Evidence map›Paper›PMID 42542519›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2026

An Overview of Mass Spectrometry-Based Methods to Analyze Post-Translational Modifications.

Rui Chen, Xu Zhang, Jianjun Li

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2026. 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

3 authors.

Rui ChenHuman Therapeutics Research Centre, National Research Council Canada, Ottawa, ON, Canada. Rui.Chen@nrc-cnrc.gc.ca.
Xu ZhangBiologic and Radiopharmaceutical Drugs Directorate, Health Products and Food Branch, Health Canada, Ottawa, ON, Canada.
Jianjun LiHuman Therapeutics Research Centre, National Research Council Canada, Ottawa, ON, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications (PTM) are the covalent modifications of proteins after their biosynthesis. PTMs change the structure and functions of proteins, which eventually regulate various biological processes that are closely related to the onset and development of diseases. Hundreds of different forms of PTMs have been discovered so far and mass spectrometry (MS) has become one of the most important tools to analyze PTMs. With the development of new methods in sample preparation, advances in MS instrumentation, and inventions of new bioinformatic tools, MS-based methods can identify most forms of PTMs, precisely locate the site of modification, sensitively and accurately quantify the changes of modification levels from various of biological samples. This chapter will summarize generic procedures to analyze PTMs with MS methods and provide an update with the latest development in sample preparation, MS analysis, and database search that advanced the way for PTM analysis, improving our knowledge of PTMs and understanding of their roles in various diseases.

Indexed as

Mass SpectrometryProtein Processing, Post-TranslationalProteinsProteomicsAnimalsComputational BiologyDatabases, ProteinHumansProteinsBottom-upDatabase searchMass spectrometryPost-translational modificationSample preparationTop-down

Identifiers

PMID42542519

What Socratic 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 Socratic graph.