Evidence map›Paper›PMID 25505155›Full record

ArticleMolecular & cellular proteomics : MCP2015

A chemical proteomics approach for global analysis of lysine monomethylome profiling.

Zhixiang Wu, Zhongyi Cheng, Mingwei Sun, Xuelian Wan, Ping Liu, Tieming He, Minjia Tan, Yingming Zhao

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
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  7. Review
  8. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
    Review
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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

8 authors at 2 institutions in 1 country.

Zhixiang WuFrom the ‡The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China;
Zhongyi Cheng§Jingjie PTM BioLab (Hangzhou) Co. Ltd, Hangzhou, P.R. China;
Mingwei SunFrom the ‡The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China;
Xuelian WanFrom the ‡The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China;
Ping LiuFrom the ‡The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China;
Tieming He§Jingjie PTM BioLab (Hangzhou) Co. Ltd, Hangzhou, P.R. China;
Minjia TanFrom the ‡The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China; Yingming.Zhao@uchicago.edu mjtan@simm.ac.cn.
Yingming ZhaoFrom the ‡The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, P.R. China; ¶Ben May Department of Cancer Research, The University of Chicago, Chicago, Illinois Yingming.Zhao@uchicago.edu mjtan@simm.ac.cn.
Chinese Academy of Sciences · CNNew England Biolabs (China) · CN

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
Proteome Characterization Center: A Genoproteomics Pipeline for Cance ResearchU24CA160036 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2011 to 2016
$10.7M
Biochemistry of lysine crotonylation pathwayR01GM105933 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHAO, YINGMING · 2013 to 2016
$1.7M
NCATS NIH HHS UL1 TR000430NCI NIH HHS CA160036NCI NIH HHS U24 CA160036NCRR NIH HHS RR020839NCRR NIH HHS U54 RR020839NIGMS NIH HHS GM105933NIGMS NIH HHS R01 GM105933
6 · The paper itself

Abstract

Methylation of lysine residues on histone proteins is known to play an important role in chromatin structure and function. However, non-histone protein substrates of this modification remain largely unknown. An effective approach for system-wide analysis of protein lysine methylation, particularly lysine monomethylation, is lacking. Here we describe a chemical proteomics approach for global screening for monomethyllysine substrates, involving chemical propionylation of monomethylated lysine, affinity enrichment of the modified monomethylated peptides, and HPLC/MS/MS analysis. Using this approach, we identified with high confidence 446 lysine monomethylation sites in 398 proteins, including three previously unknown histone monomethylation marks, representing the largest data set of protein lysine monomethylation described to date. Our data not only confirms previously discovered lysine methylation substrates in the nucleus and spliceosome, but also reveals new substrates associated with diverse biological processes. This method hence offers a powerful approach for dynamic study of protein lysine monomethylation under diverse cellular conditions and in human diseases.

Indexed as

Amino Acid SequenceAntibodiesCell LineComputational BiologyHumansIsotope LabelingLysineMethylationMolecular Sequence DataPeptidesProteomeProteomicsReproducibility of ResultsAntibodiesLysinePeptidesProteome

Identifiers

PMID25505155
PMCPMC4350029
OpenAlexW2034717128

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.