Evidence map›Paper›PMID 22705372›Full record

ArticleMolecular cell2012

Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65.

Mahavir Singh, Zhonghua Wang, Bon-Kyung Koo, Anooj Patel, Duilio Cascio, Kathleen Collins, Juli Feigon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

79 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Type 2 Diabetes From the Perspective of Telomere Biology.Endocrinology, diabetes & metabolism · 2026
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  5. A (Scientific) Lifetime Affair With Nucleic Acids.Journal of molecular biology · 2025
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  14. Progress in 7SK ribonucleoprotein structural biology.Frontiers in molecular biosciences · 2023
    Review
  15. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

19 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

7 authors at 2 institutions in 1 country.

Mahavir SinghDepartment of Chemistry, and the Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095-1569, USA.
Zhonghua Wang
Bon-Kyung Koo
Anooj Patel
Duilio Cascio
Kathleen Collins
Juli Feigon
University of California, Los Angeles · USUniversity of California, Berkeley · US

Funding

STRUCTURE OF TELOMERIC DNA OLIGONUCLEOTIDESR01GM048123 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FEIGON, JULI · 1992 to 2018
$6.4M
STRUCTURE AND FUNCTION OF TELOMERASER01GM054198 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 1996 to 2018
$5.4M
NIGMS NIH HHS R01 GM048123NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

Telomerase is a ribonucleoprotein complex essential for maintenance of telomere DNA at linear chromosome ends. The catalytic core of Tetrahymena telomerase comprises a ternary complex of telomerase RNA (TER), telomerase reverse transcriptase (TERT), and the essential La family protein p65. NMR and crystal structures of p65 C-terminal domain and its complex with stem IV of TER reveal that RNA recognition is achieved by a combination of single- and double-stranded RNA binding, which induces a 105° bend in TER. The domain is a cryptic, atypical RNA recognition motif with a disordered C-terminal extension that forms an α helix in the complex necessary for hierarchical assembly of TERT with p65-TER. This work provides the first structural insight into biogenesis and assembly of TER with a telomerase-specific protein. Additionally, our studies define a structurally homologous domain (xRRM) in genuine La and LARP7 proteins and suggest a general mode of RNA binding for biogenesis of their diverse RNA targets.

Indexed as

Amino Acid SequenceBase SequenceBinding SitesCrystallography, X-RayElectrophoretic Mobility Shift AssayHoloenzymesModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtozoan ProteinsRibonucleoproteinsRNAHoloenzymesProtozoan ProteinsRibonucleoproteinsRNARNA, ProtozoanTelomerasetelomerase RNA

Identifiers

PMID22705372
PMCPMC3398246
OpenAlexW2059422889

What OpenQuestion holds

Textmetadata
LicenceTDM
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.