Evidence map›Paper›PMID 24895380›Full record

ArticleMolecular & cellular proteomics : MCP2014

Global analysis of S-nitrosylation sites in the wild type (APP) transgenic mouse brain-clues for synaptic pathology.

Monika Zaręba-Kozioł, Agnieszka Szwajda, Michał Dadlez, Aleksandra Wysłouch-Cieszyńska, Maciej Lalowski

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

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  14. S-nitrosation of proteins relevant to Alzheimer's disease during early stages of neurodegeneration.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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  16. Review
  17. Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
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  18. 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

5 authors at 4 institutions in 2 countries.

Monika Zaręba-KoziołFrom the ‡Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland;
Agnieszka Szwajda§Institute for Molecular Medicine Finland (FIMM), Helsinki, Finland;
Michał DadlezFrom the ‡Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland;
Aleksandra Wysłouch-CieszyńskaFrom the ‡Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland; maciej.lalowski@helsinki.fi olawyslouch@ibb.waw.pl.
Maciej Lalowski¶Biomedicum Helsinki, Institute of Biomedicine, Biochemistry/Developmental Biology, Meilahti Clinical Proteomics Core Unit, University of Helsinki, Finland; ‖Folkhälsan Institute of Genetics, Helsinki, Finland maciej.lalowski@helsinki.fi olawyslouch@ibb.waw.pl.
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLInstitute for Molecular Medicine Finland · FIPolish Academy of Sciences · PLUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is characterized by an early synaptic loss, which strongly correlates with the severity of dementia. The pathogenesis and causes of characteristic AD symptoms are not fully understood. Defects in various cellular cascades were suggested, including the imbalance in production of reactive oxygen and nitrogen species. Alterations in S-nitrosylation of several proteins were previously demonstrated in various AD animal models and patients. In this work, using combined biotin-switch affinity/nano-LC-MS/MS and bioinformatic approaches we profiled endogenous S-nitrosylation of brain synaptosomal proteins from wild type and transgenic mice overexpressing mutated human Amyloid Precursor Protein (hAPP). Our data suggest involvement of S-nitrosylation in the regulation of 138 synaptic proteins, including MAGUK, CamkII, or synaptotagmins. Thirty-eight proteins were differentially S-nitrosylated in hAPP mice only. Ninety-five S-nitrosylated peptides were identified for the first time (40% of total, including 33 peptides exclusively in hAPP synaptosomes). We verified differential S-nitrosylation of 10 (26% of all identified) synaptosomal proteins from hAPP mice, by Western blotting with specific antibodies. Functional enrichment analysis linked S-nitrosylated proteins to various cellular pathways, including: glycolysis, gluconeogenesis, calcium homeostasis, ion, and vesicle transport, suggesting a basic role of this post-translational modification in the regulation of synapses. The linkage of SNO-proteins to axonal guidance and other processes related to APP metabolism exclusively in the hAPP brain, implicates S-nitrosylation in the pathogenesis of Alzheimer's disease.

Indexed as

Protein Processing, Post-TranslationalAnimalsBrainFemaleMice, TransgenicNerve Tissue ProteinsNitric Oxide Synthase Type INitric Oxide Synthase Type IIS-NitrosothiolsSynapsesSynaptosomesNerve Tissue ProteinsNitric Oxide Synthase Type INitric Oxide Synthase Type IINos1 protein, mouseNos2 protein, mouseS-Nitrosothiols

Identifiers

PMID24895380
PMCPMC4159650
OpenAlexW2140005295

What OpenQuestion holds

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Registered trials

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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.