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• W2158133029 abstract "One particularly abundant group of modular recognition domains consists of those that bind proline-rich motifs. Such modules, including the SH3, WW, and EVH1 domains, play a critical role in the assembly and regulation of many intracellular signaling complexes. These domains use strikingly similar molecular mechanisms of proline recognition. We discuss some of the potential biological advantages conferred by proline recognition, which may explain its widespread use in signaling." @default.
• W2158133029 created "2016-06-24" @default.
• W2158133029 creator A5006257775 @default.
• W2158133029 creator A5018392486 @default.
• W2158133029 creator A5042376132 @default.
• W2158133029 date "2003-04-22" @default.
• W2158133029 modified "2023-10-16" @default.
• W2158133029 title "The Structure and Function of Proline Recognition Domains" @default.
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• W2158133029 doi "https://doi.org/10.1126/stke.2003.179.re8" @default.
• W2158133029 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12709533" @default.
• W2158133029 hasPublicationYear "2003" @default.
• W2158133029 type Work @default.
• W2158133029 sameAs 2158133029 @default.

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