Evidence map›Paper›PMID 39120068›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024

Multifaceted Proteome Analysis at Solubility, Redox, and Expression Dimensions for Target Identification.

Amir A Saei, Albin Lundin, Hezheng Lyu, Hassan Gharibi, Huqiao Luo, Jaakko Teppo, Xuepei Zhang, Massimiliano Gaetani, Ákos Végvári, Rikard Holmdahl and 2 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Stability-based approaches in chemoproteomics.Expert reviews in molecular medicine · 2024
    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

12 authors.

Amir A SaeiDepartment of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA.
Albin LundinDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Hezheng LyuDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Hassan GharibiDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Huqiao LuoDivision of Immunology, Medical Inflammation Research Group, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, SE-17 177, Sweden.
Jaakko TeppoDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Xuepei ZhangDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Massimiliano GaetaniDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Ákos VégváriDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.
Rikard HolmdahlDivision of Immunology, Medical Inflammation Research Group, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, SE-17 177, Sweden.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA.
Roman A ZubarevDivision of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17 177, Sweden.ORCID 0000-0001-9839-2089

Funding

Alex och Eva Wallströms stiftelse 2023-00415Ambizione Fellowship PZ00P3_216203Cancerfonden 22 1967Cancerfonden 22 2350 Pj 01 HKarolinska Institutet 2022-02035Knut och Alice Wallenbergs Stiftelse 2019.0059Ruth och Richard Julins Stiftelse 2023-00393Svenska Läkaresällskapet SLS-961262Swedish Research Council 2019-01209Swiss National Science Foundation
6 · The paper itself

Abstract

Multifaceted interrogation of the proteome deepens the system-wide understanding of biological systems; however, mapping the redox changes in the proteome has so far been significantly more challenging than expression and solubility/stability analyses. Here, the first high-throughput redox proteomics approach integrated with expression analysis (REX) is devised and combined with the Proteome Integral Solubility Alteration (PISA) assay. The whole PISA-REX experiment with up to four biological replicates can be multiplexed into a single tandem mass tag TMTpro set. For benchmarking this compact tool, HCT116 cells treated with auranofin are analyzed, showing great improvement compared with previous studies. PISA-REX is then applied to study proteome remodeling upon stimulation of human monocytes by interferon α (IFN-α). Applying this tool to study the proteome changes in plasmacytoid dendritic cells (pDCs) isolated from wild-type versus Ncf1-mutant mice treated with interferon α, shows that NCF1 deficiency enhances the STAT1 pathway and modulates the expression, solubility, and redox state of interferon-induced proteins. Providing comprehensive multifaceted information on the proteome, the compact PISA-REX has the potential to become an industry standard in proteomics and to open new windows into the biology of health and disease.

Indexed as

Oxidation-ReductionProteomeProteomicsSolubilityAnimalsDendritic CellsHumansInterferon-alphaMiceInterferon-alphaProteomeauranofinimmunologyinterferonlupusmass spectrometryoxidation and reduction

Identifiers

PMID39120068
PMCPMC11481203

What OpenQuestion holds

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LicenceCC BY
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.