Evidence map›Paper›PMID 37059728›Full record

ArticleNature communications2023

Homology directed telomere clustering, ultrabright telomere formation and nuclear envelope rupture in cells lacking TRF2

Rekha Rai, Kevin Biju, Wenqi Sun, Tori Sodeinde, Amer Al-Hiyasat, Jaida Morgan, Xianwen Ye, Xueqing Li, Yong Chen, Sandy Chang

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.8field-weighted citation impact, top 9% 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, 16 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Rekha RaiDepartment of Laboratory Medicine, Yale University School of Medicine, New Haven, 330 Cedar Street, CT, 06520, USA. rekha.rai@yale.edu.
Kevin BijuDepartment of Laboratory Medicine, Yale University School of Medicine, New Haven, 330 Cedar Street, CT, 06520, USA.
Wenqi SunState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.
Tori SodeindeDepartment of Laboratory Medicine, Yale University School of Medicine, New Haven, 330 Cedar Street, CT, 06520, USA.
Amer Al-HiyasatDepartment of Laboratory Medicine, Yale University School of Medicine, New Haven, 330 Cedar Street, CT, 06520, USA.ORCID http://orcid.org/0000-0003-3565-2423
Jaida MorganDepartment of Laboratory Medicine, Yale University School of Medicine, New Haven, 330 Cedar Street, CT, 06520, USA.
Xianwen YeUniversity of Chinese Academy of Sciences, 100049, Beijing, China.
Xueqing LiState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.
Yong ChenState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.ORCID http://orcid.org/0000-0001-5857-6086
Sandy ChangDepartment of Laboratory Medicine, Yale University School of Medicine, New Haven, 330 Cedar Street, CT, 06520, USA. s.chang@yale.edu.ORCID http://orcid.org/0000-0002-9560-1671
Yale University · USChinese Academy of Sciences · CNJohns Hopkins University · USShanghaiTech University · CN

Funding

Telomere dysfunction induced breast cancer pathogenesisR01CA202816 · NCI · YALE UNIVERSITY · PI CHANG, SANDY S · 2016 to 2020
$1.9M
Role of POT1 in telomere length regulationR01GM141350 · NIGMS · YALE UNIVERSITY · PI CHANG, SANDY S · 2022 to 2024
$1.0M
NCI NIH HHS R01 CA202816NIGMS NIH HHS 5R01GM141350NIGMS NIH HHS R01 GM141350
6 · The paper itself

Abstract

Double-strand breaks (DSBs) due to genotoxic stress represent potential threats to genome stability. Dysfunctional telomeres are recognized as DSBs and are repaired by distinct DNA repair mechanisms. RAP1 and TRF2 are telomere binding proteins essential to protect telomeres from engaging in homology directed repair (HDR), but how this occurs remains unclear. In this study, we examined how the basic domain of TRF2 (TRF2

Indexed as

Nuclear EnvelopeTelomeric Repeat Binding Protein 2Lamin Type Arap1 GTP-Binding ProteinsTelomereTelomere-Binding ProteinsLamin Type Arap1 GTP-Binding ProteinsTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2

Identifiers

PMID37059728
PMCPMC10104862
OpenAlexW4365509174

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.