Evidence map›Paper›PMID 29057866›Full record

ArticleNature communications2017

Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity.

Ci Ji Lim, Arthur J Zaug, Hee Jin Kim, Thomas R Cech

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Inherited Telomere Biology Disorders: Pathophysiology, Clinical Presentation, Diagnostics, and Treatment.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2024
    Review
  7. Article
  8. Review
  9. TRF1 and TRF2: pioneering targets in telomere-based cancer therapy.Journal of cancer research and clinical oncology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Shelterin is a dimeric complex with extensive structural heterogeneity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. 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

4 authors at 1 institution in 1 country.

Ci Ji LimHoward Hughes Medical Institute, University of Colorado BioFrontiers Institute, Boulder, CO, 80309, USA.
Arthur J ZaugHoward Hughes Medical Institute, University of Colorado BioFrontiers Institute, Boulder, CO, 80309, USA.
Hee Jin KimHoward Hughes Medical Institute, University of Colorado BioFrontiers Institute, Boulder, CO, 80309, USA.
Thomas R CechHoward Hughes Medical Institute, University of Colorado BioFrontiers Institute, Boulder, CO, 80309, USA. Thomas.Cech@colorado.edu.ORCID http://orcid.org/0000-0001-7338-3389
Howard Hughes Medical Institute · US

Funding

TERT Promoter Mutations and Telomerase Reactivation in Cancer CellsR01GM099705 · NIGMS · UNIVERSITY OF COLORADO · PI CECH, THOMAS ROBERT · 2012 to 2019
$1.4M
Q Exactive HF Nanoflow LC Mass Spectrometry SystemS10OD025267 · OD · UNIVERSITY OF COLORADO · PI AHN, NATALIE G. · 2018 to 2018
$600k
Purchase of a CD SpectropolarimeterS10RR028036 · NCRR · UNIVERSITY OF COLORADO · PI WUTTKE, DEBORAH S. · 2010 to 2010
$194k
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR028036NIGMS NIH HHS R01 GM099705NIH HHS S10 OD025267
6 · The paper itself

Abstract

The human shelterin proteins associate with telomeric DNA to confer telomere protection and length regulation. They are thought to form higher-order protein complexes for their functions, but studies of shelterin proteins have been mostly limited to pairs of proteins. Here we co-express various human shelterin proteins and find that they form defined multi-subunit complexes. A complex harboring both TRF2 and POT1 has the strongest binding affinity to telomeric DNA substrates comprised of double-stranded DNA with a 3' single-stranded extension. TRF2 interacts with TIN2 with an unexpected 2:1 stoichiometry in the context of shelterin (RAP1

Indexed as

Cell Adhesion MoleculesCells, CulturedElectrophoretic Mobility Shift AssayHumansProtein BindingShelterin ComplexTelomeraseTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2ACD protein, humanCell Adhesion MoleculesPOT1 protein, humanShelterin ComplexTelomeraseTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2TERF2 protein, humanTINAG protein, human

Identifiers

PMID29057866
PMCPMC5651854
OpenAlexW2765080185

What OpenQuestion holds

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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.