Evidence map›Paper›PMID 23826127›Full record

ArticlePloS one2013

Structure of the human telomeric Stn1-Ten1 capping complex.

Christopher Bryan, Cory Rice, Michael Harkisheimer, David C Schultz, Emmanuel Skordalakes

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

64 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Telomeres and Cancer.Life (Basel, Switzerland) · 2021
    Review
  14. Article
  15. Article
  16. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review
  17. Review
  18. Review
  19. Review
  20. Article

4 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

5 authors at 1 institution in 1 country.

Christopher BryanGene Expression and Regulation Program, The Wistar Institute, Philadelphia, Pennsylvania, United States of America.
Cory Rice
Michael Harkisheimer
David C Schultz
Emmanuel Skordalakes
The Wistar Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
Structural and Biochemical Analysis of Telomerase FunctionR01GM088332 · NIGMS · WISTAR INSTITUTE · PI SKORDALAKES, EMMANUEL · 2010 to 2014
$1.7M
NCI NIH HHS P30 CA010815NCI NIH HHS P30 CA10815NCI NIH HHS T32 CA009171NIGMS NIH HHS 5R01 GM088332-03NIGMS NIH HHS R01 GM088332
6 · The paper itself

Abstract

The identification of the human homologue of the yeast CST in 2009 posed a new challenge in our understanding of the mechanism of telomere capping in higher eukaryotes. The high-resolution structure of the human Stn1-Ten1 (hStn1-Ten1) complex presented here reveals that hStn1 consists of an OB domain and tandem C-terminal wHTH motifs, while hTen1 consists of a single OB fold. Contacts between the OB domains facilitate formation of a complex that is strikingly similar to the replication protein A (RPA) and yeast Stn1-Ten1 (Ten1) complexes. The hStn1-Ten1 complex exhibits non-specific single-stranded DNA activity that is primarily dependent on hStn1. Cells expressing hStn1 mutants defective for dimerization with hTen1 display elongated telomeres and telomere defects associated with telomere uncapping, suggesting that the telomeric function of hCST is hTen1 dependent. Taken together the data presented here show that the structure of the hStn1-Ten1 subcomplex is conserved across species. Cell based assays indicate that hTen1 is critical for the telomeric function of hCST, both in telomere protection and downregulation of telomerase function.

Indexed as

HumansProtein BindingProtein MultimerizationProtein Structure, SecondaryTelomereTelomere-Binding ProteinsStn1 protein, humanTelomere-Binding ProteinsTen1 protein, human

Identifiers

PMID23826127
PMCPMC3691326
OpenAlexW1990329751

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.