Evidence map›Paper›PMID 21047798›Full record

ArticleThe Journal of biological chemistry2011

Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48·FOG-1 complex.

Sara Lejon, Sock Yue Thong, Andal Murthy, Saad AlQarni, Natalia V Murzina, Gerd A Blobel, Ernest D Laue, Joel P Mackay

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
2.3field-weighted citation impact, top 12% 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, 101 citations in OpenAlex.

  1. Article
  2. New Gene Therapy Strategy for β-Thalassemia.Stem cell reviews and reports · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Rbbp4 loss disrupts neural progenitor cell cycle regulation independent of Rb and leads to Tp53 acetylation and apoptosis.Developmental dynamics : an official publication of the American Association of Anatomists · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Structure Based Design of Bicyclic Peptide Inhibitors of RbAp48.Angewandte Chemie (International ed. in English) · 2021
    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

8 authors at 4 institutions in 4 countries.

Sara LejonDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
Sock Yue Thong
Andal Murthy
Saad AlQarni
Natalia V Murzina
Gerd A Blobel
Ernest D Laue
Joel P Mackay
University of Sydney · AUBridge University · SSUniversity of Cambridge · GBChildren's Hospital of Philadelphia · US

Funding

Roles of CBP &PCAF During Hematopoietic DifferentiationR01DK058044 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI BLOBEL, GERD A · 2002 to 2023
$4.5M
Epigenetic Control of Hematopoietic Gene ExpressionR37DK058044 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI BLOBEL, GERD A · 2010 to 2019
$3.7M
NIDDK NIH HHS DK058044NIDDK NIH HHS R01 DK058044NIDDK NIH HHS R37 DK058044Wellcome Trust
6 · The paper itself

Abstract

Chromatin-modifying complexes such as the NuRD complex are recruited to particular genomic sites by gene-specific nuclear factors. Overall, however, little is known about the molecular basis for these interactions. Here, we present the 1.9 Å resolution crystal structure of the NuRD subunit RbAp48 bound to the 15 N-terminal amino acids of the GATA-1 cofactor FOG-1. The FOG-1 peptide contacts a negatively charged binding pocket on top of the RbAp48 β-propeller that is distinct from the binding surface used by RpAp48 to contact histone H4. We further show that RbAp48 interacts with the NuRD subunit MTA-1 via a surface that is distinct from its FOG-binding pocket, providing a first glimpse into the way in which NuRD assembly facilitates interactions with cofactors. Our RbAp48·FOG-1 structure provides insight into the molecular determinants of FOG-1-dependent association with the NuRD complex and into the links between transcription regulation and nucleosome remodeling.

Indexed as

Histone DeacetylasesMi-2 Nucleosome Remodeling and Deacetylase ComplexNuclear ProteinsRepressor ProteinsRetinoblastoma-Binding Protein 4Transcription FactorsAmino Acid SequenceAnimalsBinding SitesCells, CulturedConserved SequenceCrystallography, X-RayHistonesMicrofilament ProteinsMolecular Sequence DataProtein Interaction Domains and MotifsHistone DeacetylasesHistonesMi-2 Nucleosome Remodeling and Deacetylase ComplexMicrofilament ProteinsMTA1 protein, humanNuclear ProteinsRBBP4 protein, humanRecombinant ProteinsRepressor ProteinsRetinoblastoma-Binding Protein 4Trans-ActivatorsTranscription FactorsWDR1 protein, humanZFPM1 protein, human

Identifiers

PMID21047798
PMCPMC3020727
OpenAlexW2021827170

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.