurology, Yale School of Medicine, New Haven, CT, 6510, USA. Electronic address: slipton@scripps.edu.
Scripps Research Institute · US

Funding

Novel Proteomics Approach to HIV-Associated Neurocognitive Disorder & Drug AbuseDP1DA041722 · NIDA · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2016 to 2020
$7.0M
Leadership in AD/ADRD Drug DiscoveryR35AG071734 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2021 to 2025
$5.4M
Omics Analyses of HIV and Substance Use DisorderR01DA048882 · NIDA · SCRIPPS RESEARCH INSTITUTE, THE · PI REPUNTE-CANONIGO, VEZ · 2019 to 2023
$4.3M
Dynamic Interactions of the S-Nitrosoproteome in Type 2 Diabetes/Metabolic Syndrome and Alzheimer’s DiseaseRF1AG057409 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2017 to 2020
$4.1M
S-Nitrosylation-Induced Posttranslational Modification and Aberrant Cell Signaling in Sporadic Alzheimer's DiseaseR01AG056259 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2017 to 2021
$3.3M
Crosstalk between innate-immunity human microglia and adaptive-immunity Tregs in Alzheimer's diseaseR01AG078756 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI STUART A LIPTON · 2022 to 2026
$2.3M
Pro-Electrophilic Drugs PEDs for Alzheimer's DiseaseR56AG065372 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI LIPTON, STUART A · 2020 to 2021
$1.8M
NIA NIH HHS R01 AG056259NIA NIH HHS R01 AG078756NIA NIH HHS R35 AG071734NIA NIH HHS R56 AG065372NIA NIH HHS RF1 AG057409NIDA NIH HHS DP1 DA041722NIDA NIH HHS R01 DA048882
6 · The paper itself

Abstract

Emerging evidence indicates the importance of S-nitrosation in regulating protein function and activity. This chemical reaction has been termed protein S-nitrosylation to emphasize its biological importance as a posttranslational modification, in some ways reminiscent of phosphorylation. The reaction at cysteine thiols is distinct from other chemical reactions of nitric oxide (NO) that activate soluble guanylate cyclase via nitrosylation of heme or formation of peroxynitrite via reaction with superoxide anion to produce tyrosine nitration. Here, we review the importance of pathological, aberrant transnitrosylation reactions, i.e., transfer of the NO group from one protein to another, and its consequent effect on the pathogenesis of neurological disorders, to date on Alzheimer's disease (AD), but also expected to affect Parkinson's disease (PD)/Lewy body dementia (LBD), HIV-associated neurocognitive disorder (HAND), and other neurodegenerative and neurodevelopmental disorders.

Indexed as

Alzheimer DiseaseHumansNitric OxideNitrosationProteinsSynapsesNitric OxideProteins

Identifiers

PMID36243209
PMCPMC9875813
OpenAlexW4304890517

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.