Evidence map›Paper›PMID 37248656›Full record

ReviewProteomics2023

Thiol redox proteomics: Characterization of thiol-based post-translational modifications.

Xiaolu Li, Austin Gluth, Tong Zhang, Wei-Jun Qian

Open access · hybridAbstract readReview
In one paragraph

Review in Proteomics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
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  7. Proteoforms as the true units of physiological function.European journal of applied physiology · 2026
    Review
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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

4 authors at 1 institution in 1 country.

Xiaolu LiBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.
Austin GluthBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.
Tong ZhangBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.
Wei-Jun QianBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington, USA.ORCID 0000-0002-5393-2827
Pacific Northwest National Laboratory · US

Funding

Pathways and Regulators Driving Progressive Islet Cell Dysfunction in Type 1 DiabetesR01DK122160 · NIDDK · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI ROHIT N. KULKARNI, CLAYTON E MATHEWS · 2019 to 2026
$3.7M
Reverse Sensitivity Analysis for Identifying Predictive Proteomics Signatures of CancerU01CA227544 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI QIAN, WEI-JUN, SAURO, HERBERT M. · 2019 to 2023
$3.1M
Integrated risk assessment and molecular characterization of pulmonary response to e-cigarette exposureR01HL139335 · NHLBI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI MIKHEEV, VLADIMIR B, QIAN, WEI-JUN · 2018 to 2021
$2.4M
NCI NIH HHS U01 CA227544NHLBI NIH HHS R01 HL139335NIDDK NIH HHS R01 DK122160
6 · The paper itself

Abstract

Redox post-translational modifications on cysteine thiols (redox PTMs) have profound effects on protein structure and function, thus enabling regulation of various biological processes. Redox proteomics approaches aim to characterize the landscape of redox PTMs at the systems level. These approaches facilitate studies of condition-specific, dynamic processes implicating redox PTMs and have furthered our understanding of redox signaling and regulation. Mass spectrometry (MS) is a powerful tool for such analyses which has been demonstrated by significant advances in redox proteomics during the last decade. A group of well-established approaches involves the initial blocking of free thiols followed by selective reduction of oxidized PTMs and subsequent enrichment for downstream detection. Alternatively, novel chemoselective probe-based approaches have been developed for various redox PTMs. Direct detection of redox PTMs without any enrichment has also been demonstrated given the sensitivity of contemporary MS instruments. This review discusses the general principles behind different analytical strategies and covers recent advances in redox proteomics. Several applications of redox proteomics are also highlighted to illustrate how large-scale redox proteomics data can lead to novel biological insights.

Indexed as

ProteomicsSulfhydryl CompoundsOxidation-ReductionProtein Processing, Post-TranslationalProteinsProteomeProteinsProteomeSulfhydryl Compoundscysteinepost-translational modificationsprotein thiolsredox proteomicsredox PTMsthiol redox proteome

Identifiers

PMID37248656
PMCPMC10764013
OpenAlexW4378745775

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.