Evidence map›Paper›PMID 40638752›Full record

ArticleScience (New York, N.Y.)2025

Cryo-EM structure of human telomerase dimer reveals H/ACA RNP-mediated dimerization.

Sebastian Balch, Zala Sekne, Elsa Franco-Echevarría, Patryk Ludzia, Rachael C Kretsch, Wenqing Sun, Haopeng Yu, George E Ghanim, Sigurdur Thorkelsson, Yiliang Ding and 2 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. How telomere attrition protects against cancer.Nature reviews. Genetics · 2026
    Review
  2. Article
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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

12 authors.

Sebastian Balch *MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0009-0005-9663-7456
Zala Sekne *MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-7584-8776
Elsa Franco-Echevarría *MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-7306-6594
Patryk LudziaMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-1678-6875
Rachael C KretschBiophysics Program, Stanford University, Stanford, CA, USA.ORCID 0000-0002-6935-518X
Wenqing SunKey Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University, Changchun, China.ORCID 0009-0004-9528-919X
Haopeng YuDepartment of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, UK.ORCID 0000-0002-5184-2430
George E GhanimMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-3341-3122
Sigurdur ThorkelssonMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-9421-9788
Yiliang DingDepartment of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, UK.ORCID 0000-0003-4161-6365
Rhiju DasBiophysics Program, Stanford University, Stanford, CA, USA.ORCID 0000-0001-7497-0972
Thi Hoang Duong NguyenMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-2180-3430

Funding

Next-generation computational/chemical methods for complex RNA structuresR35GM122579 · NIGMS · STANFORD UNIVERSITY · PI Rhiju Das · 2017 to 2026
$7.2M
Medical Research Council MC_UP_1201/19NIGMS NIH HHS R35 GM122579Wellcome Trust 226015
6 · The paper itself

Abstract

Telomerase ribonucleoprotein (RNP) synthesizes telomeric repeats at chromosome ends using a telomerase reverse transcriptase (TERT) and a telomerase RNA (hTR in humans). Previous structural work showed that human telomerase is typically monomeric, containing a single copy of TERT and hTR. Evidence for dimeric complexes exists, although the composition, high-resolution structure, and function remain elusive. Here, we report the cryo-electron microscopy (cryo-EM) structure of a human telomerase dimer bound to telomeric DNA. The structure reveals a 26-subunit assembly and a dimerization interface mediated by the Hinge and ACA box (H/ACA) RNP of telomerase. Premature aging disease mutations map to this interface. Disrupting dimer formation affects RNP assembly, bulk telomerase activity, and telomere maintenance in cells. Our findings address a long-standing enigma surrounding the telomerase dimer and suggest a role for the dimer in telomerase assembly.

Indexed as

TelomeraseCryoelectron MicroscopyDNAHumansMutationProtein MultimerizationRNATelomereDNARNATelomerasetelomerase RNATERT protein, human

Identifiers

PMID40638752
PMCPMC7618144

What OpenQuestion holds

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Registered trials

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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.