Evidence map›Paper›PMID 19920121›Full record

ArticleNucleic acids research2010

A single-molecule assay for telomerase structure-function analysis.

John Y Wu, Michael D Stone, Xiaowei Zhuang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Single-Run Catalysis and Kinetic Control of Human Telomerase Holoenzyme.Advances in experimental medicine and biology · 2022
    Review
  3. Article
  4. Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019
    Review
  5. 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
  6. Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Progress in structural studies of telomerase.Current opinion in structural biology · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Parallel multispot smFRET analysis using an 8-pixel SPAD array.Proceedings of SPIE--the International Society for Optical Engineering · 2012
    Article
  20. Functional importance of telomerase pseudoknot revealed by single-molecule analysis.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

3 authors at 2 institutions in 1 country.

John Y WuDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Michael D Stone
Xiaowei Zhuang
Howard Hughes Medical Institute · USHarvard University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The activity of the telomerase ribonucleoprotein enzyme is essential for the maintenance of genome stability and normal cell development. Despite the biomedical importance of telomerase activity, detailed structural models for the enzyme remain to be established. Here we report a single-molecule assay for direct structural analysis of catalytically active telomerase enzymes. In this assay, oligonucleotide hybridization was used to probe the primer-extension activity of individual telomerase enzymes with single nucleotide sensitivity, allowing precise discrimination between inactive, active and processive enzyme binding events. FRET signals from enzyme molecules during the active and processive binding events were then used to determine the global organization of telomerase RNA within catalytically active holoenzymes. Using this assay, we have identified an active conformation of telomerase among a heterogeneous population of enzymes with distinct structures.

Indexed as

Fluorescence Resonance Energy TransferBiocatalysisNucleic Acid ConformationNucleic Acid HybridizationRNATelomeraseRNATelomerasetelomerase RNA

Identifiers

PMID19920121
PMCPMC2817460
OpenAlexW2168419371

What OpenQuestion holds

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LicenceCC BY-NC
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.