Evidence map›Paper›PMID 29600457›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Direct Measurement of S-Nitrosothiols with an Orbitrap Fusion Mass Spectrometer: S-Nitrosoglutathione Reductase as a Model Protein.

Damian Guerra, Ian Truebridge, Stephen J Eyles, Patrick Treffon, Elizabeth Vierling

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 96% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Damian GuerraDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
Ian TruebridgeDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
Stephen J EylesDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
Patrick TreffonDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
Elizabeth VierlingDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA. Vierling@biochem.umass.edu.
University of Massachusetts Amherst · USUniversity of Colorado Anschutz Medical Campus · US

Funding

Acquisition of an Orbitrap MSS10OD010645 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI EYLES, STEPHEN J. · 2013 to 2013
$600k
NIH HHS S10 OD010645
6 · The paper itself

Abstract

Recent studies suggest cysteine S-nitrosation of S-nitrosoglutathione reductase (GSNOR) could regulate protein redox homeostasis. "Switch" assays enable discovery of putatively S-nitrosated proteins. However, with few exceptions, researchers have not examined the kinetics and biophysical consequences of S-nitrosation. Methods to quantify protein S-nitrosothiol (SNO) abundance and formation kinetics would bridge this mechanistic gap and allow interpretation of the consequences of specific modifications, as well as facilitate development of specific S-nitrosation inhibitors. Here, we describe a rapid assay to estimate protein SNO abundance with intact protein electrospray ionization mass spectrometry. Originally designed using recombinant GSNOR, these methods are applicable to any purified protein to test for or further study nitrosatable cysteines.

Indexed as

Spectrometry, Mass, Electrospray IonizationAldehyde OxidoreductasesNitrosationRecombinant Fusion ProteinsS-NitrosothiolsAldehyde Oxidoreductasesformaldehyde dehydrogenase, glutathione-independentRecombinant Fusion ProteinsS-NitrosothiolsCysteine modificationGSNORMass spectrometryOrbitrap fusionRedox switchS-nitrosationS-nitrosothiol (SNO)

Identifiers

PMID29600457
PMCPMC5901646
OpenAlexW2795063759

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.