Evidence map›Paper›PMID 20047960›Full record

ArticleNucleic acids research2010

Investigating the role of the Est3 protein in yeast telomere replication.

Jaesung Lee, Edward K Mandell, Timsi Rao, Deborah S Wuttke, Victoria Lundblad

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. Article
  7. Article
  8. A popular engagement at the ends.Nature structural & molecular biology · 2013
    Article
  9. Article
  10. Review
  11. Review
  12. Telomerase and retrotransposons: reverse transcriptases that shaped genomes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Structural anatomy of telomere OB proteins.Critical reviews in biochemistry and molecular biology · 2011
    Review
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Jaesung LeeThe Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
Edward K Mandell
Timsi Rao
Deborah S Wuttke
Victoria Lundblad
Salk Institute for Biological Studies · USUniversity of Colorado Boulder · US

Funding

TRAINING IN SIGNAL TRANSDUCTION &CELL CYCLE REGULATIONT32GM008759 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI AHN, NATALIE G. · 2000 to 2020
$5.9M
Telomere Replication and Senescence in YeastR37AG011728 · NIA · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI LUNDBLAD, VICTORIA · 2003 to 2012
$3.8M
SINGLE STRANDED DNA RECOGNITION IN TELOMERESR01GM059414 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WUTTKE, DEBORAH S. · 1999 to 2015
$3.7M
Predoctoral Training Program in Signaling and Cellular Regulation INCLUDE Down Syndrome SupplementT32GM142607 · NIGMS · UNIVERSITY OF COLORADO · PI Sabrina Leigh Spencer, Tin Tin Su · 2021 to 2026
$3.6M
TELOMERE REPLICATION AND SENESCENCE IN YEASTR01AG011728 · NIA · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI LUNDBLAD, VICTORIA · 1993 to 2019
$2.5M
NIA NIH HHS AG11728NIA NIH HHS R37 AG011728NIGMS NIH HHS R01 GM059414NIGMS NIH HHS T32 GM008759NIGMS NIH HHS T32 GM08759NIGMS NIH HHS T32 GM142607
6 · The paper itself

Abstract

The Est3 subunit of yeast telomerase, which adopts a predicted OB-fold, is essential for telomere replication. To assess the possible contributions that Est3 might make to enzyme catalysis, we compared telomerase activity from wild type and est3-Delta strains of Saccharomyces castellii, which revealed that loss of the Est3 subunit results in a 2- to 3-fold decline in nucleotide addition. This effect was not primer-specific, based on assessment of a panel of primers that spanned the template of the S. castellii telomerase RNA. Furthermore, using nuclear magnetic resonance chemical shift perturbation, no chemical shift change was observed at any site in the protein upon addition of single-stranded DNA, arguing against a role for Est3 in recognition of telomeric substrates by telomerase. Addition of exogenous Est3 protein, including mutant Est3 proteins that are severely impaired for telomere replication in vivo, fully restored activity in est3-Delta telomerase reactions. Thus, Est3 performs an in vivo regulatory function in telomere replication, which is distinct from any potential contribution that Est3 might make to telomerase activity.

Indexed as

DNA, Single-StrandedFungal ProteinsGene DeletionProtein SubunitsSaccharomycesTelomeraseTelomereDNA, Single-StrandedFungal ProteinsProtein SubunitsTelomerase

Identifiers

PMID20047960
PMCPMC2853109
OpenAlexW2151916170

What OpenQuestion holds

Textmetadata
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.