ライフサイエンスコーパス: NAD glycohydrolase

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

10 ified regions that regulated transferase and NAD glycohydrolase activities.

11 to compare their ADP-ribosyltransferase and NAD glycohydrolase activities.

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

15 to proteins (transferase activity) or water (NAD glycohydrolase activity).

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

19 of target proteins, MYPE9110 demonstrates a NAD-glycohydrolase activity by hydrolyzing NAD.

20 c domain decreased transferase, but enhanced NAD glycohydrolase, activity.

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

24 chromosomal region encoding secreted toxins NAD(+)-glycohydrolase and streptolysin O.

25 drolase activity, showing that the classical NAD+ glycohydrolases and CD38 are likely identical.

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

28 The nicotinamide adenine dinucleotide (NAD) glycohydrolase CD38, which is expressed by neurons,

29 cterial toxin and mammalian transferases and NAD glycohydrolases, consistent with the hypothesis that

30 These results support a model in which NAD+-glycohydrolase contributes to GAS pathogenesis by m

31 t SPN functions exclusively as a strict beta-NAD(+) glycohydrolase during pathogenesis.

32 mediated by pathways besides CD38, the main NAD-glycohydrolase in mammals.

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

35 ked, in that SLO is required for transfer of NAD+-glycohydrolase into epithelial cells.

36 We conclude that NAD+-glycohydrolase is a novel type of bacterial toxin t

37 tion in Streptococcus pyogenes proposes that NAD-glycohydrolase is translocated through streptolysin

38 The effector, SPN (S. pyogenes NAD-glycohydrolase), is capable of producing the potent

39 -domain enzyme and was shown to possess high NAD(+)-glycohydrolase (Km (NAD) = 68 +/- 3 mum; kcat = 9

40 consistent with the presence of cell surface NAD glycohydrolase (NADase) activities.

41 phatidylinositol (GPI)-anchored, whereas the NAD glycohydrolase (NADase) activity remained cell-assoc

42 ransferases in that it exhibited significant NAD glycohydrolase (NADase) activity.

43 (regardless of M type) and the production of NAD glycohydrolase (NADase).

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

50 ART2a (RT6.1) and ART2b (RT6.2) are NAD glycohydrolases (NADases) that are linked to T lymph

51 This model also assumes that the NAD-glycohydrolase (nga) and streptolysin O (slo) genes

52 However, the effects of NAD+-glycohydrolase on host cells are largely unexplored

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

59 The S. pyogenes NAD(+) glycohydrolase (SPN) is a virulence factor that h

60 The Streptococcus pyogenes NAD(+) glycohydrolase (SPN) is secreted from the bacteri

61 own effector of the pathway, the S. pyogenes NAD(+) glycohydrolase (SPN), and a second secreted prote

62 sduction protein, the Streptococcus pyogenes NAD-glycohydrolase (SPN).

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