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- W4211212229 abstract "Many signal transduction events are orchestrated by specific interactions of proteins mediated through discrete phosphopeptide-binding motifs. Although several phosphospecific-binding domains are now known, 14-3-3s were the first proteins recognized to specifically bind a discrete phosphoserine or phosphothreonine motif. The 14-3-3 proteins are a family of ubiquitously expressed, exclusively eukaryotic proteins with an astonishingly large number of binding partners. Consequently, 14-3-3s modulate an enormous and diverse group of cellular processes. The effects of 14-3-3 proteins on their targets can be broadly defined using three categories: (i) conformational change; (ii) physical occlusion of sequence-specific or structural protein features; and (iii) scaffolding. This review will describe the current state of knowledge on 14-3-3 proteins, highlighting several important advances, and will attempt to provide a framework by which 14-3-3 functions can be understood." @default.
- W4211212229 created "2022-02-13" @default.
- W4211212229 creator A5035368724 @default.
- W4211212229 creator A5090685901 @default.
- W4211212229 date "2005-08-09" @default.
- W4211212229 modified "2023-10-18" @default.
- W4211212229 title "14-3-3 Proteins: A Number of Functions for a Numbered Protein" @default.
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