Phosphorylation-related modification at the dimer interface of 14-3-3ω dramatically alters monomer interaction dynamics
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference47 articles.
1. 14-3-3 proteins in plant physiology
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1. PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae;Nature Communications;2024-09-14
2. Multi-dimensional demarcation of phylogenetic groups of plant 14-3-3 isoforms using biochemical signatures;2024-07-03
3. Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis;Plant And Cell Physiology;2024-05-23
4. Mechanistic insights into the function of 14-3-3 proteins as negative regulators of brassinosteroid signaling in Arabidopsis;2023-10-14
5. Autonomous Synthesis of Functional, Permanently Phosphorylated Proteins for Defining the Interactome of Monomeric 14-3-3ζ;ACS Central Science;2023-04-10
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