Evidence map›Paper›PMID 24923681›Full record

ArticleNature communications2014

Coordinated DNA dynamics during the human telomerase catalytic cycle.

Joseph W Parks, Michael D Stone

Abstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Flexibility of telomerase in binding the RNA template and DNA telomeric repeat.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. An intrinsic FRET sensor of protein-ligand interactions.Organic & biomolecular chemistry · 2020
    Article
  16. Review
  17. Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019
    Review
  18. Telomere DNA G-quadruplex folding within actively extending human telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. 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

2 authors.

Joseph W ParksDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, USA.
Michael D Stone1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, USA [2] Center for Molecular Biology of RNA, University of California, 1156 High Street, Santa Cruz, California 95064, USA.

Funding

Structure and dynamics of the Tetrahymena telomerase ribonucleoproteinR01GM095850 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STONE, MICHAEL D · 2011 to 2023
$4.4M
NIGMS NIH HHS GM095850NIGMS NIH HHS R01 GM095850
6 · The paper itself

Abstract

The human telomerase reverse transcriptase (hTERT) utilizes a template within the integral RNA subunit (hTR) to direct extension of telomeres. Telomerase exhibits repeat addition processivity (RAP) and must therefore translocate the nascent DNA product into a new RNA:DNA hybrid register to prime each round of telomere repeat synthesis. Here, we use single-molecule FRET and nuclease protection assays to monitor telomere DNA structure and dynamics during the telomerase catalytic cycle. DNA translocation during RAP proceeds through a previously uncharacterized kinetic substep during which the 3'-end of the DNA substrate base pairs downstream within the hTR template. The rate constant for DNA primer realignment reveals this step is not rate limiting for RAP, suggesting a second slow conformational change repositions the RNA:DNA hybrid into the telomerase active site and drives the extrusion of the 5'-end of the DNA primer out of the enzyme complex.

Indexed as

BiocatalysisCatalytic DomainDNADNA PrimersHumansRNATelomeraseTelomereTranscription, GeneticDNADNA PrimersRNATelomerasetelomerase RNATERT protein, human

Identifiers

PMID24923681
PMCPMC4107311

What OpenQuestion holds

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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.