Evidence map›Paper›PMID 27407146›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Single-molecule imaging reveals a common mechanism shared by G-quadruplex-resolving helicases.

Ramreddy Tippana, Helen Hwang, Patricia L Opresko, Vilhelm A Bohr, Sua Myong

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

65 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
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  20. Creation and resolution of non-B-DNA structural impediments during replication.Critical reviews in biochemistry and molecular biology · 2022
    Article

5 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

5 authors at 4 institutions in 1 country.

Ramreddy TippanaBiophysics Department, The Johns Hopkins University, Baltimore, MD 21218;
Helen HwangBioengineering Department, University of Illinois, Urbana, IL 61801; Medical Scholars Program, University of Illinois, Urbana, IL 61801;
Patricia L OpreskoDepartment of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA 15213;
Vilhelm A BohrLaboratory of Molecular Gerontology, Biomedical Research Center, Baltimore, MD 21224-6825;
Sua MyongBiophysics Department, The Johns Hopkins University, Baltimore, MD 21218; Bioengineering Department, University of Illinois, Urbana, IL 61801; Physics Frontier Center (Center for Physics of Living Cells), University of Illinois, Urbana, IL 61801 smyong@jhu.edu.
Johns Hopkins University · USUniversity of Illinois Urbana-Champaign · USUniversity of Pittsburgh · USUrbana University · US

Funding

The Function of Werner Syndrome ProteinZIAAG000721 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$7.7M
Quantitative Stepwise Analysis of RNA InterferenceDP2GM105453 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MYONG, SUA · 2012 to 2012
$2.4M
Quantitative Analysis of G-Quadruplex Folding and its Role in Gene ExpressionR01GM115631 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MYONG, SUA · 2016 to 2019
$1.2M
NIGMS NIH HHS DP2 GM105453NIGMS NIH HHS R01 GM115631
6 · The paper itself

Abstract

G-quadruplex (GQ) is a four stranded DNA secondary structure that arises from a guanine rich sequence. Stable formation of GQ in genomic DNA can be counteracted by the resolving activity of specialized helicases including RNA helicase AU (associated with AU rich elements) (RHAU) (G4 resolvase 1), Bloom helicase (BLM), and Werner helicase (WRN). However, their substrate specificity and the mechanism involved in GQ unfolding remain uncertain. Here, we report that RHAU, BLM, and WRN exhibit distinct GQ conformation specificity, but use a common mechanism of repetitive unfolding that leads to disrupting GQ structure multiple times in succession. Such unfolding activity of RHAU leads to efficient annealing exclusively within the same DNA molecule. The same resolving activity is sufficient to dislodge a stably bound GQ ligand, including BRACO-19, NMM, and Phen-DC3. Our study demonstrates a plausible biological scheme where different helicases are delegated to resolve specific GQ structures by using a common repetitive unfolding mechanism that provides a robust resolving power.

Indexed as

G-QuadruplexesBase SequenceCircular DichroismDEAD-box RNA HelicasesDNAHumansModels, MolecularNucleic Acid ConformationProtein BindingProtein ConformationRecQ HelicasesSingle Molecule ImagingSubstrate SpecificityTelomereWerner Syndrome HelicaseBloom syndrome proteinDEAD-box RNA HelicasesDHX36 protein, humanDNARecQ HelicasesWerner Syndrome HelicaseWRN protein, humanBLMG-quadruplexresolving activityRHAUWRN

Identifiers

PMID27407146
PMCPMC4968719
OpenAlexW2470082626

What OpenQuestion holds

Textmetadata
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.