Modulators of 14-3-3 Protein–Protein Interactions
Type de document :
Article dans une revue scientifique
URL permanente :
Titre :
Modulators of 14-3-3 Protein–Protein Interactions
Auteur(s) :
Stevers, Loes M. [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Sijbesma, Eline [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Botta, Maurizio [Auteur]
Università degli Studi di Siena = University of Siena [UNISI]
MacKintosh, Carol [Auteur]
University of Dundee
Obsil, Tomas [Auteur]
Landrieu, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Cau, Ylenia [Auteur]
Università degli Studi di Siena = University of Siena [UNISI]
Wilson, Andrew J. [Auteur]
University of Leeds
Karawajczyk, Anna [Auteur]
Eickhoff, Jan [Auteur]
Davis, Jeremy [Auteur]
Hann, Michael [Auteur]
GlaxoSmithKline [Stevenage, UK] [GSK]
O’Mahony, Gavin [Auteur]
AstraZeneca
Doveston, Richard G. [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Brunsveld, Luc [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Ottmann, Christian [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Eindhoven University of Technology [Eindhoven] [TU/e]
Sijbesma, Eline [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Botta, Maurizio [Auteur]
Università degli Studi di Siena = University of Siena [UNISI]
MacKintosh, Carol [Auteur]
University of Dundee
Obsil, Tomas [Auteur]
Landrieu, Isabelle [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Cau, Ylenia [Auteur]
Università degli Studi di Siena = University of Siena [UNISI]
Wilson, Andrew J. [Auteur]
University of Leeds
Karawajczyk, Anna [Auteur]
Eickhoff, Jan [Auteur]
Davis, Jeremy [Auteur]
Hann, Michael [Auteur]
GlaxoSmithKline [Stevenage, UK] [GSK]
O’Mahony, Gavin [Auteur]
AstraZeneca
Doveston, Richard G. [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Brunsveld, Luc [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Ottmann, Christian [Auteur]
Eindhoven University of Technology [Eindhoven] [TU/e]
Titre de la revue :
Journal of medicinal chemistry
Numéro :
61
Pagination :
3755-3778
Date de publication :
2017-10-19
ISSN :
0022-2623
Mot(s)-clé(s) en anglais :
Peptides and proteins
Monomers
Crystal structure
Inhibitors
Inhibition
Monomers
Crystal structure
Inhibitors
Inhibition
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Direct interactions between proteins are essential for the regulation of their functions in biological pathways. Targeting the complex network of protein–protein interactions (PPIs) has now been widely recognized as an ...
Lire la suite >Direct interactions between proteins are essential for the regulation of their functions in biological pathways. Targeting the complex network of protein–protein interactions (PPIs) has now been widely recognized as an attractive means to therapeutically intervene in disease states. Even though this is a challenging endeavor and PPIs have long been regarded as “undruggable” targets, the last two decades have seen an increasing number of successful examples of PPI modulators, resulting in growing interest in this field. PPI modulation requires novel approaches and the integrated efforts of multiple disciplines to be a fruitful strategy. This perspective focuses on the hub-protein 14-3-3, which has several hundred identified protein interaction partners, and is therefore involved in a wide range of cellular processes and diseases. Here, we aim to provide an integrated overview of the approaches explored for the modulation of 14-3-3 PPIs and review the examples resulting from these efforts in both inhibiting and stabilizing specific 14-3-3 protein complexes by small molecules, peptide mimetics, and natural products.Lire moins >
Lire la suite >Direct interactions between proteins are essential for the regulation of their functions in biological pathways. Targeting the complex network of protein–protein interactions (PPIs) has now been widely recognized as an attractive means to therapeutically intervene in disease states. Even though this is a challenging endeavor and PPIs have long been regarded as “undruggable” targets, the last two decades have seen an increasing number of successful examples of PPI modulators, resulting in growing interest in this field. PPI modulation requires novel approaches and the integrated efforts of multiple disciplines to be a fruitful strategy. This perspective focuses on the hub-protein 14-3-3, which has several hundred identified protein interaction partners, and is therefore involved in a wide range of cellular processes and diseases. Here, we aim to provide an integrated overview of the approaches explored for the modulation of 14-3-3 PPIs and review the examples resulting from these efforts in both inhibiting and stabilizing specific 14-3-3 protein complexes by small molecules, peptide mimetics, and natural products.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
RMN et interactions moléculaires
Date de dépôt :
2020-02-12T15:45:01Z
2021-07-13T12:28:08Z
2021-07-13T12:30:44Z
2021-07-13T12:28:08Z
2021-07-13T12:30:44Z
Fichiers
- acs.jmedchem.7b00574.pdf
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