Evidence map›Paper›PMID 40879984›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Enrichment Workflow for Pyrophosphoproteome Analysis.

Sarah Lampe, Dorothea Fiedler

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Sarah LampeLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Dorothea FiedlerLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, Germany. Fiedler@fmp-berlin.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteome-wide detection of different posttranslational modifications (PTMs) still poses a notable analytical challenge. Nevertheless, the identification of protein pyrophosphorylation sites using mass spectrometry (MS) was reported recently. The implementation of an enrichment workflow proved to be key to characterize this substoichiometric modification within complex cell lysate samples. Analysis of the enriched samples using data-dependent neutral-loss triggered electron transfer/higher-energy collision dissociation (DDNL EThcD) MS enabled the detection of endogenous protein pyrophosphorylation. In this chapter, the bottom-up pyrophosphoproteomics analysis, including an enrichment workflow, to identify protein pyrophosphorylation sites is described.

Indexed as

Protein Processing, Post-TranslationalProteomeProteomicsHumansMass SpectrometryTandem Mass SpectrometryWorkflowProteomeBottom-up proteomicsEnrichmentEThcDFractionationLambda protein phosphataseMass spectrometry sample preparationPosttranslational modificationPyrophosphorylationSIMAC

Identifiers

What OpenQuestion holds

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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.