Evidence map›Paper›PMID 12835755›Full record

ArticleEMBO reports2003

The human telomere-associated protein TIN2 stimulates interactions between telomeric DNA tracts in vitro.

Sahn-Ho Kim, Seungil Han, Young-Hyun You, David J Chen, Judith Campisi

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Trial
  2. Article
  3. Non-canonical roles of canonical telomere binding proteins in cancers.Cellular and molecular life sciences : CMLS · 2021
    Review
  4. A Truncating Germline Mutation ofThyroid : official journal of the American Thyroid Association · 2020
    Article
  5. The Role of Ubiquitination and SUMOylation in Telomere Biology.Current issues in molecular biology · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. Telomeric armor: the layers of end protection.Journal of cell science · 2009
    Article
  10. Article
  11. Article
  12. Article
  13. A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  14. The telomerase cycle: normal and pathological aspects.Journal of molecular medicine (Berlin, Germany) · 2005
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

Sahn-Ho KimLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA.
Seungil Han
Young-Hyun You
David J Chen
Judith Campisi
Lawrence Berkeley National Laboratory · US

Funding

CELLULAR SENESCENCE AND CONTROL OF GENE EXPRESSIONR37AG009909 · NIA · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CAMPISI, JUDITH · 1995 to 2015
$7.6M
KU, TELOMERE MAINTENANCE AND CELLULAR SENESCENCER01AG018949 · NIA · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI CHEN, DAVID J · 2000 to 2004
$2.8M
Cellular senescence and control of gene expressionR56AG009909 · NIA · BUCK INSTITUTE FOR RESEARCH ON AGING · PI CAMPISI, JUDITH · 2017 to 2017
$592k
CELLULAR SENESCENCE AND CONTROL OF GENE EXPRESSIONR01AG009909 · NIA · UNIVERSITY OF CALIFORNIA BERKELEY · PI CAMPISI, JUDITH · 1990 to 1994
–
NIA NIH HHS AG09909NIA NIH HHS AG18949NIA NIH HHS R01 AG018949NIA NIH HHS R37 AG009909NIA NIH HHS R56 AG009909
6 · The paper itself

Abstract

Human TIN2 interacts with the telomeric-DNA-binding protein TRF1, suppresses telomere elongation in telomerase-positive cells, and may control telomere length by modulating telomere structure. To test the latter idea, we developed an in vitro assay, using biotinylated telomeric DNA probes and streptavidin-agarose, to quantify the ability of TRF1 and TIN2 to stimulate interactions of telomeric DNA tracts with each other (probe clustering). This assay revealed that TRF1 alone had weak probe-clustering activity, but TIN2 stimulated activity fivefold to tenfold. A dominant-negative TIN2 mutant protein that increased telomere length in vivo disrupted probe clusters formed by TRF1 and TIN2, suggesting that the ability to stimulate telomeric DNA interactions is important for telomere-length regulation. Unlike TRF1, TIN2 did not form homodimers. We propose that TIN2 alters the conformation of TRF1, which favours a tertiary telomeric structure that hinders telomerase from gaining access to telomeres.

Indexed as

DNADNA ProbesHumansMutationTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1DNADNA ProbesTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1TINF2 protein, human

Identifiers

PMID12835755
PMCPMC1326318
OpenAlexW1969807575

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.