Evidence map›Paper›PMID 19329795›Full record

ArticleThe Journal of biological chemistry2009

Telomerase-associated protein 1, HSP90, and topoisomerase IIalpha associate directly with the BLM helicase in immortalized cells using ALT and modulate its helicase activity using telomeric DNA substrates.

Saumitri Bhattacharyya, Jeremy Keirsey, Beatriz Russell, Juraj Kavecansky, Kate Lillard-Wetherell, Kambiz Tahmaseb, John J Turchi, Joanna Groden

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Inhibition ofFrontiers in parasitology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. The many facets of homologous recombination at telomeres.Microbial cell (Graz, Austria) · 2015
    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

8 authors at 5 institutions in 1 country.

Saumitri BhattacharyyaDepartment of Molecular Virology, Immunology and Medical Genetics, The Ohio State University College of Medicine, Columbus, Ohio 43210-2207, USA.
Jeremy Keirsey
Beatriz Russell
Juraj Kavecansky
Kate Lillard-Wetherell
Kambiz Tahmaseb
John J Turchi
Joanna Groden
The Ohio State University · USHoward Hughes Medical Institute · USIndiana University – Purdue University Indianapolis · USUniversity of Cincinnati · USWright State University · US

Funding

Functions of the BLM Helicase in Telomere MaintenanceR01CA117898 · NCI · OHIO STATE UNIVERSITY · PI GRODEN, JOANNA LOUISE · 2008 to 2012
$1.5M
NCI NIH HHS CA-117898
6 · The paper itself

Abstract

The BLM helicase associates with the telomere structural proteins TRF1 and TRF2 in immortalized cells using the alternative lengthening of telomere (ALT) pathways. This work focuses on identifying protein partners of BLM in cells using ALT. Mass spectrometry and immunoprecipitation techniques have identified three proteins that bind directly to BLM and TRF2 in ALT cells: telomerase-associated protein 1 (TEP1), heat shock protein 90 (HSP90), and topoisomerase IIalpha (TOPOIIalpha). BLM predominantly co-localizes with these proteins in foci actively synthesizing DNA during late S and G(2)/M phases of the cell cycle when ALT is thought to occur. Immunoprecipitation studies also indicate that only HSP90 and TOPOIIalpha are components of a specific complex containing BLM, TRF1, and TRF2 but that this complex does not include TEP1. TEP1, TOPOIIalpha, and HSP90 interact directly with BLM in vitro and modulate its helicase activity on telomere-like DNA substrates but not on non-telomeric substrates. Initial studies suggest that knockdown of BLM in ALT cells reduces average telomere length but does not do so in cells using telomerase.

Indexed as

Antigens, NeoplasmBlotting, WesternCarrier ProteinsCell Line, TransformedCell Nucleus StructuresDNADNA-Binding ProteinsDNA Topoisomerases, Type IIHSP90 Heat-Shock ProteinsHumansMass SpectrometryProtein TransportRecQ HelicasesRNA-Binding ProteinsTelomereTelomeric Repeat Binding Protein 2Antigens, NeoplasmBloom syndrome proteinCarrier ProteinsDNADNA-Binding ProteinsDNA Topoisomerases, Type IIHSP90 Heat-Shock ProteinsRecQ HelicasesRNA-Binding ProteinsTelomeric Repeat Binding Protein 2TEP1 protein, humanTERF2 protein, human

Identifiers

PMID19329795
PMCPMC2685679
OpenAlexW2033993988

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.