Evidence map›Paper›PMID 41105763›Full record

ArticleScience advances2025

CysMP reveals metal ion-specific metalloproteomes and copper-regulated PGK1 activity in glycolysis.

Yamei Yuan, Zhiyuan Wang, Chenfang Si, Jianlong Li, Fandong Ren, Yi Yuan, Ziqi Shi, Nana Sun, Xiaonuo Ma, Xingbang Dai and 7 more

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

17 authors.

Yamei YuanInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0009-0002-3758-5279
Zhiyuan WangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0002-3930-0006
Chenfang SiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0002-6604-7464
Jianlong LiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.
Fandong RenInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.
Yi YuanInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.
Ziqi ShiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.
Nana SunThe College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.
Xiaonuo MaInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.
Xingbang DaiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.
Yunxia LiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0001-6377-1281
Yixiao ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0003-1540-4334
Jianping LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0001-7090-2112
Hongbin WangThe College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.
Zhengjiang ZhuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0002-3272-3567
Bing ShanInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0003-4178-3526
Yaoyang ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai 201210, China.ORCID 0000-0001-5363-9834

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal ions are essential in regulating protein functions through interactions with residues such as cysteine, but comprehensive mapping of metal-specific metalloproteomes in mammals remains limited. Here, we introduce CysMP, a cysteine-centered metalloprotein profiling strategy to profile the metalloproteomes of 11 key metal ions. CysMP identified 8895 metal-binding sites across 4150 proteins, enabling quantitative comparisons between different metals and revealing both their binding promiscuity and preferences. Notably, zinc and copper ions exhibit the broadest protein interaction profiles. CysMP uncovers numerous potential metalloproteins. We demonstrate that copper and zinc bind to and inhibit 5'-methylthioadenosine phosphorylase, resulting in the accumulation of 5'-methylthioadenosine. Furthermore, copper binding suppresses phosphoglycerate kinase 1 activity, leading to a down-regulation of glycolysis. Our work not only establishes a valuable resource for a dual-specific metalloproteome database but also paves the way for understanding the molecular insights of metalloprotein functions.

Indexed as

CopperGlycolysisMetalloproteinsMetalsPhosphoglycerate KinaseBinding SitesCysteineHumansIonsProtein BindingProteomeZincCopperCysteineIonsMetalloproteinsMetalsPGK1 protein, humanPhosphoglycerate KinaseProteomeZinc

Identifiers

PMID41105763
PMCPMC12533568

What OpenQuestion holds

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LicenceCC BY-NC
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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.