Evidence map›Paper›PMID 15994230›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Telomerase can act as a template- and RNA-independent terminal transferase.

Neal F Lue, Dimitry Bosoy, Tara J Moriarty, Chantal Autexier, Brian Altman, Siyang Leng

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Impaired manganese metabolism causes mitotic misregulation.The Journal of biological chemistry · 2012
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A widespread class of reverse transcriptase-related cellular genes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Separation of telomerase functions by reverse genetics.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  18. Single-stranded DNA repeat synthesis by telomerase.Current opinion in chemical biology · 2011
    Review
  19. Article
  20. Ribonucleoprotein multimers and their functions.Critical reviews in biochemistry and molecular biology · 2010
    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

6 authors at 3 institutions in 2 countries.

Neal F LueDepartment of Microbiology and Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA. nflue@med.cornell.edu
Dimitry Bosoy
Tara J Moriarty
Chantal Autexier
Brian Altman
Siyang Leng
McGill University · CACornell University · USJewish General Hospital · CA

Funding

ANALYSIS OF TELOMERASE REVERSE TRANSCRIPTASER01GM062631 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LUE, NEAL F · 2001 to 2010
$3.0M
CIHR 54638NIGMS NIH HHS GM 62631NIGMS NIH HHS R01 GM062631
6 · The paper itself

Abstract

Telomerase is a special reverse transcriptase that extends one strand of the telomere repeat by using a template embedded in an RNA subunit. Like other polymerases, telomerase is believed to use a pair of divalent metal ions (coordinated by a triad of aspartic acid residues) for catalyzing nucleotide addition. Here we show that, in the presence of manganese, both yeast and human telomerase can switch to a template- and RNA-independent mode of DNA synthesis, acting in effect as a terminal transferase. Even as a terminal transferase, yeast telomerase retains a species-dependent preference for GT-rich, telomere-like DNA on the 5' end of the substrate. The terminal transferase activity of telomerase may account for some of the hitherto unexplained effects of telomerase overexpression on cell physiology.

Indexed as

Base SequenceDNADNA PrimersDNA ReplicationElectrophoresisHumansManganeseReticulocytesSaccharomyces cerevisiaeTelomeraseTelomereTransferasesDNADNA PrimersManganeseTelomeraseTransferases

Identifiers

PMID15994230
PMCPMC1174988
OpenAlexW2111498124

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.