Evidence map›Paper›PMID 35868236›Full record

ArticleCell chemical biology2022

Native chemical ligation approach to sensitively probe tissue acyl-CoA pools.

Andrew M James, Abigail A I Norman, Jack W Houghton, Hiran A Prag, Angela Logan, Robin Antrobus, Richard C Hartley, Michael P Murphy

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell chemical biology, 2022. 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
0.5field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  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

8 authors at 2 institutions in 1 country.

Andrew M JamesMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: aj@mrc-mbu.cam.ac.uk.
Abigail A I NormanSchool of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, UK.
Jack W HoughtonCambridge Institute of Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Hiran A PragMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Angela LoganMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Robin AntrobusCambridge Institute of Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.
Richard C HartleySchool of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, UK.
Michael P MurphyMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: mpm@mrc-mbu.cam.ac.uk.
University of Cambridge · GBUniversity of Glasgow · GB

Funding

Medical Research Council MC_UU_00015/3Wellcome Trust 110158/Z/15/ZWellcome Trust 220257/Z/20/Z
6 · The paper itself

Abstract

During metabolism, carboxylic acids are often activated by conjugation to the thiol of coenzyme A (CoA). The resulting acyl-CoAs comprise a group of ∼100 thioester-containing metabolites that could modify protein behavior through non-enzymatic N-acylation of lysine residues. However, the importance of many potential acyl modifications remains unclear because antibody-based methods to detect them are unavailable and the in vivo concentrations of their respective acyl-CoAs are poorly characterized. Here, we develop cysteine-triphenylphosphonium (CysTPP), a mass spectrometry probe that uses "native chemical ligation" to sensitively detect the major acyl-CoAs present in vivo through irreversible modification of its amine via a thioester intermediate. Using CysTPP, we show that longer-chain (C13-C22) acyl-CoAs often constitute ∼60% of the acyl-CoA pool in rat tissues. These hydrophobic longer-chain fatty acyl-CoAs have the potential to non-enzymatically modify protein residues.

Indexed as

Acyl Coenzyme ACoenzyme AAcylationAnimalsCysteineMass SpectrometryProteinsRatsAcyl Coenzyme ACoenzyme ACysteineProteinsacylationacyl-CoAcoenzyme Acysteinenative chemical ligationthioesterthioltriphenylphosphonium

Identifiers

PMID35868236
PMCPMC9586882
OpenAlexW4286512541

What OpenQuestion holds

Textmetadata
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.