Evidence map›Paper›PMID 28141967›Full record

ReviewAnnual review of biochemistry2017

Telomerase Mechanism of Telomere Synthesis.

R Alex Wu, Heather E Upton, Jacob M Vogan, Kathleen Collins

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
16.3field-weighted citation impact, top 1% 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

131 citing papers in PubMed, 221 citations in OpenAlex.

  1. Article
  2. Article
  3. Fission yeast RPA-TERT-Tpz1bioRxiv : the preprint server for biology · 2026
    Article
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
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  13. RNA Triple Helices: From Structures and Mechanisms to Therapeutic Targets.International journal of biological sciences · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

71 more citing papers are in PubMed but not listed here.

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.

R Alex WuDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202; email: rawu@berkeley.edu , hupton@berkeley.edu , jacob.vogan@berkeley.edu , kcollins@berkeley.edu.
Heather E UptonDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202; email: rawu@berkeley.edu , hupton@berkeley.edu , jacob.vogan@berkeley.edu , kcollins@berkeley.edu.
Jacob M VoganDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202; email: rawu@berkeley.edu , hupton@berkeley.edu , jacob.vogan@berkeley.edu , kcollins@berkeley.edu.
Kathleen CollinsDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202; email: rawu@berkeley.edu , hupton@berkeley.edu , jacob.vogan@berkeley.edu , kcollins@berkeley.edu.
University of California, Berkeley · 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 R01 HL079585NHLBI NIH HHS R56 HL079585NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

Telomerase is the essential reverse transcriptase required for linear chromosome maintenance in most eukaryotes. Telomerase supplements the tandem array of simple-sequence repeats at chromosome ends to compensate for the DNA erosion inherent in genome replication. The template for telomerase reverse transcriptase is within the RNA subunit of the ribonucleoprotein complex, which in cells contains additional telomerase holoenzyme proteins that assemble the active ribonucleoprotein and promote its function at telomeres. Telomerase is distinct among polymerases in its reiterative reuse of an internal template. The template is precisely defined, processively copied, and regenerated by release of single-stranded product DNA. New specificities of nucleic acid handling that underlie the catalytic cycle of repeat synthesis derive from both active site specialization and new motif elaborations in protein and RNA subunits. Studies of telomerase provide unique insights into cellular requirements for genome stability, tissue renewal, and tumorigenesis as well as new perspectives on dynamic ribonucleoprotein machines.

Indexed as

DNA ReplicationAnimalsCatalytic DomainDNA, Single-StrandedGene Expression RegulationHumansMicrosatellite RepeatsNucleic Acid ConformationOxytrichaRibonucleoproteinsRNASaccharomyces cerevisiaeTelomeraseTelomereTetrahymena thermophilaDNA, Single-StrandedRibonucleoproteinsRNATelomeraseDNA replicationreverse transcriptaseribonucleoprotein biogenesistelomere

Identifiers

PMID28141967
PMCPMC5812681
OpenAlexW2550983084

What OpenQuestion holds

Textmetadata
LicenceTDM
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.