Kinetics measurements of G-quadruplex binding and unfolding by helicases.

Bruce Chang-Gu, Sneha Venkatesan, Rick Russell

Open access · greenAbstract read

In one paragraph

Article in Methods (San Diego, Calif.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.2field-weighted citation impact, top 53% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

Unwinding process of DNA/RNA quadruplexes by proteins under label-free nanopore monitoring.Nucleic acids research · 2025
Article

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.

Bruce Chang-GuDepartment of Molecular Biosciences, University of Texas at Austin, Austin TX 78712, United States.

Sneha VenkatesanDepartment of Molecular Biosciences, University of Texas at Austin, Austin TX 78712, United States.

Rick RussellDepartment of Molecular Biosciences, University of Texas at Austin, Austin TX 78712, United States. Electronic address: rick_russell@cm.utexas.edu.

The University of Texas at Austin · US

Funding

Mechanisms and Specificity of Proteins that Manipulate DNA and RNA StructureR35GM131777 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Rick Russell · 2019 to 2026

$3.2M

NIGMS NIH HHS R35 GM131777

6 · The paper itself

Abstract

G-quadruplex structures (G4s) form readily in DNA and RNA and play diverse roles in gene expression and other processes, and their inappropriate formation and stabilization are linked to human diseases. G4s are inherently long-lived, such that their timely unfolding depends on a suite of DNA and RNA helicase proteins. Biochemical analysis of G4 binding and unfolding by individual helicase proteins is important for establishing their levels of activity, affinity, and specificity for G4s, including individual G4s of varying sequence and structure. Here we describe a set of simple, accessible methods in which electrophoretic mobility shift assays (EMSA) are used to measure the kinetics of G4 binding, dissociation, and unfolding by helicase proteins. We focus on practical considerations and the pitfalls that are most likely to arise when these methods are used to study the activities of helicases on G4s.

Indexed as

DEAD-box RNA HelicasesG-QuadruplexesDNADNA HelicasesHumansKineticsRNADEAD-box RNA HelicasesDNADNA HelicasesRNADHX36Pre-steady-state kineticsPulse-chase methodsRHAURNA helicase

Identifiers

PMID35483547

DOI10.1016/j.ymeth.2022.04.012

PMCPMC10034854

OpenAlexW4224879713

What OpenQuestion holds

Textmetadata

LicenceTDM

Read underepoch 390

Registered trials

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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.