Evidence map›Paper›PMID 24129315›Full record

ArticleMolecular & cellular proteomics : MCP2014

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

Ailan Guo, Hongbo Gu, Jing Zhou, Daniel Mulhern, Yi Wang, Kimberly A Lee, Vicky Yang, Mike Aguiar, Jon Kornhauser, Xiaoying Jia and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed
16.4field-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

246 citing papers in PubMed, 469 citations in OpenAlex.

  1. Review
  2. Review
  3. SMARCD1 and Its Functional Relevance in SWI/SNF and Cancer.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. LC-MS profiling ofbioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Review
  11. An NMR-Based Approach for Global Arginine Methylation Analysis.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. DynamicJournal of the American Chemical Society · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Review

186 more citing papers are in PubMed but not listed here.

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

16 authors at 2 institutions in 1 country.

Ailan GuoCell Signaling Technology Inc., 3 Trask Lane, Danvers, Massachusetts 01923;
Hongbo Gu
Jing Zhou
Daniel Mulhern
Yi Wang
Kimberly A Lee
Vicky Yang
Mike Aguiar
Jon Kornhauser
Xiaoying Jia
Jianmin Ren
Sean A Beausoleil
Jeffrey C Silva
Vidyasiri Vemulapalli
Mark T Bedford
Michael J Comb
Cell Signaling Technology (United States) · USThe University of Texas MD Anderson Cancer Center · US

Funding

The Functional Analysis of the Coactivator CARM1R01DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T. · 2002 to 2015
$4.2M
NIDDK NIH HHS R01 DK062248
6 · The paper itself

Abstract

Protein methylation is a common posttranslational modification that mostly occurs on arginine and lysine residues. Arginine methylation has been reported to regulate RNA processing, gene transcription, DNA damage repair, protein translocation, and signal transduction. Lysine methylation is best known to regulate histone function and is involved in epigenetic regulation of gene transcription. To better study protein methylation, we have developed highly specific antibodies against monomethyl arginine; asymmetric dimethyl arginine; and monomethyl, dimethyl, and trimethyl lysine motifs. These antibodies were used to perform immunoaffinity purification of methyl peptides followed by LC-MS/MS analysis to identify and quantify arginine and lysine methylation sites in several model studies. Overall, we identified over 1000 arginine methylation sites in human cell line and mouse tissues, and ∼160 lysine methylation sites in human cell line HCT116. The number of methylation sites identified in this study exceeds those found in the literature to date. Detailed analysis of arginine-methylated proteins observed in mouse brain compared with those found in mouse embryo shows a tissue-specific distribution of arginine methylation, and extends the types of proteins that are known to be arginine methylated to include many new protein types. Many arginine-methylated proteins that we identified from the brain, including receptors, ion channels, transporters, and vesicle proteins, are involved in synaptic transmission, whereas the most abundant methylated proteins identified from mouse embryo are transcriptional regulators and RNA processing proteins.

Indexed as

Protein Processing, Post-TranslationalAmino Acid MotifsAnimalsArginineBrainChromatography, LiquidHCT116 CellsHumansLysineMethylationMiceTandem Mass SpectrometryArginineLysine

Identifiers

PMID24129315
PMCPMC3879628
OpenAlexW2151026975

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.