Evidence map›Paper›PMID 37353133›Full record

ReviewBiochimica et biophysica acta. Proteins and proteomics2023

The Fe and Zn cofactor dilemma.

Jiahua Chen, Logan A Calderone, Luying Pan, Trent Quist, Maria-Eirini Pandelia

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Proteins and proteomics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Journal of the American Chemical Society · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Iron: Life's primeval transition metal.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. 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

5 authors at 1 institution in 1 country.

Jiahua ChenDepartment of Biochemistry, Brandeis University, Waltham, MA 02453, USA.
Logan A CalderoneDepartment of Biochemistry, Brandeis University, Waltham, MA 02453, USA.
Luying PanDepartment of Biochemistry, Brandeis University, Waltham, MA 02453, USA.
Trent QuistDepartment of Biochemistry, Brandeis University, Waltham, MA 02453, USA.
Maria-Eirini PandeliaDepartment of Biochemistry, Brandeis University, Waltham, MA 02453, USA. Electronic address: mepandelia@brandeis.edu.
Brandeis University · US

Funding

Macromolecular Structure, Dynamics, and MechanismT32GM135126 · NIGMS · BRANDEIS UNIVERSITY · PI JEFF GELLES, Douglas Lowell Theobald · 2020 to 2026
$2.1M
How does a metallofactor in Hepatitis B viral protein X orchestrate pathogenesis and liver cancerR01GM126303 · NIGMS · BRANDEIS UNIVERSITY · PI PANDELIA, MARIA-EIRINI · 2019 to 2023
$1.8M
Functional diversification of the HD-superfamily; the Hydrolase/Oxygenase DilemmaR00GM111978 · NIGMS · BRANDEIS UNIVERSITY · PI PANDELIA, MARIA-EIRINI · 2016 to 2018
$740k
Functional diversification of the HD-superfamily; the Hydrolase/Oxygenase DilemmaK99GM111978 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI PANDELIA, MARIA-EIRINI · 2014 to 2015
$107k
NIGMS NIH HHS K99 GM111978NIGMS NIH HHS R00 GM111978NIGMS NIH HHS R01 GM126303NIGMS NIH HHS T32 GM135126
6 · The paper itself

Abstract

Fe and Zn ions are essential enzymatic cofactors across all domains of life. Fe is an electron donor/acceptor in redox enzymes, while Zn is typically a structural element or catalytic component in hydrolases. Interestingly, the presence of Zn in oxidoreductases and Fe in hydrolases challenge this apparent functional dichotomy. In hydrolases, Fe either substitutes for Zn or specifically catalyzes certain reactions. On the other hand, Zn can replace divalent Fe and substitute for more complex Fe assemblies, known as Fe-S clusters. Although many zinc-binding proteins interchangeably harbor Zn and Fe-S clusters, these cofactors are only sometimes functional proxies.

Indexed as

CoenzymesOxidoreductasesHydrolasesOxidation-ReductionZincCoenzymesHydrolasesOxidoreductasesZincFe-S clustersHydrolasesViral proteinsZinc-finger proteins

Identifiers

PMID37353133
PMCPMC12533603
OpenAlexW4381514048

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.