Evidence map›Paper›PMID 28714690›Full record

ArticleJournal of proteome research2017

Selective Affinity Enrichment of Nitrotyrosine-Containing Peptides for Quantitative Analysis in Complex Samples.

Yingxin Zhao, Yueqing Zhang, Hong Sun, Rosario Maroto, Allan R Brasier

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Nitration in cancer signaling.Redox biology · 2026
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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

5 authors at 2 institutions in 1 country.

Yingxin ZhaoDepartment of Internal Medicine, University of Texas Medical Branch (UTMB) , Galveston, Texas 77555, United States.ORCID 0000-0002-8872-5860
Yueqing ZhangDepartment of Internal Medicine, University of Texas Medical Branch (UTMB) , Galveston, Texas 77555, United States.
Hong SunDepartment of Internal Medicine, University of Texas Medical Branch (UTMB) , Galveston, Texas 77555, United States.
Rosario MarotoInstitute for Translational Sciences, UTMB , Galveston, Texas 77555, United States.
Allan R BrasierDepartment of Internal Medicine, University of Texas Medical Branch (UTMB) , Galveston, Texas 77555, United States.
John Sealy Hospital · USThe University of Texas Medical Branch at Galveston · US

Funding

UTMB Clinical and Translational Science AwardUL1TR001439 · NCATS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI URBAN, RANDALL J · 2015 to 2024
$40.0M
Virus, Tissue Culture and ImmunoassayP01AI062885 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI GAROFALO, ROBERTO P · 2005 to 2022
$23.9M
Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
NCATS NIH HHS UL1 TR001439NIAID NIH HHS P01 AI062885NIEHS NIH HHS P30 ES006676
6 · The paper itself

Abstract

Protein tyrosine nitration by oxidative and nitrate stress is important in the pathogenesis of many inflammatory or aging-related diseases. Mass spectrometry analysis of protein nitrotyrosine is very challenging because the non-nitrated peptides suppress the signals of the low-abundance nitrotyrosine (NT) peptides. No validated methods for enrichment of NT-peptides are currently available. Here we report an immunoaffinity enrichment of NT-peptides for proteomics analysis. The effectiveness of this approach was evaluated using nitrated protein standards and whole-cell lysates in vitro. A total of 1881 NT sites were identified from a nitrated whole-cell extract, indicating that this immunoaffinity-MS method is a valid approach for the enrichment of NT-peptides, and provides a significant advance for characterizing the nitrotyrosine proteome. We noted that this method had higher affinity to peptides with N-terminal nitrotyrosine relative to peptides with other nitrotyrosine locations, which raises the need for future study to develop a pan-specific nitrotyrosine antibody for unbiased, proteome-wide analysis of tyrosine nitration. We applied this method to quantify the changes in protein tyrosine nitration in mouse lungs after intranasal poly(I:C) treatment and quantified 237 NT sites. This result indicates that the immunoaffinity-MS method can be used for quantitative analysis of protein nitrotyrosines in complex samples.

Indexed as

AnimalsAntibodiesBinding SitesLungMicePeptidesPoly I-CProteomicsTyrosine3-nitrotyrosineAntibodiesPeptidesPoly I-CTyrosineaffinity enrichmentmass spectrometryposttranslational modificationsprotein tyrosine nitration

Identifiers

PMID28714690
PMCPMC5656043
OpenAlexW2734877409

What OpenQuestion holds

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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.