Evidence map›Paper›PMID 42681361›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Identification of Target Disulfide Bonds Using Mechanism-Based Kinetic Trapping Combined with Differential Cysteine Labeling.

Jinyu Wang, Yaofeng Li, Chao Fang

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. 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
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.

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

3 authors.

Jinyu WangDepartment of Pharmacology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Huazhong University of Science and Technology, Wuhan, Hubei, 430030, China.ORCID http://orcid.org/0000-0002-5081-8850
Yaofeng LiDepartment of Pharmacy, Renmin Hospital of Wuhan University, Wuhan, Hubei, 430060, China.ORCID http://orcid.org/0009-0008-5009-2210
Chao FangDepartment of Pharmacology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Huazhong University of Science and Technology, Wuhan, Hubei, 430030, China. fangc@hust.edu.cn.ORCID http://orcid.org/0000-0003-2524-3730

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation and cleavage of disulfide bonds, tightly controlled processes, are critical to maintain protein structures and functions in many physiological and pathological scenarios. Thiol isomerases catalyze the rearrangement of disulfide bonds and therefore are important in the regulation of protein functions. ERp72, a member in the thiol isomerase family, directly activates integrin Mac-1 by cleaving functional disulfide bonds. Using a mechanism-based kinetic trapping mutant of ERp72, stepwise labeling of cysteines by different alkylating agents allows the identification of specific disulfide bonds targeted by ERp72. The method described here may also be applied to other oxidoreductases to map potential target disulfides.

Indexed as

CysteineDisulfidesAlkylating AgentsAlkylationHumansKineticsStaining and LabelingAlkylating AgentsCysteineDisulfidesCysteine alkylationDifferential labelingDisulfide bondsEndoplasmic reticulum protein 72 (ERp72)Mass spectrometry

Identifiers

PMID42681361

What OpenQuestion holds

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Registered trials

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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.