Evidence map›Paper›PMID 21288002›Full record

ReviewBiochemistry2011

Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription.

Kyoko L Yap, Ming-Ming Zhou

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 4% 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

68 citing papers in PubMed, 1 synthesis or guideline pooled it, 116 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026
    Review
  4. Review
  5. Article
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  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Multimodal interactions drive chromatin phase separation and compaction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Review
  15. Dominant-negative variants in CBX1 cause a neurodevelopmental disorder.Genetics in medicine : official journal of the American College of Medical Genetics · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

8 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

2 authors at 1 institution in 1 country.

Kyoko L YapDepartment of Structural and Chemical Biology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1677, New York, New York 10065, United States.
Ming-Ming Zhou
Icahn School of Medicine at Mount Sinai · US

Funding

PW1--A mediator of cell survival by NFKB and cell death by p53P01CA080058 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI AARONSON, STUART A · 2000 to 2016
$20.2M
Chemical Genomics Paradigm for Epigentic RegulationR01HG004508 · NHGRI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI ZHOU, MING-MING · 2008 to 2014
$6.7M
STRUCTURE OF PROTEIN MODULES IN CHROMATIN REMODELINGR01CA087658 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI ZHOU, MING-MING · 2000 to 2016
$4.8M
A Novel Epigenetic Gene Silencing TechnologyRC1DA028776 · NIDA · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI WALSH, MARTIN JOHN, ZHOU, MING-MING · 2009 to 2010
$977k
NCI NIH HHS CA80058-11NCI NIH HHS CA87658-10NCI NIH HHS P01 CA080058NCI NIH HHS R01 CA087658NHGRI NIH HHS R01 HG004508NIDA NIH HHS DA028776-01NIDA NIH HHS RC1 DA028776
6 · The paper itself

Abstract

Histone methylation recognition is accomplished by a number of evolutionarily conserved protein domains, including those belonging to the methylated lysine-binding Royal family of structural folds. One well-known member of the Royal family, the chromodomain, is found in the HP1/chromobox and CHD subfamilies of proteins, in addition to a small number of other proteins that are involved in chromatin remodeling and gene transcriptional silencing. Here we discuss the structure and function of the chromodomain within these proteins as methylated histone lysine binders and how the functions of these chromodomains can be modulated by additional post-translational modifications or binding to nucleic acids.

Indexed as

Transcription, GeneticAmino Acid SequenceAnimalsChromatinChromatin Assembly and DisassemblyHumansLysineMethylationMolecular Sequence DataProtein Structure, TertiaryChromatinLysine

Identifiers

PMID21288002
PMCPMC3062707
OpenAlexW1992720699

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.