Evidence map›Paper›PMID 41099621›Full record

ArticleNucleic acids research2026

PMADS: an integrated database of curated and proteomics-inferred associations between protein post-translational modifications and drug sensitivity.

Jie Zheng, Shuting Chen, Yinuo Zhang, Bingyue Zhang, Keying Qiao, Junbo Xu, Yuxiao Fan, Mengying Feng, Zhiyi Feng, Ziyan Wang and 1 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

11 authors.

Jie ZhengResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Shuting ChenResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Yinuo ZhangResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Bingyue ZhangResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Keying QiaoResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Junbo XuResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Yuxiao FanResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Mengying FengResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Zhiyi FengResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Ziyan WangResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.
Haiyun WangResearch Center for Translational Medicine, Shanghai East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China.ORCID 0000-0001-8364-8328

Funding

National Natural Science Foundation of China 31771469National Natural Science Foundation of China 32370702
6 · The paper itself

Abstract

Post-translational modifications (PTMs) are critical regulators of protein stability, localization, and function and have been increasingly implicated in shaping drug responses across diverse diseases. While numerous studies have reported PTM-related mechanisms of drug sensitivity or resistance, no resource has systematically catalogued these associations in disease-specific contexts. Here, we present protein modification and drug sensitivity (PMADS), an integrated database that systematically organizes PTM-drug-disease ternary associations, defined as PTM-centered drug responses in disease context. PMADS catalogues over 4700 curated associations manually extracted from biomedical literature and over 43 800 predicted associations derived from analysis of large-scale proteomics datasets. Together, PMADS covers >6000 proteins, 1000 drugs, 19 types of PTMs, and 300 disease classes. The database emphasizes both upstream regulatory mechanisms, such as drug-induced modulation of PTMs, and downstream effects, such as PTM-mediated changes in drug sensitivity. Each entry includes detailed annotations such as PTM site, effect description, ternary diagram, supporting evidence, confidence score, and cross-references to external databases, including PDB, PhosphoSitePlus, and DrugBank. PMADS features a user-friendly web interface with advanced search, interactive visualizations, and structured data export to support research in pharmacology, functional genomics, and precision medicine. PMADS is freely available at https://pmads-db.org.

Indexed as

Databases, ProteinProtein Processing, Post-TranslationalProteinsProteomicsHumansInternetProteins

Identifiers

PMID41099621
PMCPMC12807662

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LicenceCC BY
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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.