Evidence map›Paper›PMID 38925478›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2024

Proteomic strategies to interrogate the Fe-S proteome.

Daniel W Bak, Eranthie Weerapana

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Review
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

2 authors.

Daniel W BakDepartment of Chemistry, Boston College, Chestnut Hill, MA, United States of America. Electronic address: bakd@bc.edu.
Eranthie WeerapanaDepartment of Chemistry, Boston College, Chestnut Hill, MA, United States of America. Electronic address: eranthie@bc.edu.

Funding

Developing chemical-proteomic tools to investigate cysteine oxidationR35GM134964 · NIGMS · BOSTON COLLEGE · PI WEERAPANA, ERANTHIE · 2020 to 2024
$3.1M
NIGMS NIH HHS R35 GM134964
6 · The paper itself

Abstract

Iron‑sulfur (Fe-S) clusters, inorganic cofactors composed of iron and sulfide, participate in numerous essential redox, non-redox, structural, and regulatory biological processes within the cell. Though structurally and functionally diverse, the list of all proteins in an organism capable of binding one or more Fe-S clusters is referred to as its Fe-S proteome. Importantly, the Fe-S proteome is highly dynamic, with continuous cluster synthesis and delivery by complex Fe-S cluster biogenesis pathways. This cluster delivery is balanced out by processes that can result in loss of Fe-S cluster binding, such as redox state changes, iron availability, and oxygen sensitivity. Despite continued expansion of the Fe-S protein catalogue, it remains a challenge to reliably identify novel Fe-S proteins. As such, high-throughput techniques that can report on native Fe-S cluster binding are required to both identify new Fe-S proteins, as well as characterize the in vivo dynamics of Fe-S cluster binding. Due to the recent rapid growth in mass spectrometry, proteomics, and chemical biology, there has been a host of techniques developed that are applicable to the study of native Fe-S proteins. This review will detail both the current understanding of the Fe-S proteome and Fe-S cluster biology as well as describing state-of-the-art proteomic strategies for the study of Fe-S clusters within the context of a native proteome.

Indexed as

Iron-Sulfur ProteinsProteomeProteomicsHumansIronMass SpectrometryOxidation-ReductionIronIron-Sulfur ProteinsProteomeActivity-based protein profilingAutoradiographyInductively-coupled plasmaIron‑sulfurMass spectrometryNative MSProteomeProteomicsThermal protein profiling

Identifiers

PMID38925478
PMCPMC11365765

What OpenQuestion holds

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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.