Evidence map›Paper›PMID 36142374›Full record

ArticleInternational journal of molecular sciences2022

In Vitro Characterization of the Physical Interactions between the Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2.

Patricia L Abreu, Yong Woo Lee, Claus M Azzalin

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Kinetic Control of Condensate Function: How the Formation Dynamics of APBs Influence ALT Cancer Telomere Length Heterogeneity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. G-Quadruplexes: Structural Diversity and Emerging Roles in Biomolecular Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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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

3 authors at 1 institution in 1 country.

Patricia L AbreuInstituto de Medicina Molecular João Lobo Antunes (iMM), Faculty of Medicine, University of Lisbon, 1649-028 Lisbon, Portugal.
Yong Woo LeeInstituto de Medicina Molecular João Lobo Antunes (iMM), Faculty of Medicine, University of Lisbon, 1649-028 Lisbon, Portugal.
Claus M AzzalinInstituto de Medicina Molecular João Lobo Antunes (iMM), Faculty of Medicine, University of Lisbon, 1649-028 Lisbon, Portugal.ORCID 0000-0002-9396-1980
University of Lisbon · PT

Funding

Fundação para a Ciência e Tecnologia PTDC/BIA-MOL/6624/2020; PTDC/MED-ONC/7864/2020; PD/BD/128284/2017; COVID/BD/151621/2021LaCaixa Foundation LCF/PR/HP21/52310016Tessellate Bio RC-CMAzzalin
6 · The paper itself

Abstract

RNA-protein interactions drive key cellular pathways such as protein translation, nuclear organization and genome stability maintenance. The human telomeric protein TRF2 binds to the long noncoding RNA TERRA through independent domains, including its N-terminal B domain. We previously demonstrated that TRF2 B domain binding to TERRA supports invasion of TERRA into telomeric double stranded DNA, leading to the formation of telomeric RNA:DNA hybrids. The other telomeric protein TRF1, which also binds to TERRA, suppresses this TRF2-associated activity by preventing TERRA-B domain interactions. Herein, we show that the binding of both TRF1 and TRF2 to TERRA depends on the ability of the latter to form G-quadruplex structures. Moreover, a cluster of arginines within the B domain is largely responsible for its binding to TERRA. On the other side, a patch of glutamates within the N-terminal A domain of TRF1 mainly accounts for the inhibition of TERRA-B domain complex formation. Finally, mouse TRF2 B domain binds to TERRA, similarly to its human counterpart, while mouse TRF1 A domain lacks the inhibitory activity. Our data shed further light on the complex crosstalk between telomeric proteins and RNAs and suggest a lack of functional conservation in mouse.

Indexed as

RNA, Long NoncodingTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2AnimalsDNAGlutamatesHumansMiceTelomereDNAGlutamatesRNA, Long NoncodingTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2G-quadruplexesR-loopsRNA-protein interactionstelomeresTERRATRF1TRF2

Identifiers

PMID36142374
PMCPMC9500956
OpenAlexW4296793936

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.