Evidence map›Paper›PMID 21950380›Full record

ReviewCritical reviews in biochemistry and molecular biology2011

Structural anatomy of telomere OB proteins.

Martin P Horvath

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Telomere maintenance in African trypanosomes.Frontiers in molecular biosciences · 2023
    Review
  7. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review
  8. A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Emerging roles of CST in maintaining genome stability and human disease.Frontiers in bioscience (Landmark edition) · 2018
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. 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

1 author at 1 institution in 1 country.

Martin P HorvathDepartment of Biology, University of Utah, Salt Lake City, Utah 84112-0840, USA. horvath@biology.utah.edu
University of Utah · US

Funding

Structures of the ends of telomeresR01GM067994 · NIGMS · UNIVERSITY OF UTAH · PI HORVATH, MARTIN P · 2003 to 2007
$1.3M
NIGMS NIH HHS GM067994NIGMS NIH HHS R01 GM067994
6 · The paper itself

Abstract

Telomere DNA-binding proteins protect the ends of chromosomes in eukaryotes. A subset of these proteins are constructed with one or more OB folds and bind with G+T-rich single-stranded DNA found at the extreme termini. The resulting DNA-OB protein complex interacts with other telomere components to coordinate critical telomere functions of DNA protection and DNA synthesis. While the first crystal and NMR structures readily explained protection of telomere ends, the picture of how single-stranded DNA becomes available to serve as primer and template for synthesis of new telomere DNA is only recently coming into focus. New structures of telomere OB fold proteins alongside insights from genetic and biochemical experiments have made significant contributions towards understanding how protein-binding OB proteins collaborate with DNA-binding OB proteins to recruit telomerase and DNA polymerase for telomere homeostasis. This review surveys telomere OB protein structures alongside highly comparable structures derived from replication protein A (RPA) components, with the goal of providing a molecular context for understanding telomere OB protein evolution and mechanism of action in protection and synthesis of telomere DNA.

Indexed as

Amino Acid SequenceCrystallography, X-RayDNADNA, Single-StrandedEukaryotaMolecular Sequence DataPhylogenyProtein ConformationProtein FoldingProtein Structure, TertiaryReplication Protein ATelomereTelomere-Binding ProteinsDNADNA, Single-StrandedReplication Protein ATelomere-Binding Proteins

Identifiers

PMID21950380
PMCPMC4666000
OpenAlexW2328756205

What OpenQuestion holds

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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.