Evidence map›Paper›PMID 31544934›Full record

ArticleNucleic acids research2019

Quantifying the impact of small molecule ligands on G-quadruplex stability against Bloom helicase.

Parastoo Maleki, Golam Mustafa, Prabesh Gyawali, Jagat B Budhathoki, Yue Ma, Kazuo Nagasawa, Hamza Balci

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 24% 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, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Selective Recognition ofACS medicinal chemistry letters · 2024
    Article
  5. Review
  6. Emerging accessibility patterns in long telomeric overhangs.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. 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

7 authors at 2 institutions in 2 countries.

Parastoo MalekiDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Golam MustafaDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Prabesh GyawaliDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Jagat B BudhathokiDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Yue MaDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
Kazuo NagasawaDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
Hamza BalciDepartment of Physics, Kent State University, Kent, OH 44242, USA.
Kent State University · USTokyo University of Agriculture and Technology · JP

Funding

Influence of small molecules on G-quadruplex stability, folding kinetics, and interactions with proteinsR15GM123443 · NIGMS · KENT STATE UNIVERSITY · PI BALCI, HAMZA · 2018 to 2018
$438k
A Single Molecule Exploration of Protein and G-quadruplex InteractionsR15GM109386 · NIGMS · KENT STATE UNIVERSITY · PI BALCI, HAMZA · 2015 to 2015
$346k
NIGMS NIH HHS R15 GM109386NIGMS NIH HHS R15 GM123443
6 · The paper itself

Abstract

G-quadruplex (GQ) stabilizing small molecule (SM) ligands have been used to stabilize human telomeric GQ (hGQ) to inhibit telomerase activity, or non-telomeric GQs to manipulate gene expression at transcription or translation level. GQs are known to inhibit DNA replication unless destabilized by helicases, such as Bloom helicase (BLM). Even though the impact of SM ligands on thermal stability of GQs is commonly used to characterize their efficacy, how these ligands influence helicase-mediated GQ unfolding is not well understood. Three prominent SM ligands (an oxazole telomestatin derivative, pyridostatin, and PhenDC3), which thermally stabilize hGQ at different levels, were utilized in this study. How these ligands influence BLM-mediated hGQ unfolding was investigated using two independent single-molecule approaches. While the frequency of dynamic hGQ unfolding events was used as the metric in the first approach, the second approach was based on quantifying the cumulative unfolding activity as a function of time. All three SM ligands inhibited BLM activity at similar levels, 2-3 fold, in both approaches. Our observations suggest that the impact of SM ligands on GQ thermal stability is not an ideal predictor for their inhibition of helicase-mediated unfolding, which is physiologically more relevant.

Indexed as

G-QuadruplexesHumansLigandsRecQ HelicasesTelomereBloom syndrome proteinLigandsRecQ Helicases

Identifiers

PMID31544934
PMCPMC6847008
OpenAlexW2975215332

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.