Evidence map›Paper›PMID 34188089›Full record

ArticleScientific reports2021

Constrained G4 structures unveil topology specificity of known and new G4 binding proteins.

A Pipier, A Devaux, T Lavergne, A Adrait, Y Couté, S Britton, P Calsou, J F Riou, E Defrancq, D Gomez

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

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  16. The Relevance of G-Quadruplexes for DNA Repair.International journal of molecular sciences · 2021
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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

10 authors at 2 institutions in 1 country.

A PipierInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.
A DevauxDépartement de Chimie Moléculaire, UMR CNRS 5250, Université Grenoble Alpes, 38058, Grenoble, France.
T LavergneDépartement de Chimie Moléculaire, UMR CNRS 5250, Université Grenoble Alpes, 38058, Grenoble, France.ORCID 0000-0002-0029-0015
A AdraitCEA, INSERM, IRIG, BGE, Université Grenoble Alpes, 38000, Grenoble, France.ORCID 0000-0002-1565-2859
Y CoutéCEA, INSERM, IRIG, BGE, Université Grenoble Alpes, 38000, Grenoble, France.ORCID 0000-0003-3896-6196
S BrittonInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID 0000-0002-7008-5316
P CalsouInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID 0000-0001-7951-9806
J F RiouStructure et Instabilité des Génomes, Muséum National d'Histoire Naturelle, CNRS, INSERM, CP 26, 75005, Paris, France.ORCID 0000-0002-0055-6506
E DefrancqDépartement de Chimie Moléculaire, UMR CNRS 5250, Université Grenoble Alpes, 38058, Grenoble, France.ORCID 0000-0002-3911-6241
D GomezInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France. dennis.gomez@ipbs.fr.ORCID 0000-0001-9942-1451
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-quadruplexes (G4) are non-canonical secondary structures consisting in stacked tetrads of hydrogen-bonded guanines bases. An essential feature of G4 is their intrinsic polymorphic nature, which is characterized by the equilibrium between several conformations (also called topologies) and the presence of different types of loops with variable lengths. In cells, G4 functions rely on protein or enzymatic factors that recognize and promote or resolve these structures. In order to characterize new G4-dependent mechanisms, extensive researches aimed at identifying new G4 binding proteins. Using G-rich single-stranded oligonucleotides that adopt non-controlled G4 conformations, a large number of G4-binding proteins have been identified in vitro, but their specificity towards G4 topology remained unknown. Constrained G4 structures are biomolecular objects based on the use of a rigid cyclic peptide scaffold as a template for directing the intramolecular assembly of the anchored oligonucleotides into a single and stabilized G4 topology. Here, using various constrained RNA or DNA G4 as baits in human cell extracts, we establish the topology preference of several well-known G4-interacting factors. Moreover, we identify new G4-interacting proteins such as the NELF complex involved in the RNA-Pol II pausing mechanism, and we show that it impacts the clastogenic effect of the G4-ligand pyridostatin.

Indexed as

G-QuadruplexesDNA-Binding ProteinsHeLa CellsHumansOligonucleotidesRNA Polymerase IITranscription FactorsDNA-Binding ProteinsNSMF protein, humanOligonucleotidesRNA Polymerase IITranscription Factors

Identifiers

PMID34188089
PMCPMC8241873
OpenAlexW3176438142

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.