Evidence map›Paper›PMID 28439018›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Conservation and divergence of C-terminal domain structure in the retinoblastoma protein family.

Tyler J Liban, Edgar M Medina, Sarvind Tripathi, Satyaki Sengupta, R William Henry, Nicolas E Buchler, Seth M Rubin

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Large Yellow Croaker (International journal of molecular sciences · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

7 authors at 3 institutions in 1 country.

Tyler J LibanDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064.
Edgar M MedinaDepartment of Biology, Duke University, Durham, NC 27708.
Sarvind TripathiDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064.ORCID 0000-0002-6959-0577
Satyaki SenguptaDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824.
R William HenryDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824.
Nicolas E BuchlerDepartment of Biology, Duke University, Durham, NC 27708.ORCID 0000-0003-3940-3432
Seth M RubinDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064; srubin@ucsc.edu.
University of California, Santa Cruz · USDuke University · USMichigan State University · US

Funding

Molecular Mechanisms Regulating the Retinoblastoma Protein FamilyR01CA132685 · NCI · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI RUBIN, SETH MICHAEL · 2008 to 2017
$3.0M
NCI NIH HHS R01 CA132685
6 · The paper itself

Abstract

The retinoblastoma protein (Rb) and the homologous pocket proteins p107 and p130 negatively regulate cell proliferation by binding and inhibiting members of the E2F transcription factor family. The structural features that distinguish Rb from other pocket proteins have been unclear but are critical for understanding their functional diversity and determining why Rb has unique tumor suppressor activities. We describe here important differences in how the Rb and p107 C-terminal domains (CTDs) associate with the coiled-coil and marked-box domains (CMs) of E2Fs. We find that although CTD-CM binding is conserved across protein families, Rb and p107 CTDs show clear preferences for different E2Fs. A crystal structure of the p107 CTD bound to E2F5 and its dimer partner DP1 reveals the molecular basis for pocket protein-E2F binding specificity and how cyclin-dependent kinases differentially regulate pocket proteins through CTD phosphorylation. Our structural and biochemical data together with phylogenetic analyses of Rb and E2F proteins support the conclusion that Rb evolved specific structural motifs that confer its unique capacity to bind with high affinity those E2Fs that are the most potent activators of the cell cycle.

Indexed as

Crystallography, X-RayE2F Transcription FactorsHumansProtein DomainsRetinoblastoma-Like Protein p107Retinoblastoma ProteinE2F Transcription FactorsRBL1 protein, humanRetinoblastoma-Like Protein p107Retinoblastoma Proteincell cycleE2Fevolutionprotein–protein interactionstumor suppressor protein

Identifiers

PMID28439018
PMCPMC5441720
OpenAlexW2608290560

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.