Evidence map›Paper›PMID 18082603›Full record

ArticleMolecular cell2007

Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation.

Dragony Fu, Kathleen Collins

Registry-linked trialOpen access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT06732843 (Does Recombinant FSH), which is not on this map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
6.3field-weighted citation impact, top 3% 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.

NCT06732843 recruitingnot on this mapstarted 2025, after this paper: background citation

Does Recombinant FSH (rFSH, i.g. Gonal F®) as Compared to Human Menopausal Gonadotrophin (hMG) Affect Telomere Length of Cumulus Cells During Antral Follicle Growth and Impact Blastocyst Status?

Typeobservational_patient_registrySponsorART Fertility Clinics LLCRan2025 to 2027Enrolled10ConditionsOVARIAN STIMULATION, Telomere Length, Telomere Length, Mean Leukocyte
3 · Its place in the literature

Who cites it

132 citing papers in PubMed, 225 citations in OpenAlex.

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72 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Dragony FuDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3200, USA.
Kathleen Collins
University of California, Berkeley · US

Funding

Molecular Mechanism of X-linked Dyskeratosis CongenitaR01HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2004 to 2017
$4.1M
Biogenesis and Regulation of Human TelomeraseR56HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2008 to 2008
$367k
NHLBI NIH HHS HL079585NHLBI NIH HHS R01 HL079585NHLBI NIH HHS R56 HL079585
6 · The paper itself

Abstract

The identities and roles of proteins associated with human telomerase remain poorly defined. To gain insight, we undertook an affinity purification of endogenously assembled human telomerase complexes. We show that specific subsets of H/ACA, Sm, and hnRNP proteins associate with active and inactive telomerase RNPs, while two NTPase proteins associate preferentially with active enzyme. All three core H/ACA-motif binding proteins are telomerase holoenzyme components essential for RNP accumulation. On the other hand, telomerase RNPs lacking interaction with Sm proteins or hnRNP C remain fully functional for telomere elongation. Curiously, overexpression of either associated hnRNP protein (hnRNP C and hnRNP U) or either NTPase protein (NAT10 and GNL3L) induced telomere shortening. Our findings suggest that endogenous human telomerase complexes are more heterogeneous than those of single-celled eukaryotes, have predominantly shared rather than telomerase-specific proteins, and make numerous regulatory interactions.

Indexed as

AcetyltransferasesCells, CulturedChromatography, AffinityGTP-Binding ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear Ribonucleoprotein UHoloenzymesHumansN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesNuclear ProteinsProtein BindingRibonucleoproteins, Small NuclearRNARNA, Long NoncodingRNA, UntranslatedAcetyltransferasesGNL3L protein, humanGTP-Binding ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear Ribonucleoprotein UHNRNPC protein, humanHoloenzymesNAT10 protein, humanN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesNuclear ProteinsRibonucleoproteins, Small NuclearRNARNA, Long NoncodingRNA, UntranslatedTelomerasetelomerase RNATERT protein, human

Identifiers

PMID18082603
PMCPMC2917595
OpenAlexW2101061969

What OpenQuestion holds

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Read underepoch 390

Registered trials

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.