Structurally Constrained Residues Outside the Binding Motif Are Essential in the Interaction of 14-3-3 and Phosphorylated Partner
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference20 articles.
1. The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development;Morrison;Trends Cell Biol.,2009
2. Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins;Bustos;Proteins,2006
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4. Restricted mobility of conserved residues in protein–protein interfaces in molecular simulations;Yogurtcu;Biophys. J.,2008
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1. The Integration of Proteome-Wide PTM Data with Protein Structural and Sequence Features Identifies Phosphorylations that Mediate 14-3-3 Interactions;Journal of Molecular Biology;2023-01
2. Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins;Biochemical and Biophysical Research Communications;2021-09
3. 14‐3‐3β isoform is specifically acetylated at Lys51 during differentiation to the osteogenic lineage;Journal of Cellular Biochemistry;2021-08-11
4. 14-3-3ε protein-loaded 3D hydrogels favor osteogenesis;Journal of Materials Science: Materials in Medicine;2020-11
5. YWHAE/14-3-3ε expression impacts the protein load, contributing to proteasome inhibitor sensitivity in multiple myeloma;Blood;2020-07-23
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