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1 californica ADP-ribosyl cyclase or mammalian NAD glycohydrolase.
2 in the formation of aggregates of an 18-kDa NAD glycohydrolase.
3 Unlike RT6.2, mRt6.1 was a weak NAD glycohydrolase.
4 to 2'-P-ADPR by the action of canine spleen NAD glycohydrolase.
5 of an acceptor protein, the toxin acts as a NAD+ glycohydrolase.
6 n to be a nicotinamide adenine dinucleotide (NAD+) glycohydrolase.
7 nicotinamide mononucleotide, an inhibitor of NAD(+) glycohydrolases.
8 D) did not possess ADP-ribosyltransferase or NAD glycohydrolase activities and did not elicit a pheno
9 osyltransferase, whereas the transferase and NAD glycohydrolase activities of the recombinant Yac-2 p
12 alpha-helical region reduced transferase and NAD glycohydrolase activities; however, truncation to re
13 are compatible with the conclusion that the NAD glycohydrolase activity was generated in NMU cells b
14 y but had little effect on the expression of NAD glycohydrolase activity while a E381D mutation inhib
16 ing pilin production, biofilm formation, and NAD glycohydrolase activity, demonstrated the role that
17 showed a complete loss of tissue-associated NAD+ glycohydrolase activity, showing that the classical
18 fied recombinant Rt6-2, but not Rt6-1, shows NAD+ glycohydrolase activity, which is inhibited by the
21 om canine spleen previously shown to contain NAD glycohydrolase, ADPR cyclase, and cADPR hydrolase ac
22 ne lymphoma cells or rabbit muscle increased NAD glycohydrolase and ADP-ribosyltransferase activities
23 y, is a multifunctional enzyme and catalyzes NAD(+) glycohydrolase and base-exchange reactions to pro
26 Two such products, streptolysin O (SLO) and NAD+-glycohydrolase, appear to be functionally linked, i
27 8 predominantly hydrolyzes it to ADP-ribose (NAD glycohydrolase), but a trace amount of cADPR is also
29 cterial toxin and mammalian transferases and NAD glycohydrolases, consistent with the hypothesis that
33 t that SPN is evolving and has diverged into NAD(+) glycohydrolase-inactive variants that correlate w
34 olved in cytolysin-mediated translocation of NAD-glycohydrolase, including the immunity factor IFS an
37 tion in Streptococcus pyogenes proposes that NAD-glycohydrolase is translocated through streptolysin
39 -domain enzyme and was shown to possess high NAD(+)-glycohydrolase (Km (NAD) = 68 +/- 3 mum; kcat = 9
41 phatidylinositol (GPI)-anchored, whereas the NAD glycohydrolase (NADase) activity remained cell-assoc
44 under positive selection and diverging into NAD(+) glycohydrolase (NADase)-active and -inactive subt
45 y ARTase activity, but indirectly through an NAD(+)-glycohydrolase (NADase) activity that releases fr
46 Two such proteins, streptolysin O (SLO) and NAD(+)-glycohydrolase (NADase), have been shown to inter
47 igen with nicotinamide adenine dinucleotide (NAD) glycohydrolase (NADase) and auto-ADP-ribosyltransfe
48 mal region encoding the extracellular toxins NAD+-glycohydrolase (NADase) and streptolysin O (SLO).
49 ivity, SLO mediates the translocation of GAS NAD-glycohydrolase (NADase) into human epithelial cells
53 strains deficient in the expression of SLO, NAD+-glycohydrolase or both proteins in the background o
54 the transglycosidase activity of solubilized NAD glycohydrolase (porcine brain) to incorporate caged
55 nversely, depletion of cytosolic NAD(+) with NAD(+) glycohydrolase produced a block in glycolysis inh
56 ysin Streptolysin O (SLO) to translocate the NAD(+) glycohydrolase SPN into host cells during infecti
57 ysin Streptolysin O (SLO) to translocate the NAD(+) -glycohydrolase (SPN) into the host cell during i
58 thogen Streptococcus pyogenes injects a beta-NAD(+) glycohydrolase (SPN) into the cytosol of an infec
61 own effector of the pathway, the S. pyogenes NAD(+) glycohydrolase (SPN), and a second secreted prote
63 sferase activities, making SPN the only beta-NAD(+) glycohydrolase that can catalyze all of these rea
64 ated ecto-nicotinamide adenine dinucleotide (NAD+) glycohydrolase that is expressed on multiple hemat
65 We now report that SLO-mediated delivery of NAD+-glycohydrolase to the cytoplasm of human keratinocy
66 Rat RT6.1 (RT6.1) and rat RT6.2 (RT6.2) are NAD glycohydrolases, which catalyze auto-ADP-ribosylatio
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