Evidence map›Paper›PMID 19531742›Full record

ArticleNucleic acids research2009

The Myb/SANT domain of the telomere-binding protein TRF2 alters chromatin structure.

Asmaa M Baker, Qiang Fu, William Hayward, Stuart M Lindsay, Terace M Fletcher

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. TRF1 and TRF2: pioneering targets in telomere-based cancer therapy.Journal of cancer research and clinical oncology · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Myb proteins: angels and demons in normal and transformed cells.Frontiers in bioscience (Landmark edition) · 2011
    Review
  17. Article
  18. Conservation of telomere protein complexes: shuffling through evolution.Critical reviews in biochemistry and molecular biology
    Review
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.

Asmaa M BakerDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33101-6129, USA.
Qiang Fu
William Hayward
Stuart M Lindsay
Terace M Fletcher
University of Miami · USArizona State University · US

Funding

Structural Analysis of Telomere ChromatinF31GM075427 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BAKER, ASMAA M. · 2005 to 2007
$113k
NIGMS NIH HHS 31-GM75427-01
6 · The paper itself

Abstract

Eukaryotic DNA is packaged into chromatin, which regulates genome activities such as telomere maintenance. This study focuses on the interactions of a myb/SANT DNA-binding domain from the telomere-binding protein, TRF2, with reconstituted telomeric nucleosomal array fibers. Biophysical characteristics of the factor-bound nucleosomal arrays were determined by analytical agarose gel electrophoresis (AAGE) and single molecules were visualized by atomic force microscopy (AFM). The TRF2 DNA-binding domain (TRF2 DBD) neutralized more negative charge on the surface of nucleosomal arrays than histone-free DNA. Binding of TRF2 DBD at lower concentrations increased the radius and conformational flexibility, suggesting a distortion of the fiber structure. Additional loading of TRF2 DBD onto the nucleosomal arrays reduced the flexibility and strongly blocked access of micrococcal nuclease as contour lengths shortened, consistent with formation of a unique, more compact higher-order structure. Mirroring the structural results, TRF2 DBD stimulated a strand invasion-like reaction, associated with telomeric t-loops, at lower concentrations while inhibiting the reaction at higher concentrations. Full-length TRF2 was even more effective at stimulating this reaction. The TRF2 DBD had less effect on histone-free DNA structure and did not stimulate the t-loop reaction with this substrate, highlighting the influence of chromatin structure on the activities of DNA-binding proteins.

Indexed as

AnimalsDNAHumansMicrococcal NucleaseMicroscopy, Atomic ForceNucleosomesOligonucleotidesProtein Structure, TertiaryTelomereTelomeric Repeat Binding Protein 2DNAMicrococcal NucleaseNucleosomesOligonucleotidesTelomeric Repeat Binding Protein 2

Identifiers

PMID19531742
PMCPMC2731900
OpenAlexW2109931741

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.