Evidence map›Paper›PMID 11027287›Full record

ArticleMolecular and cellular biology2000

Telomerase-associated protein TEP1 is not essential for telomerase activity or telomere length maintenance in vivo.

Y Liu, B E Snow, M P Hande, G Baerlocher, V A Kickhoefer, D Yeung, A Wakeham, A Itie, D P Siderovski, P M Lansdorp and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 87 citations in OpenAlex.

  1. TIR-like NADases act in bacterial immunity and the RNA vault.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Vault RNAs: hidden gems in RNA and protein regulation.Cellular and molecular life sciences : CMLS · 2021
    Review
  11. Article
  12. Article
  13. The vault RNA ofThe Journal of biological chemistry · 2019
    Article
  14. Telomerase and drug resistance in cancer.Cellular and molecular life sciences : CMLS · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

12 authors at 9 institutions in 3 countries.

Y LiuOntario Cancer Institute/Amgen Institute, Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2C1, Canada.
B E Snow
M P Hande
G Baerlocher
V A Kickhoefer
D Yeung
A Wakeham
A Itie
D P Siderovski
P M Lansdorp
M O Robinson
L Harrington
Cancer Institute (WIA) · INCancer Research Center · USOntario Institute for Cancer Research · CAAmgen (Canada) · CAAmgen (United States) · USColumbia University · USUniversity of California, Los Angeles · USUniversity of North Carolina Health Care · USUniversity of Toronto · CA

Funding

NIA NIH HHS AG8422117
6 · The paper itself

Abstract

TEP1 is a mammalian telomerase-associated protein with similarity to the Tetrahymena telomerase protein p80. Like p80, TEP1 is associated with telomerase activity and the telomerase reverse transcriptase, and it specifically interacts with the telomerase RNA. To determine the role of mTep1 in telomerase function in vivo, we generated mouse embryonic stem (ES) cells and mice lacking mTep1. The mTep1-deficient (mTep1(-/-)) mice were viable and were bred for seven successive generations with no obvious phenotypic abnormalities. All murine tissues from mTep1(-/-) mice possessed a level of telomerase activity comparable to that in wild-type mice. In addition, analysis of several tissues that normally lack telomerase activity revealed no reactivation of telomerase activity in mTep1(-/-) mice. Telomere length, even in later generations of mTep1(-/-) mice, was equivalent to that in wild-type animals. ES cells deficient in mTep1 also showed no detectable alteration in telomerase activity or telomere length with increased passage in culture. Thus, mTep1 appears to be completely dispensable for telomerase function in vivo. Recently, TEP1 has been identified within a second ribonucleoprotein (RNP) complex, the vault particle. TEP1 can also specifically bind to a small RNA, vRNA, which is associated with the vault particle and is unrelated in sequence to mammalian telomerase RNA. These results reveal that TEP1 is an RNA binding protein that is not restricted to the telomerase complex and that TEP1 plays a redundant role in the assembly or localization of the telomerase RNP in vivo.

Indexed as

AnimalsCarrier ProteinsCatalysisEmbryo, MammalianIn Situ Hybridization, FluorescenceMiceMice, Inbred C57BLMice, Inbred ICRMice, TransgenicModels, GeneticMutagenesis, Site-DirectedPrecipitin TestsRecombination, GeneticRNARNA-Binding ProteinsSpleenCarrier ProteinsRNARNA-Binding ProteinsTelomerasetelomerase p80 protein, TetrahymenaTep1 protein, mouse

Identifiers

PMID11027287
PMCPMC86427
OpenAlexW2124840664

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.