Evidence map›Paper›PMID 16415788›Full record

ArticleEMBO reports2006

Tudor, MBT and chromo domains gauge the degree of lysine methylation.

Jeesun Kim, Jeremy Daniel, Alexsandra Espejo, Aimee Lake, Murli Krishna, Li Xia, Yi Zhang, Mark T Bedford

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 260 papers.

0numbers the graph read from it
0cells of the map it votes in
260citing papers in PubMed
21.5field-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

260 citing papers in PubMed, 485 citations in OpenAlex.

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  16. Epigenetic Causes of Overgrowth Syndromes.The Journal of clinical endocrinology and metabolism · 2024
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200 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

8 authors at 3 institutions in 1 country.

Jeesun KimThe University of Texas MD Anderson Cancer Center, Science Park-Research Division, Smithville, 78957, USA.
Jeremy Daniel
Alexsandra Espejo
Aimee Lake
Murli Krishna
Li Xia
Yi Zhang
Mark T Bedford
The University of Texas MD Anderson Cancer Center · USUniversity of North Carolina at Chapel Hill · USHartford Financial Services (United States)

Funding

Pilot Project ProgramP30ES007784 · NIEHS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI RICHIE, ELLEN R · 1996 to 2011
$16.4M
Mouse Model of Cell Cycle Deregulation in CancerU01ES011047 · NIEHS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI JOHNSON, DAVID G. · 2001 to 2006
$6.8M
The Functional Analysis of the Coactivator CARM1R01DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T. · 2002 to 2015
$4.2M
Mechanisms of Polycomb SilencingR01GM068804 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YI · 2003 to 2010
$2.1M
The Functional Analysis of the Coactivator CARM1R56DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T · 2007 to 2007
$77k
NIDDK NIH HHS DK62248NIDDK NIH HHS R01 DK062248NIDDK NIH HHS R56 DK062248NIEHS NIH HHS ES011047NIEHS NIH HHS ES07784NIEHS NIH HHS P30 ES007784NIEHS NIH HHS U01 ES011047NIGMS NIH HHS GM68804NIGMS NIH HHS R01 GM068804
6 · The paper itself

Abstract

The post-translational modification of histones regulates many cellular processes, including transcription, replication and DNA repair. A large number of combinations of post-translational modifications are possible. This cipher is referred to as the histone code. Many of the enzymes that lay down this code have been identified. However, so far, few code-reading proteins have been identified. Here, we describe a protein-array approach for identifying methyl-specific interacting proteins. We found that not only chromo domains but also tudor and MBT domains bind to methylated peptides from the amino-terminal tails of histones H3 and H4. Binding specificity observed on the protein-domain microarray was corroborated using peptide pull-downs, surface plasma resonance and far western blotting. Thus, our studies expose tudor and MBT domains as new classes of methyl-lysine-binding protein modules, and also demonstrates that protein-domain microarrays are powerful tools for the identification of new domain types that recognize histone modifications.

Indexed as

HistonesLysineMethylationProtein Array AnalysisProtein BindingProtein Structure, TertiaryHistonesLysine

Identifiers

PMID16415788
PMCPMC1456902
OpenAlexW2121356384

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.