Evidence map›Paper›PMID 40371726›Full record

ArticleProtein science : a publication of the Protein Society2025

Extrinsic and intrinsic factors affect copper-induced protein precipitation across eukaryotic and prokaryotic proteomes.

Grace R Sturrock, Amy T R Robison, Azim Dharani, Eric E Monson, Katherine J Franz, Michael C Fitzgerald

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 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. Article
  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

6 authors.

Grace R SturrockDepartment of Chemistry, Duke University, Durham, North Carolina, USA.
Amy T R RobisonDepartment of Chemistry, Duke University, Durham, North Carolina, USA.
Azim DharaniDepartment of Chemistry, Duke University, Durham, North Carolina, USA.
Eric E MonsonCenter for Data and Visualization Sciences, Duke University, Durham, North Carolina, USA.
Katherine J FranzDepartment of Chemistry, Duke University, Durham, North Carolina, USA.ORCID 0000-0002-9015-0998
Michael C FitzgeraldDepartment of Chemistry, Duke University, Durham, North Carolina, USA.

Funding

Elucidating the Molecular Basis of Cellular Metal Stress by using Mass Spectrometry-Based Proteomic MethodsR01GM145035 · NIGMS · DUKE UNIVERSITY · PI FITZGERALD, MICHAEL C, FRANZ, KATHERINE J. · 2022 to 2025
$2.1M
NIGMS NIH HHS R01 GM145035NIH HHS R01-GM145035North Carolina Biotechnology Center 2014-IDG-1017
6 · The paper itself

Abstract

The susceptibility of a protein to aggregation upon exposure to copper ions (Cu) has been recognized as a contributor to Cu-induced cellular dysfunction and toxicity. Different cell types succumb to Cu to varying degrees, indicating innate differences between species in the mechanisms used to tolerate exposure to Cu in excess of their biological needs. Investigated here are properties associated with metal-induced protein precipitation (MiPP) compared across cell lysates generated from three cell lines from three different species: Escherichia coli, Candida albicans, and the human prostate cancer cell line 22Rv1. The human cell line was the most sensitive to Cu-induced protein precipitation, while C. albicans was the most tolerant. This trend aligns with the relative susceptibilities of these cells to Cu-induced cytotoxicity. The unique susceptibilities of these proteomes to precipitation by Cu were examined to identify factors that influence a protein's relative sensitivity to this effect. Identified were intrinsic factors such as frequency and solvent accessibility of known metal-binding amino acids, as well as external factors related to the molecular composition of their native cell lysates. Overall, our findings help to elucidate the biomolecular basis underpinning the unique capacity of adventitious Cu to have differential effects on eukaryotic and prokaryotic organisms and the level of Cu needed to induce protein precipitation.

Indexed as

Candida albicansCopperEscherichia coliProteomeCell Line, TumorChemical PrecipitationHumansCopperProteomecoppercopperomecuproptosislabile metal poolprotein aggregationprotein misfolding

Identifiers

PMID40371726
PMCPMC12079486

What OpenQuestion holds

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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.