Novel, tightly structurally related N-myristoyltransferase inhibitors display equally potent yet distinct inhibitory mechanisms-Reference-Cited by-同舟云学术

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Novel, tightly structurally related N-myristoyltransferase inhibitors display equally potent yet distinct inhibitory mechanisms

Published:2024-08 Issue: Volume: Page:
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Rivière Frédéric,Dian Cyril,Dutheil Rémi F.,Monassa Paul,Giglione Carmela,Meinnel Thierry^ORCID

Publisher

Elsevier BV

Reference75 articles.

1. Myristoylation, an ancient protein modification mirroring eukaryogenesis and evolution;Meinnel;Trends Biochem. Sci.,2020

2. Mapping the myristoylome through a complete understanding of protein myristoylation biochemistry;Giglione;Prog. Lipid Res.,2022

3. N-Myristoyltransferase as a glycine and lysine myristoyltransferase in cancer, immunity, and infections;Kosciuk;ACS Chem. Biol.,2020

4. NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle;Kosciuk;Nat. Commun.,2020

5. Structural and large-scale analysis unveil the intertwined paths promoting NMT-catalyzed lysine and glycine myristoylation;Rivière;J. Mol. Biol.,2022

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