Evidence map›Paper›PMID 19172753›Full record

ArticleNature structural & molecular biology2008

A proposed OB-fold with a protein-interaction surface in Candida albicans telomerase protein Est3.

Eun Young Yu, Feng Wang, Ming Lei, Neal F Lue

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 55 citations in OpenAlex.

  1. Evolutionary relationship between yeast telomeric protein Cdc13 and Pot1.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
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  9. Article
  10. Article
  11. Review
  12. 21st Century Genetics: Mass Spectrometry of Yeast Telomerase.Cold Spring Harbor symposia on quantitative biology · 2015
    Article
  13. Article
  14. 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
  15. Article
  16. Article
  17. DNA repair at telomeres: keeping the ends intact.Cold Spring Harbor perspectives in biology · 2013
    Review
  18. Phosphorylation of TPP1 regulates cell cycle-dependent telomerase recruitment.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013
    Review
  20. A popular engagement at the ends.Nature structural & molecular biology · 2013
    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

4 authors at 2 institutions in 1 country.

Eun Young YuDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10065, USA.
Feng Wang
Ming Lei
Neal F Lue
University of Michigan–Ann Arbor · USCornell University · US

Funding

Structure of the Telomere Shelterin ComplexR01GM083015 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LEI, MING · 2008 to 2012
$1.2M
Telomerase function and regulation in a new model systemR01GM069507 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LUE, NEAL F · 2004 to 2007
$1.2M
NIGMS NIH HHS GM069507NIGMS NIH HHS GM083015NIGMS NIH HHS R01 GM069507NIGMS NIH HHS R01 GM083015
6 · The paper itself

Abstract

Ever shorter telomeres 3 (Est3) is an essential telomerase regulatory subunit thought to be unique to budding yeasts. Here we use multiple sequence alignment and hidden Markov model-hidden Markov model (HMM-HMM) comparison to uncover potential similarities between Est3 and the mammalian telomeric protein Tpp1. Analysis of site-specific mutants of Candida albicans Est3 revealed functional distinctions between residues that are conserved between Est3 and Tpp1 and those that are unique to Est3. Although both types of residues are important for telomere maintenance in vivo, only the former contributes to telomerase activity in vitro and facilitates the association of Est3 with telomerase core components. Consistent with a function in protein-protein interaction, the residues common to Est3 and Tpp1 map to one face of an OB-fold model structure, away from the canonical nucleic acid binding surface. We propose that Est3 and the OB-fold domain of Tpp1 mediate a conserved function in telomerase regulation.

Indexed as

Amino Acid SequenceBase SequenceCandida albicansDNA, FungalFungal ProteinsGenes, FungalModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhenotypeProtein FoldingProtein Interaction Domains and MotifsRecombinant ProteinsSequence Homology, Amino AcidShelterin ComplexTelomeraseACD protein, humanDNA, FungalFungal ProteinsRecombinant ProteinsShelterin ComplexTelomeraseTelomere-Binding Proteins

Identifiers

PMID19172753
PMCPMC2656765
OpenAlexW2052490288

What OpenQuestion holds

Textmetadata
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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.