Evidence map›Paper›PMID 31606089›Full record

ReviewMethods in enzymology2019

The roles of S-nitrosylation and S-glutathionylation in Alzheimer's disease.

Ryan R Dyer, Katarena I Ford, Renã A S Robinson

Open access · greenAbstract readReview
In one paragraph

Review in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

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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 1 institution in 1 country.

Ryan R DyerDepartment of Chemistry, Vanderbilt University, Nashville, TN, United States.
Katarena I FordDepartment of Chemistry, Vanderbilt University, Nashville, TN, United States.
Renã A S RobinsonDepartment of Chemistry, Vanderbilt University, Nashville, TN, United States; Department of Neurology, Vanderbilt University Medical Center, Nashville, TN, United States; Vanderbilt Memory & Alzheimer's Center, Nashville, TN, United States; Vanderbilt Institute of Chemical Biology, Nashville, TN, United States; Vanderbilt Brain Institute, Nashville, TN, United States. Electronic address: rena.as.robinson@vanderbilt.edu.
Vanderbilt University · US

Funding

Novel Multiplexing Proteomics to Study the Periphery in Alzheimer's DiseaseR01GM117191 · NIGMS · VANDERBILT UNIVERSITY · PI ROBINSON, RENA A. S. · 2016 to 2020
$2.1M
NIGMS NIH HHS R01 GM117191
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a debilitating dementia with complex pathophysiological alterations including modifications to endogenous cysteine. S-nitrosylation (SNO) is a well-studied posttranslational modification (PTM) in the context of AD while S-glutathionylation (PSSG) remains less studied. Excess reactive oxygen and reactive nitrogen species (ROS/RNS) directly or indirectly generate SNO and PSSG. SNO is dysregulated in AD and plays a pervasive role in processes such as protein function, cell signaling, metabolism, and apoptosis. Despite some studies into the role of SNO in AD, multiple identified SNO proteins lack deep investigation and SNO modifications outside of brain tissues are limited, leaving the full role of SNO in AD to be elucidated. PSSG homeostasis is perturbed in AD and may affect a myriad of cellular processes. Here we overview the role of nitric oxide (NO) in AD, discuss proteomic methodologies to investigate SNO and PSSG, and review SNO and PSSG in AD. A more thorough understanding of SNO, PSSG, and other cysteinyl PTMs in AD will be helpful for the development of novel therapeutics against neurodegenerative diseases.

Indexed as

Alzheimer DiseaseAnimalsGlutathioneHumansModels, MolecularNitric OxideProtein Processing, Post-TranslationalProteinsProteomicsReactive Nitrogen SpeciesReactive Oxygen SpeciesS-NitrosothiolsGlutathioneNitric OxideProteinsReactive Nitrogen SpeciesReactive Oxygen SpeciesS-NitrosothiolsAlzheimer's diseaseCysteineProteomicsPTMsRedox proteomicsS-gluathionylationS-nitrosylation

Identifiers

PMID31606089
PMCPMC6908309
OpenAlexW2980281056

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.