Evidence map›Paper›PMID 22244753›Full record

ReviewStructure (London, England : 1993)2012

Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.

Karen A Lewis, Deborah S Wuttke

Open access · bronzeAbstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  9. Article
  10. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Molecular characterization ofLife science alliance · 2019
    Article
  16. Cell discovery · 2019
    Article
  17. Review
  18. TheThe Journal of biological chemistry · 2018
    Article
  19. Review
  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 at 1 institution in 1 country.

Karen A LewisDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA.
Deborah S Wuttke
University of Colorado Boulder · US

Funding

SINGLE STRANDED DNA RECOGNITION IN TELOMERESR01GM059414 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WUTTKE, DEBORAH S. · 1999 to 2015
$3.7M
In Vitro Reconstitution and Biochemical Characterization of Yeast TelomeraseF32GM093528 · NIGMS · UNIVERSITY OF COLORADO · PI LEWIS, KAREN ADELL · 2011 to 2012
$105k
NIGMS NIH HHS F32 GM093528NIGMS NIH HHS GM059414NIGMS NIH HHS GM093528NIGMS NIH HHS R01 GM059414
6 · The paper itself

Abstract

Recent advances in our structural understanding of telomerase and telomere-associated proteins have contributed significantly to elucidating the molecular mechanisms of telomere maintenance. The structures of telomerase TERT domains have provided valuable insights into how experimentally identified conserved motifs contribute to the telomerase reverse transcriptase reaction. Additionally, structures of telomere-associated proteins in a variety of organisms have revealed that, across evolution, telomere-maintenance mechanisms employ common structural elements. For example, the single-stranded 3' overhang of telomeric DNA is specifically and tightly bound by an OB-fold in nearly all species, including ciliates (TEBP and Pot1a), fission yeast (SpPot1), budding yeast (Cdc13), and humans (hPOT1). Structures of the yeast Cdc13, Stn1, and Ten1 proteins demonstrated that telomere maintenance is regulated by a complex that bears significant similarity to the RPA heterotrimer. Similarly, proteins that specifically bind double-stranded telomeric DNA in divergent species use homeodomains to execute their functions (human TRF1 and TRF2 and budding yeast ScRap1). Likewise, the conserved protein Rap1, which is found in budding yeast, fission yeast, and humans, contains a structural motif that is known to be critical for protein-protein interaction. In addition to revealing the common underlying themes of telomere maintenance, structures have also elucidated the specific mechanisms by which many of these proteins function, including identifying a telomere-specific domain in Stn1 and how the human TRF proteins avoid heterodimerization. In this review, we summarize the high-resolution structures of telomerase and telomere-associated proteins and discuss the emergent common structural themes among these proteins. We also address how these high-resolution structures complement biochemical and cellular studies to enhance our understanding of telomere maintenance and function.

Indexed as

Evolution, MolecularModels, MolecularProtein Structure, TertiaryHumansSpecies SpecificityTelomeraseTelomere-Binding ProteinsTelomeraseTelomere-Binding Proteins

Identifiers

PMID22244753
PMCPMC4180718
OpenAlexW2006496261

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.