Evidence map›Paper›PMID 22336916›Full record

ArticleCell cycle (Georgetown, Tex.)2012

Telomere proteins POT1, TRF1 and TRF2 augment long-patch base excision repair in vitro.

Adam S Miller, Lata Balakrishnan, Noah A Buncher, Patricia L Opresko, Robert A Bambara

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Oxidative Stress and DNA Damage at Telomeres.Cold Spring Harbor perspectives in biology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. The Intra- and Extra-Telomeric Role of TRF2 in the DNA Damage Response.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  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

5 authors at 2 institutions in 1 country.

Adam S MillerDepartment of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA.
Lata Balakrishnan
Noah A Buncher
Patricia L Opresko
Robert A Bambara
University of Rochester · USUniversity of Pittsburgh · US

Funding

ENZYMATIC MECHANISMS OF DNA SYNTHESISR01GM024441 · NIGMS · UNIVERSITY OF ROCHESTER · PI BAMBARA, ROBERT A · 1985 to 2011
$3.8M
Mechanisms of Telomeric DNA Loss and RepairR01ES015052 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI OPRESKO, PATRICIA L · 2006 to 2010
$2.4M
NIEHS NIH HHS ES015052NIEHS NIH HHS R01 ES015052NIGMS NIH HHS GM024441NIGMS NIH HHS R01 GM024441
6 · The paper itself

Abstract

Human telomeres consist of multiple tandem hexameric repeats, each containing a guanine triplet. Guanosine-rich clusters are highly susceptible to oxidative base damage, necessitating base excision repair (BER). Previous demonstration of enhanced strand displacement synthesis by the BER component DNA polymerase β in the presence of telomere protein TRF2 suggests that telomeres employ long-patch (LP) BER. Earlier analyses in vitro showed that efficiency of BER reactions is reduced in the DNA-histone environment of chromatin. Evidence presented here indicates that BER is promoted at telomeres. We found that the three proteins that contact telomere DNA, POT1, TRF1 and TRF2, enhance the rate of individual steps of LP-BER and stimulate the complete reconstituted LP-BER pathway. Thought to protect telomere DNA from degradation, these proteins still apparently evolved to allow selective access of repair proteins.

Indexed as

DNA-(Apurinic or Apyrimidinic Site) LyaseDNA Ligase ATPDNA LigasesDNA Polymerase betaDNA RepairElectrophoretic Mobility Shift AssayFlap EndonucleasesHumansProtein BindingShelterin ComplexSubstrate SpecificityTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2APEX1 protein, humanDNA-(Apurinic or Apyrimidinic Site) LyaseDNA Ligase ATPDNA LigasesDNA Polymerase betaFlap EndonucleasesPOT1 protein, humanShelterin ComplexTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2

Identifiers

PMID22336916
PMCPMC3323798
OpenAlexW1985392545

What OpenQuestion holds

Textmetadata
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.