Evidence map›Paper›PMID 22464331›Full record

ArticleCell2012

Histone recognition and large-scale structural analysis of the human bromodomain family.

Panagis Filippakopoulos, Sarah Picaud, Maria Mangos, Tracy Keates, Jean-Philippe Lambert, Dalia Barsyte-Lovejoy, Ildiko Felletar, Rudolf Volkmer, Susanne Müller, Tony Pawson and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 892 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
892citing papers in PubMed, 1 pooled it
41.1field-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

892 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,724 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Structural basis for P-TEFb association with BRD4.bioRxiv : the preprint server for biology · 2026
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832 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

13 authors at 7 institutions in 4 countries.

Panagis FilippakopoulosNuffield Department of Clinical Medicine, Structural Genomics Consortium, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7LD, UK. panagis.filippakopoulos@sgc.ox.ac.uk
Sarah Picaud
Maria Mangos
Tracy Keates
Jean-Philippe Lambert
Dalia Barsyte-Lovejoy
Ildiko Felletar
Rudolf Volkmer
Susanne Müller
Tony Pawson
Anne-Claude Gingras
Cheryl H Arrowsmith
Stefan Knapp
University of Toronto · CAStructural Genomics Consortium · CAUniversity of Oxford · GBCharité - Universitätsmedizin Berlin · DEGeorge Washington University · USLunenfeld-Tanenbaum Research Institute · CAOntario Institute for Cancer Research · CA

Funding

CIHRWellcome Trust 092809Wellcome Trust 095751/Z/11/Z
6 · The paper itself

Abstract

Bromodomains (BRDs) are protein interaction modules that specifically recognize ε-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present 29 high-resolution crystal structures, covering all BRD families. Comprehensive crossfamily structural analysis identifies conserved and family-specific structural features that are necessary for specific acetylation-dependent substrate recognition. Screening of more than 30 representative BRDs against systematic histone-peptide arrays identifies new BRD substrates and reveals a strong influence of flanking posttranslational modifications, such as acetylation and phosphorylation, suggesting that BRDs recognize combinations of marks rather than singly acetylated sequences. We further uncovered a structural mechanism for the simultaneous binding and recognition of diverse diacetyl-containing peptides by BRD4. These data provide a foundation for structure-based drug design of specific inhibitors for this emerging target family.

Indexed as

Protein Processing, Post-TranslationalProtein Structure, TertiaryAcetylationAmino Acid SequenceAnimalsCrystallography, X-RayGenome, HumanHistonesHumansLysineModels, MolecularMolecular Sequence DataPhylogenyProtein Interaction Domains and MotifsProteomeHistonesLysineProteome

Identifiers

PMID22464331
PMCPMC3326523
OpenAlexW2123647733

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.