Evidence map›Paper›PMID 24619002›Full record

ArticleThe EMBO journal2014

Human telomerase specialization for repeat synthesis by unique handling of primer-template duplex.

Robert Alexander Wu, Kathleen Collins

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.6field-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

41 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020
    Review
  10. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  11. Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018
    Review
  17. Article
  18. Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017
    Review
  19. Article
  20. Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017
    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

2 authors at 2 institutions in 1 country.

Robert Alexander WuDepartment of Molecular and Cell Biology, University of California, Berkeley, CA, USA.
Kathleen Collins
University of California, Berkeley · USUniversity of California System · US

Funding

STRUCTURE AND FUNCTION OF TELOMERASER01GM054198 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 1996 to 2018
$5.4M
Molecular Mechanism of X-linked Dyskeratosis CongenitaR01HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2004 to 2017
$4.1M
Biogenesis and Regulation of Human TelomeraseR56HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2008 to 2008
$367k
NHLBI NIH HHS HL079585NHLBI NIH HHS R01 HL079585NHLBI NIH HHS R56 HL079585NIGMS NIH HHS GM054198NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

With eukaryotic genome replication, incomplete telomere synthesis results in chromosome shortening and eventual compromise of genome stability. Telomerase counteracts this terminal sequence loss by synthesizing telomeric repeats through repeated cycles of reverse transcription of its internal RNA template. Using human telomerase domain-complementation assays for telomerase reverse transcriptase protein (TERT) and RNA in combination with the first direct footprinting assay for telomerase association with bound DNA, we resolve mechanisms by which TERT domains and RNA motifs direct repeat synthesis. Surprisingly, we find that product-template hybrid is sensed in a length- and sequence-dependent manner to set the template 5' boundary. We demonstrate that the TERT N-terminal (TEN) domain determines active-site use of the atypically short primer-template hybrid necessary for telomeric-repeat synthesis. Also against expectation, we show that the remainder of TERT (the TERT ring) supports functional recognition and physical protection of single-stranded DNA adjacent to the template hybrid. These findings establish unprecedented polymerase recognition specificities for DNA-RNA hybrid and single-stranded DNA and suggest a new perspective on the mechanisms of telomerase specialization for telomeric-repeat synthesis.

Indexed as

Templates, GeneticDNAHumansRepetitive Sequences, Nucleic AcidRNATelomeraseDNARNARNA primersTelomeraseTERT protein, human

Identifiers

PMID24619002
PMCPMC4194115
OpenAlexW1970770718

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.