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• W209818230 startingPage "S155" @default.
• W209818230 abstract "Many aspects of protein function regulation require specific protein-protein interactions to carry out the exact biochemical and cellular functions. The highly conserved members of the 14-3-3 protein family mediate such interactions and through binding to hundreds of other proteins provide multitude of regulatory functions, thus playing key roles in many cellular processes. The 14-3-3 protein binding can affect the function of the target protein in many ways including the modulation of its enzyme activity, its subcellular localization, its structure and stability, or its molecular interactions. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin." @default.
• W209818230 created "2016-06-24" @default.
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• W209818230 date "2014-02-12" @default.
• W209818230 modified "2023-10-01" @default.
• W209818230 title "Mechanisms of the 14-3-3 Protein Function: Regulation of Protein Function Through Conformational Modulation" @default.
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• W209818230 doi "https://doi.org/10.33549/physiolres.932659" @default.
• W209818230 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24564655" @default.
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