Evidence map›Paper›PMID 28450148›Full record

ArticleFree radical biology & medicine2017

Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry.

Changgong Wu, Huacheng Dai, Lin Yan, Tong Liu, Chuanglong Cui, Tong Chen, Hong Li

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Free radical biology & medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

7 authors at 1 institution in 1 country.

Changgong WuCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America.
Huacheng DaiCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America.
Lin YanCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America.
Tong LiuCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America.
Chuanglong CuiCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America.
Tong ChenCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America.
Hong LiCenter for Advanced Proteomics Research and the Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers University - New Jersey Medical School, Cancer Center, Newark, NJ 07103, The United States of America. Electronic address: liho2@rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Rutgers Mass Spectrometry Core for Integrative Neuroscience ResearchP30NS046593 · NINDS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI LOBEL, PETER · 2004 to 2018
$9.9M
NO signaling by a Soluble Guanylyl Cyclase-Thioredoxin transnitrosation complexR01GM112415 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI BEUVE, ANNIE V · 2015 to 2023
$3.5M
NIGMS NIH HHS R01 GM112415NINDS NIH HHS P30 NS046593
6 · The paper itself

Abstract

Peroxiredoxin 1 (Prx1) is an essential peroxidase that reduces cellular peroxides. It holds 2 indispensable cysteines for its activity: a peroxidatic cysteine (C

Indexed as

AnimalsCysteineHeLa CellsHumansHydrogen PeroxideMammalsMass SpectrometryOxidation-ReductionOxidative StressPeroxiredoxinsProtein EngineeringCysteinecysteine sulfonateHydrogen PeroxidePeroxiredoxinsPRDX1 protein, humanMass spectrometryOxidative stressPeroxiredoxinSulfonation

Identifiers

PMID28450148
PMCPMC5564515
OpenAlexW2610093409

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.