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Significance of 14-3-3 Self-Dimerization for Phosphorylation-dependent Target Binding

Data up to Jan 2025

Published2003
Citations114
References47

Total Citations Per Year

Abstract

References (47)

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Calyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo

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Raf-1 Kinase and Exoenzyme S Interact with 14-3-3ζ through a Common Site Involving Lysine 49

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14-3-3 Is Phosphorylated by Casein Kinase I on Residue 233

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A Novel Sphingosine-dependent Protein Kinase (SDK1) Specifically Phosphorylates Certain Isoforms of 14-3-3 Protein

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The 14‐3‐3 protein binds its target proteins with a common site located towards the C‐terminus

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Exoenzyme S binds its cofactor 14-3-3 through a non-phosphorylated motif

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Phosphorylation-independent interaction between 14-3-3 protein and the plant plasma membrane H+-ATPase

2002 • 22 citations

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