Evidence map›Paper›PMID 23583077›Full record

ArticleMolecular cell2013

A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.

Kaitlyn E Moore, Scott M Carlson, Nathan D Camp, Peggie Cheung, Richard G James, Katrin F Chua, Alejandro Wolf-Yadlin, Or Gozani

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
10.9field-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

89 citing papers in PubMed, 162 citations in OpenAlex.

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  16. Deciphering the PTM codes of the tumor suppressor p53.Journal of molecular cell biology · 2022
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29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Kaitlyn E MooreDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Scott M Carlson
Nathan D Camp
Peggie Cheung
Richard G James
Katrin F Chua
Alejandro Wolf-Yadlin
Or Gozani
Stanford University · USUniversity of Washington · USGeriatric Research Education and Clinical Center · US

Funding

Leveraging innovative technologies in basic and clinical cancer researchT32CA009302 · NCI · STANFORD UNIVERSITY · PI LAURA D ATTARDI, Aaron M Newman · 1985 to 2026
$19.1M
Function of PHD Domain Proteins in Chromatin RegulationR01GM079641 · NIGMS · STANFORD UNIVERSITY · PI GOZANI, OR P. · 2007 to 2020
$4.5M
Molecular Mechanisms of Mammalian SIRT6 FunctionR01AG028867 · NIA · STANFORD UNIVERSITY · PI CHUA, KATRIN F · 2006 to 2010
$1.6M
In vivo role of BTK-mediated inhibition of Wnt/b-catenin signaling during hematopR00HL103768 · NHLBI · SEATTLE CHILDREN'S HOSPITAL · PI JAMES, RICHARD GOFF · 2012 to 2014
$717k
LTQ Orbitrap XL ETD Mass SpectrometerS10RR027425 · NCRR · STANFORD UNIVERSITY · PI WANDLESS, THOMAS JAMES · 2010 to 2010
$500k
NCI NIH HHS 5T32 CA09302-35NCI NIH HHS T32 CA009302NCRR NIH HHS S10 RR027425NCRR NIH HHS S10RR027425NHLBI NIH HHS 4R00HL103768NHLBI NIH HHS R00 HL103768NIA NIH HHS R01 AG028867NIGMS NIH HHS R01 GM079641
6 · The paper itself

Abstract

Lysine methylation of histone proteins regulates chromatin dynamics and plays important roles in diverse physiological and pathological processes. However, beyond histone proteins, the proteome-wide extent of lysine methylation remains largely unknown. We have engineered the naturally occurring MBT domain repeats of L3MBTL1 to serve as a universal affinity reagent for detecting, enriching, and identifying proteins carrying a mono- or dimethylated lysine. The domain is broadly specific for methylated lysine ("pan-specific") and can be applied to any biological system. We have used our approach to demonstrate that SIRT1 is a substrate of the methyltransferase G9a both in vitro and in cells, to perform proteome-wide detection and enrichment of methylated proteins, and to identify candidate in-cell substrates of G9a and the related methyltransferase GLP. Together, our results demonstrate a powerful new approach for global and quantitative analysis of methylated lysine, and they represent the first systems biology understanding of lysine methylation.

Indexed as

AnimalsCell LineHEK293 CellsHumansInsectaLysineMethylationProtein Structure, TertiaryProteomeProteomicsSf9 CellsSirtuin 1LysineProteomeSIRT1 protein, humanSirtuin 1

Identifiers

PMID23583077
PMCPMC3660009
OpenAlexW2047552911

What OpenQuestion holds

Textmetadata
LicenceTDM
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.