Evidence map›Paper›PMID 35776679›Full record

ArticleChembiochem : a European journal of chemical biology2022

Investigating Peptide-Coenzyme A Conjugates as Chemical Probes for Proteomic Profiling of N-Terminal and Lysine Acetyltransferases.

Julia Sindlinger, Stefan Schön, Jürgen Eirich, Sören Kirchgäßner, Iris Finkemeier, Dirk Schwarzer

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

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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 at 2 institutions in 1 country.

Julia SindlingerInterfaculty Institute of Biochemistry (IFIB), University of Tübingen, Auf der Morgenstelle 34, 72076, Tübingen, Germany.ORCID 0000-0002-7265-8093
Stefan SchönInterfaculty Institute of Biochemistry (IFIB), University of Tübingen, Auf der Morgenstelle 34, 72076, Tübingen, Germany.
Jürgen EirichInstitute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 7, 48149, Münster, Germany.ORCID 0000-0003-0963-1872
Sören KirchgäßnerInterfaculty Institute of Biochemistry (IFIB), University of Tübingen, Auf der Morgenstelle 34, 72076, Tübingen, Germany.ORCID 0000-0003-3445-3123
Iris FinkemeierInstitute of Plant Biology and Biotechnology, University of Münster, Schlossplatz 7, 48149, Münster, Germany.ORCID 0000-0002-8972-4026
Dirk SchwarzerInterfaculty Institute of Biochemistry (IFIB), University of Tübingen, Auf der Morgenstelle 34, 72076, Tübingen, Germany.ORCID 0000-0002-7477-3319
University of Tübingen · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetyl groups are transferred from acetyl-coenzyme A (Ac-CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA conjugates as KAT probes, we have synthesized peptide probes with CoA conjugated to N-terminal alanine (α-Ala-CoA), proline (α-Pro-CoA) or tri-glutamic acid (α-3Glu-CoA) units for interactome profiling of NAT complexes. The α-Ala-CoA probe enriched the majority of NAT catalytic and auxiliary subunits, while a lysine CoA-conjugate bound only a subset of endogenous KATs. Interactome profiling with the α-Pro-CoA probe showed reduced NAT recruitment in favor of metabolic CoA binding proteins and α-3Glu-CoA steered the interactome towards NAA80 and NatB. These findings agreed with the inherent substrate specificities of the target proteins and showed that N-terminal CoA-conjugated peptides are versatile probes for NAT complex profiling in lysates of physiological and pathological backgrounds.

Indexed as

Lysine AcetyltransferasesAcetylationAcetyltransferasesCoenzyme ALysinePeptidesProteomicsAcetyltransferasesCoenzyme ALysineLysine AcetyltransferasesPeptidesacetylationchemoproteomicscoenzyme Alysine acetyltransferaseN-terminal acetyltransferase

Identifiers

PMID35776679
PMCPMC9541820
OpenAlexW4283768038

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.