Evidence map›Paper›PMID 29848782›Full record

ArticleMolecular & cellular proteomics : MCP2018

ProteomeTools: Systematic Characterization of 21 Post-translational Protein Modifications by Liquid Chromatography Tandem Mass Spectrometry (LC-MS/MS) Using Synthetic Peptides.

Daniel Paul Zolg, Mathias Wilhelm, Tobias Schmidt, Guillaume Médard, Johannes Zerweck, Tobias Knaute, Holger Wenschuh, Ulf Reimer, Karsten Schnatbaum, Bernhard Kuster

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
7.3field-weighted citation impact, top 1% 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

52 citing papers in PubMed, 133 citations in OpenAlex.

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  10. Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome.Journal of cardiovascular development and disease · 2026
    Review
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  18. Ethylene Signaling in Plant Development and Stress Adaptation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
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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

10 authors at 3 institutions in 1 country.

Daniel Paul ZolgFrom the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Mathias WilhelmFrom the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.ORCID 0000-0002-9224-3258
Tobias SchmidtFrom the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Guillaume MédardFrom the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Johannes Zerweck§JPT Peptide Technologies GmbH, Berlin, Germany.
Tobias Knaute§JPT Peptide Technologies GmbH, Berlin, Germany.
Holger Wenschuh§JPT Peptide Technologies GmbH, Berlin, Germany.
Ulf ReimerFrom the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Karsten Schnatbaum§JPT Peptide Technologies GmbH, Berlin, Germany.
Bernhard KusterFrom the ‡Chair of Proteomics and Bioanalytics, Technical University of Munich, Freising, Germany; kuster@tum.de.
Technical University of Munich · DEJPT Peptide Technologies (Germany) · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The analysis of the post-translational modification (PTM) state of proteins using mass spectrometry-based bottom-up proteomic workflows has evolved into a powerful tool for the study of cellular regulatory events that are not directly encoded at the genome level. Besides frequently detected modifications such as phosphorylation, acetylation and ubiquitination, many low abundant or less frequently detected PTMs are known or postulated to serve important regulatory functions. To more broadly understand the LC-MS/MS characteristics of PTMs, we synthesized and analyzed ∼5,000 peptides representing 21 different naturally occurring modifications of lysine, arginine, proline and tyrosine side chains and their unmodified counterparts. The analysis identified changes in retention times, shifts of precursor charge states and differences in search engine scores between modifications. PTM-dependent changes in the fragmentation behavior were evaluated using eleven different fragmentation modes or collision energies. We also systematically investigated the formation of diagnostic ions or neutral losses for all PTMs, confirming 10 known and identifying 5 novel diagnostic ions for lysine modifications. To demonstrate the value of including diagnostic ions in database searching, we reprocessed a public data set of lysine crotonylation and showed that considering the diagnostic ions increases confidence in the identification of the modified peptides. To our knowledge, this constitutes the first broad and systematic analysis of the LC-MS/MS properties of common and rare PTMs using synthetic peptides, leading to direct applicable utility for bottom-up proteomic experiments.

Indexed as

Protein Processing, Post-TranslationalChromatography, LiquidChromatography, Reverse-PhaseDatabases, ProteinIonsPeptidesProteomeTandem Mass SpectrometryIonsPeptidesProteome

Identifiers

PMID29848782
PMCPMC6126394
OpenAlexW2807369168

What OpenQuestion holds

Textmetadata
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.