Evidence map›Paper›PMID 37004988›Full record

ArticleMolecular & cellular proteomics : MCP2023

MSFragger-Labile: A Flexible Method to Improve Labile PTM Analysis in Proteomics.

Daniel A Polasky, Daniel J Geiszler, Fengchao Yu, Kai Li, Guo Ci Teo, Alexey I Nesvizhskii

Open access · goldAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

34 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  8. CLASPP: A unified model for predicting post-translational modifications.bioRxiv : the preprint server for biology · 2026
    Article
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  13. Review
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  19. Quantitative proteome-wide O-glycoproteomics analysis with FragPipe.Analytical and bioanalytical chemistry · 2025
    Article
  20. 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

6 authors at 1 institution in 1 country.

Daniel A PolaskyDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA. Electronic address: dpolasky@umich.edu.
Daniel J GeiszlerDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA.
Fengchao YuDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA.
Kai LiDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA.
Guo Ci TeoDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA.
Alexey I NesvizhskiiDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA; Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA. Electronic address: nesvi@med.umich.edu.
University of Michigan · US

Funding

COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
Michigan Center for Translational Cancer Proteogenomics-Diversity SupplementU24CA271037 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Saravana Mohan Dhanasekaran, Alexey I Nesvizhskii · 2022 to 2026
$4.4M
Proteogenomics of Cancer Training ProgramT32CA140044 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAO, ARVIND, SARTOR, MAUREEN AGNES · 2010 to 2024
$3.9M
Systematic screening for new histone marks and studying their epigenetic functionR01GM135504 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHAO, YINGMING · 2020 to 2023
$2.1M
NCI NIH HHS T32 CA140044NCI NIH HHS U24 CA271037NIGMS NIH HHS R01 GM094231NIGMS NIH HHS R01 GM135504
6 · The paper itself

Abstract

Posttranslational modifications of proteins play essential roles in defining and regulating the functions of the proteins they decorate, making identification of these modifications critical to understanding biology and disease. Methods for enriching and analyzing a wide variety of biological and chemical modifications of proteins have been developed using mass spectrometry-based proteomics, largely relying on traditional database search methods to identify the resulting mass spectra of modified peptides. These database search methods treat modifications as static attachments of a mass to particular position in the peptide sequence, but many modifications undergo fragmentation in tandem mass spectrometry experiments alongside, or instead of, the peptide backbone. While this fragmentation can confound traditional search methods, it also offers unique opportunities for improved searches that incorporate modification-specific fragment ions. Here, we present a new labile mode in the MSFragger search engine that provides the flexibility to tailor modification-centric searches to the fragmentation observed. We show that labile mode can dramatically improve spectrum identification rates of phosphopeptides, RNA-crosslinked peptides, and ADP-ribosylated peptides. Each of these modifications presents distinct fragmentation characteristics, showcasing the flexibility of MSFragger labile mode to improve search for a wide variety of biological and chemical modifications.

Indexed as

Protein Processing, Post-TranslationalProteomicsDatabases, ProteinPhosphopeptidesProteinsTandem Mass SpectrometryPhosphopeptidesProteinsfragmentationlabilemass spectrometryphosphorylationpost-translational modificationproteomicssearch

Identifiers

PMID37004988
PMCPMC10182319
OpenAlexW4362471247

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.