Front Cover: Chromenone Derivatives as CRM1 Inhibitors for Targeting Glioblastoma (ChemBioChem 15/2025)

The cover image illustrates the inhibition of the nuclear export receptor CRM1 by a small molecule inhibitor (in red) that covalently binds to cysteine at position 528. CRM1, a ring-shaped protein, is overexpressed in several human cancers, including glioblastoma (GBM). Its inhibition can disrupt three key oncogenic signaling pathways that drive GBM progression. CRM1 facilitates the nuclear export of proteins containing a nuclear export signal through the nuclear pore complex (depicted in yellow), which is embedded in the nuclear envelope, from the nucleus to the cytoplasm. More details can be found in the article 10.1002/cbic.202500195 by Wolfgang Link and co-workers.

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Publication Details

Journal
ChemBioChem
Published
2025-08-22
DOI
https://doi.org/10.1002/cbic.70013
Primary Topic
Multicomponent Synthesis of Heterocycles
Type
article
Field-Weighted Citation Impact
0.00
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article

Front Cover: Chromenone Derivatives as CRM1 Inhibitors for Targeting Glioblastoma (ChemBioChem 15/2025)

Salvatore Princiotto, Wolfgang Link, Bruno Paiva dos Santos, João G. N. Sequeira et al.
ChemBioChem
Multicomponent Synthesis of Heterocycles
article

Front Cover: Chromenone Derivatives as CRM1 Inhibitors for Targeting Glioblastoma (ChemBioChem 15/2025)

Salvatore Princiotto, Wolfgang Link, Bruno Paiva dos Santos, João G. N. Sequeira, Miguel Machuqueiro, Lucía Domínguez, Lucía Jiménez, Sabrina Dallavalle, Bibiana I. Ferreira, Cristiana Mourato, Alba Orea‐Soufi
article en

Abstract

The cover image illustrates the inhibition of the nuclear export receptor CRM1 by a small molecule inhibitor (in red) that covalently binds to cysteine at position 528. CRM1, a ring-shaped protein, is overexpressed in several human cancers, including glioblastoma (GBM). Its inhibition can disrupt three key oncogenic signaling pathways that drive GBM progression. CRM1 facilitates the nuclear export of proteins containing a nuclear export signal through the nuclear pore complex (depicted in yellow), which is embedded in the nuclear envelope, from the nucleus to the cytoplasm. More details can be found in the article 10.1002/cbic.202500195 by Wolfgang Link and co-workers.

ChemBioChemVol. 26(15)
University of Lisbon (PT), University of Milan (IT), Instituto de Investigaciones Biomédicas Sols-Morreale (ES), Universidad Autónoma de Madrid (ES), University of Algarve (PT)
Openalex Percentile: Top 84%
Multicomponent Synthesis of Heterocycles
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