Literature DB >> 30377945

Backbone chemical shift assignments of human 14-3-3σ.

João Filipe Neves1, Isabelle Landrieu2, Hamida Merzougui1, Emmanuelle Boll1, Xavier Hanoulle1, François-Xavier Cantrelle1.   

Abstract

14-3-3 proteins are a group of seven dimeric adapter proteins that exert their biological function by interacting with hundreds of phosphorylated proteins, thus influencing their sub-cellular localization, activity or stability in the cell. Due to this remarkable interaction network, 14-3-3 proteins have been associated with several pathologies and the protein-protein interactions (PPIs) established with a number of partners are now considered promising drug targets. The activity of 14-3-3 proteins is often isoform specific and to our knowledge only one out of seven isoforms, 14-3-3[Formula: see text], has been assigned. Despite the availability of the crystal structures of all seven isoforms of 14-3-3, the additional NMR assignments of 14-3-3 proteins are important for both biological mechanism studies and chemical biology approaches. Herein, we present a robust backbone assignment of 14-3-3σ, which will allow advances in the discovery of potential therapeutic compounds. This assignment is now being applied to the discovery of both inhibitors and stabilizers of 14-3-3 PPIs.

Entities:  

Keywords:  14-3-3 proteins; Drug discovery; NMR resonance assignments; Protein–protein interactions

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Year:  2018        PMID: 30377945     DOI: 10.1007/s12104-018-9860-1

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  2 in total

1.  Selectivity via Cooperativity: Preferential Stabilization of the p65/14-3-3 Interaction with Semisynthetic Natural Products.

Authors:  Madita Wolter; Pim de Vink; João Filipe Neves; Sonja Srdanović; Yusuke Higuchi; Nobuo Kato; Andrew Wilson; Isabelle Landrieu; Luc Brunsveld; Christian Ottmann
Journal:  J Am Chem Soc       Date:  2020-06-23       Impact factor: 15.419

Review 2.  NMR Spectroscopy of supramolecular chemistry on protein surfaces.

Authors:  Peter Bayer; Anja Matena; Christine Beuck
Journal:  Beilstein J Org Chem       Date:  2020-10-09       Impact factor: 2.883

  2 in total

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