Evidence map›Paper›PMID 17996702›Full record

ArticleMolecular cell2007

Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture.

Markus Hassler, Shradha Singh, Wyatt W Yue, Maciej Luczynski, Rachid Lakbir, Francisco Sanchez-Sanchez, Thomas Bader, Laurence H Pearl, Sibylle Mittnacht

Abstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

44 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Chromatin association promotes UBR5-mediated degradation of Rb.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
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  8. Article
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  13. Article
  14. NovelDiagnostics (Basel, Switzerland) · 2020
    Article
  15. Review
  16. Regulating tumor suppressor genes: post-translational modifications.Signal transduction and targeted therapy · 2020
    Review
  17. A tumor suppressor Retinoblastoma1 is essential for embryonic development in the sea urchin.Developmental dynamics : an official publication of the American Association of Anatomists · 2019
    Article
  18. Article
  19. Article
  20. Article
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

9 authors.

Markus HasslerCancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, The Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK.
Shradha Singh
Wyatt W Yue
Maciej Luczynski
Rachid Lakbir
Francisco Sanchez-Sanchez
Thomas Bader
Laurence H Pearl
Sibylle Mittnacht

Funding

Cancer Research UK A7640
6 · The paper itself

Abstract

The retinoblastoma susceptibility protein, Rb, has a key role in regulating cell-cycle progression via interactions involving the central "pocket" and C-terminal regions. While the N-terminal domain of Rb is dispensable for this function, it is nonetheless strongly conserved and harbors missense mutations found in hereditary retinoblastoma, indicating that disruption of its function is oncogenic. The crystal structure of the Rb N-terminal domain (RbN), reveals a globular entity formed by two rigidly connected cyclin-like folds. The similarity of RbN to the A and B boxes of the Rb pocket domain suggests that Rb evolved through domain duplication. Structural and functional analysis provides insight into oncogenicity of mutations in RbN and identifies a unique phosphorylation-regulated site of protein interaction. Additionally, this analysis suggests a coherent conformation for the Rb holoprotein in which RbN and pocket domains directly interact, and which can be modulated through ligand binding and possibly Rb phosphorylation.

Indexed as

Amino Acid SequenceBinding SitesCell Cycle ProteinsCrystallography, X-RayHumansLigandsModels, MolecularMolecular Sequence DataNuclear ProteinsProtein Interaction MappingProtein Structure, TertiaryRepressor ProteinsRetinoblastomaRetinoblastoma ProteinCell Cycle ProteinsEID1 protein, humanLigandsNuclear ProteinsRepressor ProteinsRetinoblastoma Protein

Identifiers

PMID17996702
PMCPMC4944837

What OpenQuestion holds

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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.