Evidence map›Paper›PMID 39763191›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.

Pasquale Russomanno, Pasquale Zizza, Linda Cerofolini, Federica D'Aria, Sara Iachettini, Serena Di Vito, Annamaria Biroccio, Jussara Amato, Marco Fragai, Bruno Pagano

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 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

10 authors.

Pasquale RussomannoDepartment of Pharmacy, University of Naples Federico II, Naples, 80131, Italy.
Pasquale ZizzaTranslational Oncology Research Unit, IRCCS-Regina Elena National Cancer Institute, Rome, 00144, Italy.
Linda CerofoliniCERM-CIRMMP and Department of Chemistry "Ugo Schiff", University of Florence, Sesto Fiorentino (FI), 50019, Italy.
Federica D'AriaDepartment of Pharmacy, University of Naples Federico II, Naples, 80131, Italy.
Sara IachettiniTranslational Oncology Research Unit, IRCCS-Regina Elena National Cancer Institute, Rome, 00144, Italy.
Serena Di VitoTranslational Oncology Research Unit, IRCCS-Regina Elena National Cancer Institute, Rome, 00144, Italy.
Annamaria BiroccioTranslational Oncology Research Unit, IRCCS-Regina Elena National Cancer Institute, Rome, 00144, Italy.
Jussara AmatoDepartment of Pharmacy, University of Naples Federico II, Naples, 80131, Italy.ORCID https://orcid.org/0000-0001-6096-3544
Marco FragaiCERM-CIRMMP and Department of Chemistry "Ugo Schiff", University of Florence, Sesto Fiorentino (FI), 50019, Italy.
Bruno PaganoDepartment of Pharmacy, University of Naples Federico II, Naples, 80131, Italy.ORCID https://orcid.org/0000-0002-7716-9010

Funding

Associazione Italiana per la Ricerca sul Cancro 21579Associazione Italiana per la Ricerca sul Cancro 24590European Union NextGenerationEU CN00000041
6 · The paper itself

Abstract

KHSRP (KH-type splicing regulatory protein) is a multifunctional nucleic acid-binding protein that regulates various cellular processes, with critical roles in controlling gene expression. G-quadruplexes (G4s) are noncanonical nucleic acid structures involved in essential cellular activities, including gene expression, and are recognized as potential therapeutic targets in cancer. The biological functions of G4s are mediated by proteins making their formation highly dynamic within cells. Therefore, the recognition of G4s by specific proteins is crucial for modulating physiological and pathological pathways. Given the growing interest in DNA G4s, a deeper understanding of the proteins that interact with them and their molecular recognition is imperative. This study demonstrates that KHSRP binds to these DNA structures. Biophysical analyses provide insights into the thermodynamics, kinetics, and structural aspects of these interactions, showing that G4 structural variability significantly influences KHSRP binding, in which the KH3 protein domain plays a key role. Validation of these interactions in cancer cells further highlights their biological relevance. Notably, the G4 ligand pyridostatin affects KHSRP/G4 interactions both in vitro and in cells, suggesting that small molecules can modulate this molecular recognition. These findings underscore KHSRP's potential role in regulating cellular mechanisms through binding to G4-forming DNA, positioning it as a possible therapeutic target in cancer.

Indexed as

DNAG-QuadruplexesRNA-Binding ProteinsAminoquinolinesHumansPicolinic AcidsProtein BindingThermodynamicsAminoquinolinesDNAPicolinic AcidspyridostatinRNA-Binding Proteinsbiophysical methodsgene promotersG‐quadruplex DNAprotein‐DNA interactions

Identifiers

PMID39763191
PMCPMC11848572

What OpenQuestion holds

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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.