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• W2029381551 abstract "Transglutaminase (TGase) is a family of enzymes that catalyzes cross-linking reaction between glutamine- and lysine residue of substrate proteins in several mammalian biological events. Substrate proteins for TGase and their physiological relevance have been still in research, continuously expanding. In this study, we have established a novel screening system that enables identification of cDNA sequence encoding favorable primary structure as a substrate for tissue-type transglutaminase (TGase 2), a multifunctional and ubiquitously expressing isozyme. By the screening, we identified several T7 phage clones that displayed substrate peptides for TGase 2 as a translated product from human brain cDNA library. Among the selected clones, the C-terminal region of IKAP, IkappaB kinase complex associated protein, appeared as a highly reactive substrate sequence for TGase 2. This system will open possibility of rapid identification of substrate sequences for transglutaminases at a genetic level." @default.
• W2029381551 created "2016-06-24" @default.
• W2029381551 creator A5050243357 @default.
• W2029381551 creator A5055222159 @default.
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• W2029381551 date "2010-09-25" @default.
• W2029381551 modified "2023-10-14" @default.
• W2029381551 title "Screening of substrate peptide sequences for tissue-type transglutaminase (TGase 2) using T7 phage cDNA library" @default.
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• W2029381551 doi "https://doi.org/10.1007/s10616-010-9308-7" @default.
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