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1 ould not interact with other subunits of the transamidase.
2 tion is carried out by an ER enzyme, GPtdIns transamidase.
3 ing the presumed substrate for the yeast GPI transamidase.
4  provide a potential means for isolating the transamidase.
5 gnition of the omega site by the GPI-protein transamidase.
6 ered to be an intermediate in catalysis by a transamidase.
7 udy COOH-terminal processing by the putative transamidase.
8 cadaverine (MDC), which binds to the enzyme (transamidase) active site of tissue transglutaminase (TG
9  Ala abolishes glutaminase and Gln-dependent transamidase activities of Glu-AdT (>300-fold), but reta
10 or ATP-gammaS hydrolysis and glutaminase and transamidase activities reveals tight coupling among the
11 ar to that with ATP, but without concomitant transamidase activity and with a very low level of ATP-g
12                                              Transamidase activity is inhibited by direct inhibitor b
13                                          The transamidase activity potential of factor XIII, measured
14 We recently showed that GTP binding, but not transamidase activity, is required for TG2-dependent can
15 g/GTPase activity, and the open conformation transamidase activity.
16 y at the TG2 transamidase site, inhibit both transamidase and GTP-binding activities.
17 e that the interaction between a protein-GPI transamidase and the COOH-terminal GPI signal sequence p
18 me that catalyzes a large number of amidase, transamidase, and ester hydrolysis reactions.
19  also identify signal recognition by the GPI-transamidase as a potential step for selective small mol
20 or must first undergo cleavage by a putative transamidase between the omega and omega + 1 positions w
21 ons to an open conformation that exposes the transamidase catalytic site involved in protein-protein
22 n near the carboxyl terminus, and a putative transamidase cleavage site in the proprotein.
23 tachment 1) is an essential component of the transamidase complex along with PIGK, PIGS, PIGT, and PI
24 ts of the glycosylphosphatidylinositol (GPI) transamidase complex in human breast cancer.
25     These findings highlight the role of the transamidase complex in the development and function of
26           These results suggest that the GPI transamidase complex is composed of a group of proto-onc
27 osphatidylinositol glycan class U (PIG-U), a transamidase complex unit in the glycosylphosphatidylino
28 he ER-localized glycosylphosphatidylinositol transamidase complex, are retained in the ER.
29 identified subunits of the mammalian GPtdIns transamidase complex.
30 Genetic studies with yeast indicate that the transamidase consists of a dynamic complex of at least t
31 ryl alkylating reagents, suggesting that the transamidase enzyme contains a functionally important su
32 rexpression of different subunits of the GPI transamidase, from strong suppression by Gpi8p and Gpi17
33 I) anchoring of proteins is catalyzed by GPI transamidase (GPIT), a multisubunit, endoplasmic reticul
34           Glycosylphosphatidylinositol (GPI) transamidase (GPIT), the enzyme that attaches GPI anchor
35 iple subunit enzyme complex known as the GPI transamidase (GPIT).
36 rocessed in the endoplasmic reticulum by GPI transamidase (GPIT).
37  reticulum membrane, and GPI-anchored by GPI transamidase (GPIT).
38 GPI-attachment signal can be modified by the transamidase irrespective of whether it is first release
39 ant K cells are defective in part of the GPI transamidase machinery.
40 r glycosylphosphatidylinositol (GPI):protein transamidase, metacaspase and separase, and their differ
41 gs with HDZ provide further evidence for the transamidase nature of the enzyme and also provide a sta
42   These results suggest the carboxy-terminal transamidase recognizes a more extended structure simila
43 blocked because inhibitor interaction at the transamidase site locks the protein in the extended/open
44 inhibited by direct inhibitor binding at the transamidase site, and GTP binding is blocked because in
45  and VA5, which react exclusively at the TG2 transamidase site, inhibit both transamidase and GTP-bin
46                  These findings suggest that transamidase site-specific inhibitors can inhibit GTP bi
47              However, we were surprised that transamidase site-specific inhibitors reduce cancer stem
48 w that proproteins can be crosslinked to the transamidase subunit Gpi8p, as well as to ER proteins of
49 strate and one of the genetically identified transamidase subunits.
50                       In addition to being a transamidase, TG undergoes a GTP-binding/GTPase cycle ev
51 r coordinated coupling of Gln hydrolysis and transamidase transition states during catalysis, and val
52 ach by isolating binders toward Sortase A, a transamidase which is required for virulence of Staphylo
53 s suggest that Gab1p is a subunit of the GPI transamidase with distinct relationships to other subuni

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