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1 alpha in the cytosol of cells overexpressing TGase 2.
2 e as well as I-kappaBalpha polymerization by TGase 2.
3 minor extent by TGase 1, and probably not by TGase 2.
7 l lines, whereas the expression of wild-type TGase-2 and the GTP hydrolysis-defective mutant was sust
8 ies that in fact three members, the TGase 1, TGase 2, and TGase 3 enzymes, and are differentially exp
9 mer's patients, encoding a truncated form of TGase-2 (called TGase-S), shows strong apoptotic activit
10 y shown that calcium-activated TGase 3, like TGase 2, can bind, hydrolyze, and is inhibited by GTP de
15 yme isoforms known in the human genome, only TGase 2 is known to bind and hydrolyze GTP to GDP; bindi
17 the expression of the GTP-binding-defective TGase-2 mutants in different cell lines, whereas the exp
20 e demonstrated previously that inhibitors of TGase 2 reduce nitric oxide (NO) generation in a lipopol
21 chondrial/mitoplast TGase activity is due to TGase 2, the TGase isoform responsible for the majority
22 s, at least three of which, namely, TGase 1, TGase 2 (tissue transglutaminase), and TGase 3, are pres
23 in and gene expression for transglutaminase (TGase 2; tissue transglutaminase (tTG)) in hippocampus a
25 GTP-binding capability of full-length human TGase-2 would prevent it from conferring protection agai
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