Evidence map›Paper›PMID 28341808›Full record

ArticleThe Biochemical journal2017

Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells.

Yugo Tsuchiya, Sew Yeu Peak-Chew, Clare Newell, Sheritta Miller-Aidoo, Sriyash Mangal, Alexander Zhyvoloup, Jovana Bakovic, Oksana Malanchuk, Gonçalo C Pereira, Vassilios Kotiadis and 10 more

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 94 citations in OpenAlex.

  1. Type III intermediate filaments as novel CoAlation targets.Redox report : communications in free radical research · 2026
    Article
  2. Review
  3. DietaryFood science & nutrition · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Deacetylation of SOD3 by sirtuins restores furin cleavage.Redox biochemistry and chemistry · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Investigating the Regulation of Ribosomal Protein S6 Kinase 1 by CoAlation.International journal of molecular sciences · 2024
    Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors at 3 institutions in 2 countries.

Yugo TsuchiyaDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K.
Sew Yeu Peak-ChewBiological Mass Spectrometry & Proteomics Cell Biology, MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, U.K.
Clare NewellDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K.
Sheritta Miller-AidooDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K.
Sriyash MangalDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K.
Alexander ZhyvoloupDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K.
Jovana BakovicDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K.
Oksana MalanchukInstitute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv 03680, Ukraine.
Gonçalo C PereiraDepartment of Cell and Developmental Biology, University College London, London WC1E 6BT, U.K.
Vassilios KotiadisDepartment of Cell and Developmental Biology, University College London, London WC1E 6BT, U.K.
Gyorgy SzabadkaiDepartment of Cell and Developmental Biology, University College London, London WC1E 6BT, U.K.
Michael R DuchenDepartment of Cell and Developmental Biology, University College London, London WC1E 6BT, U.K.
Mark CampbellWellcome Trust-MRC Institute of Metabolic Science and MRC Metabolic Diseases Unit, Addenbrooke's Hospital, Cambridge CB2 OQQ, U.K.
Sergio Rodriguez CuencaWellcome Trust-MRC Institute of Metabolic Science and MRC Metabolic Diseases Unit, Addenbrooke's Hospital, Cambridge CB2 OQQ, U.K.
Antonio Vidal-PuigWellcome Trust-MRC Institute of Metabolic Science and MRC Metabolic Diseases Unit, Addenbrooke's Hospital, Cambridge CB2 OQQ, U.K.
Andrew M JamesMRC Mitochondrial Biology Unit, Wellcome Trust, MRC Building, University of Cambridge, Cambridge CB2 0XY, U.K.
Michael P MurphyMRC Mitochondrial Biology Unit, Wellcome Trust, MRC Building, University of Cambridge, Cambridge CB2 0XY, U.K.
Valeriy FilonenkoInstitute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv 03680, Ukraine.
Mark SkehelBiological Mass Spectrometry & Proteomics Cell Biology, MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, U.K.
Ivan GoutDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, U.K. i.gout@ucl.ac.uk.
National Academy of Sciences of Ukraine · UAInstitute of Molecular Biology and Genetics · UALudwig-Maximilians-Universität München · DE

Funding

Biotechnology and Biological Sciences Research Council BB/H002731/1Biotechnology and Biological Sciences Research Council BB/L010410/1Biotechnology and Biological Sciences Research Council BB/L020874/1British Heart Foundation RG/12/13/29853Medical Research Council 4050281695Medical Research Council MC_EX_MR/K015680/1Medical Research Council MC_U105178788Medical Research Council MC_U105663142Medical Research Council MC_UU_12012/2Medical Research Council MC_UU_12012/5Medical Research Council MRC_MC_UU_12012/2Medical Research Council MRC_MC_UU_12012/5Wellcome Trust 100574/Z/12/ZWellcome Trust 110158/Z/15/ZWellcome Trust 110159/Z/15/Z
6 · The paper itself

Abstract

Coenzyme A (CoA) is an obligatory cofactor in all branches of life. CoA and its derivatives are involved in major metabolic pathways, allosteric interactions and the regulation of gene expression. Abnormal biosynthesis and homeostasis of CoA and its derivatives have been associated with various human pathologies, including cancer, diabetes and neurodegeneration. Using an anti-CoA monoclonal antibody and mass spectrometry, we identified a wide range of cellular proteins which are modified by covalent attachment of CoA to cysteine thiols (CoAlation). We show that protein CoAlation is a reversible post-translational modification that is induced in mammalian cells and tissues by oxidising agents and metabolic stress. Many key cellular enzymes were found to be CoAlated

Indexed as

AnimalsCoenzyme ACysteineHEK293 CellsHep G2 CellsHumansKidneyLiverMaleMyocardiumOrgan SpecificityOxidation-ReductionOxidative StressProtein Processing, Post-TranslationalProteinsRabbitsCoenzyme ACysteineProteinsSulfhydryl Compoundscoenzyme Ametabolic and oxidative stresspost-translational modificationproteomics

Identifiers

PMID28341808
PMCPMC5509381
OpenAlexW2602531789

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.