Evidence map›Paper›PMID 23685356›Full record

ArticleThe EMBO journal2013

HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment.

Dennis Kappei, Falk Butter, Christian Benda, Marion Scheibe, Irena Draškovič, Michelle Stevense, Clara Lopes Novo, Claire Basquin, Masatake Araki, Kimi Araki and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.5field-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

47 citing papers in PubMed, 85 citations in OpenAlex.

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  6. Ensartinib in a primary pulmonaryFrontiers in medicine · 2025
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  10. Role of telomere length in human carcinogenesis (Review).International journal of oncology · 2023
    Review
  11. Biological roles of the RNA mExperimental & molecular medicine · 2022
    Review
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  13. Article
  14. Superficial ALK-rearranged myxoid spindle cell neoplasm: a cutaneous soft tissue tumor with distinctive morphology and immunophenotypic profile.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2021
    Article
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  19. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 8 institutions in 4 countries.

Dennis KappeiMedical Systems Biology, Faculty of Medicine Carl Gustav Carus, University Cancer Center, Dresden University of Technology, 01307 Dresden, Germany.
Falk Butter
Christian Benda
Marion Scheibe
Irena Draškovič
Michelle Stevense
Clara Lopes Novo
Claire Basquin
Masatake Araki
Kimi Araki
Dragomir Blazhev Krastev
Ralf Kittler
Rolf Jessberger
J Arturo Londoño-Vallejo
Matthias Mann
Frank Buchholz
Max Planck Society · DEMax Planck Institute of Molecular Cell Biology and Genetics · DEInstitut Curie · FRKumamoto University · JPCentre National de la Recherche Scientifique · FRSouthwestern Medical Center · USTechnische Universität Dresden · DEUniversity Hospital Carl Gustav Carus · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Telomeres are repetitive DNA structures that, together with the shelterin and the CST complex, protect the ends of chromosomes. Telomere shortening is mitigated in stem and cancer cells through the de novo addition of telomeric repeats by telomerase. Telomere elongation requires the delivery of the telomerase complex to telomeres through a not yet fully understood mechanism. Factors promoting telomerase-telomere interaction are expected to directly bind telomeres and physically interact with the telomerase complex. In search for such a factor we carried out a SILAC-based DNA-protein interaction screen and identified HMBOX1, hereafter referred to as homeobox telomere-binding protein 1 (HOT1). HOT1 directly and specifically binds double-stranded telomere repeats, with the in vivo association correlating with binding to actively processed telomeres. Depletion and overexpression experiments classify HOT1 as a positive regulator of telomere length. Furthermore, immunoprecipitation and cell fractionation analyses show that HOT1 associates with the active telomerase complex and promotes chromatin association of telomerase. Collectively, these findings suggest that HOT1 supports telomerase-dependent telomere elongation.

Indexed as

ChromatinHeLa CellsHomeodomain ProteinsHumansMultiprotein ComplexesRepetitive Sequences, Nucleic AcidTelomeraseTelomereTelomere-Binding ProteinsChromatinHMBOX1 protein, humanHomeodomain ProteinsMultiprotein ComplexesTelomeraseTelomere-Binding Proteins

Identifiers

PMID23685356
PMCPMC3680732
OpenAlexW2116891709

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.