Evidence map›Paper›PMID 39742810›Full record

ArticleCell2025

The human zinc-binding cysteine proteome.

Nils Burger, Melanie J Mittenbühler, Haopeng Xiao, Sanghee Shin, Shelley M Wei, Erik K Henze, Sebastian Schindler, Sepideh Mehravar, David M Wood, Jonathan J Petrocelli and 11 more

Abstract read
In one paragraph

Article in Cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
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  11. Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026
    Review
  12. Article
  13. Review
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  15. Article
  16. A long-term quasi-equivalentBioactive materials · 2025
    Article
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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

21 authors.

Nils BurgerDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Melanie J MittenbühlerDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Haopeng XiaoDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Sanghee ShinDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Shelley M WeiDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.
Erik K HenzeDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Sebastian SchindlerDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.
Sepideh MehravarMedically Associated Science and Technology (MAST) Program, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA.
David M WoodDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Jonathan J PetrocelliDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Yizhi SunDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Hans-Georg SprengerDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Pedro Latorre-MuroDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Amanda L SmythersDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Luiz H M BoziDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Narek DarabedianDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Yingde ZhuDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.
Hyuk-Soo SeoChemical Biology Program, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Sirano Dhe-PaganonChemical Biology Program, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Jianwei CheDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Edward T ChouchaniDepartment of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA. Electronic address: edwardt_chouchani@dfci.harvard.edu.

Funding

PGC1alpha Pathway: Novel Intracellular and Extracellular MediatorsR01DK119117 · NIDDK · DANA-FARBER CANCER INST · PI BRUCE M. SPIEGELMAN · 2019 to 2026
$4.9M
Determining mechanisms of the succinate thermogenesis pathways on UCP1-dependent and UCP1-independent thermogenesisR01DK123095 · NIDDK · DANA-FARBER CANCER INST · PI Edward Thomas Chouchani · 2019 to 2026
$4.2M
Defining the landscape and mechanisms of protein redox regulation during agingR01AG071966 · NIA · DANA-FARBER CANCER INST · PI Edward Thomas Chouchani · 2022 to 2026
$2.9M
Training Program in Cardiovascular ResearchT32HL160522 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI Jennifer E Ho · 2022 to 2026
$2.7M
Cancer Chemical Biology and Metabolism Training ProgramT32CA236754 · NCI · DANA-FARBER CANCER INST · PI Nika N Danial, THOMAS M ROBERTS · 2019 to 2026
$2.6M
Defining the landscape and mechanisms of redox regulation of metabolism during agingR00AG073461 · NIA · STANFORD UNIVERSITY · PI Haopeng Xiao · 2025 to 2026
$497k
The Role of Mitochondrial TNAP in Adaptive ThermogenesisK01DK132455 · NIDDK · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI SUN, YIZHI · 2023 to 2025
$385k
Defining the landscape and mechanisms of protein redox regulation during agingR56AG071966 · NIA · DANA-FARBER CANCER INST · PI CHOUCHANI, EDWARD THOMAS · 2021 to 2021
$344k
Elucidating the Mechanisms of Translational Approaches to Enhance Recovery of Aged MuscleK00AG073493 · NIA · DANA-FARBER CANCER INST · PI Jonathan Joseph Petrocelli · 2023 to 2026
$320k
Defining the landscape and mechanisms of redox regulation of metabolism during agingK99AG073461 · NIA · DANA-FARBER CANCER INST · PI XIAO, HAOPENG · 2022 to 2023
$220k
Mechanisms of mitochondrial-ER communication during dietary and thermal induced stressK99DK133502 · NIDDK · DANA-FARBER CANCER INST · PI LATORRE MURO, PEDRO ANTONIO · 2023 to 2024
$180k
NCI NIH HHS T32 CA236754NHLBI NIH HHS T32 HL160522NIA NIH HHS K00 AG073493NIA NIH HHS K99 AG073461NIA NIH HHS R00 AG073461NIA NIH HHS R01 AG071966NIA NIH HHS R56 AG071966NIDDK NIH HHS K01 DK132455NIDDK NIH HHS K99 DK133502NIDDK NIH HHS R01 DK119117NIDDK NIH HHS R01 DK123095
6 · The paper itself

Abstract

Zinc is an essential micronutrient that regulates a wide range of physiological processes, most often through zinc binding to protein cysteine residues. Despite being critical for modulation of protein function, the cysteine sites in the majority of the human proteome that are subject to zinc binding remain undefined. Here, we develop ZnCPT, a deep and quantitative mapping of the zinc-binding cysteine proteome. We define 6,173 zinc-binding cysteines, uncovering protein families across major domains of biology that are subject to constitutive or inducible zinc binding. ZnCPT enables systematic discovery of zinc-regulated structural, enzymatic, and allosteric functional domains. On this basis, we identify 52 cancer genetic dependencies subject to zinc binding and nominate malignancies sensitive to zinc-induced cytotoxicity. We discover a mechanism of zinc regulation over glutathione reductase (GSR), which drives cell death in GSR-dependent lung cancers. We provide ZnCPT as a resource for understanding mechanisms of zinc regulation of protein function.

Indexed as

CysteineProteomeZincGlutathione ReductaseHumansLung NeoplasmsProtein BindingCysteineGlutathione ReductaseProteomeZinccancercysteine proteomicsglutathione reductaseGSRzinczinc-binding proteome

Identifiers

PMID39742810
PMCPMC12120685

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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.