ライフサイエンスコーパス: glycohydrolase

1 se)-DRAG (dinitrogenase reductase-activating glycohydrolase).

2 the ADP-HPD binding site of poly(ADP-ribose) glycohydrolase.

3 and used to photoderivatize poly(ADP-ribose) glycohydrolase.

4 as photoaffinity labels for poly(ADP-ribose) glycohydrolase.

5 the formation of aggregates of an 18-kDa NAD glycohydrolase.

6 n acceptor protein, the toxin acts as a NAD+ glycohydrolase.

7 Unlike RT6.2, mRt6.1 was a weak NAD glycohydrolase.

8 e a nicotinamide adenine dinucleotide (NAD+) glycohydrolase.

9 eveal that PARG acts predominantly as an exo-glycohydrolase.

10 2'-P-ADPR by the action of canine spleen NAD glycohydrolase.

11 olymerases or, conversely, upon knockdown of glycohydrolase.

12 fornica ADP-ribosyl cyclase or mammalian NAD glycohydrolase.

13 x without assistance from a mono(ADP-ribose) glycohydrolase.

14 erase (PARP) and removed by poly(ADP-ribose) glycohydrolase.

15 te-binding sites characteristic of family 18 glycohydrolases.

16 polymerases and degraded by poly(ADP-ribose) glycohydrolases.

17 amide mononucleotide, an inhibitor of NAD(+) glycohydrolases.

18 id not possess ADP-ribosyltransferase or NAD glycohydrolase activities and did not elicit a phenotype

19 Increases in serum glycohydrolase activities appear to provide sensitive an

20 transferase, whereas the transferase and NAD glycohydrolase activities of the recombinant Yac-2 prote

21 compare their ADP-ribosyltransferase and NAD glycohydrolase activities.

22 d regions that regulated transferase and NAD glycohydrolase activities.

23 a-helical region reduced transferase and NAD glycohydrolase activities; however, truncation to residu

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

25 DP-ribose) glycohydrolase (PARG), whose endo-glycohydrolase activity generates PAR fragments.

26 These data indicate that the glycohydrolase activity of SPN may not be the only contr

27 The enhanced glycohydrolase activity of the shorter mutants indicates

28 compatible with the conclusion that the NAD glycohydrolase activity was generated in NMU cells by pr

29 t had little effect on the expression of NAD glycohydrolase activity while a E381D mutation inhibited

30 roteins (transferase activity) or water (NAD glycohydrolase activity).

31 Remarkably, despite differences in glycohydrolase activity, all versions of SPN were equall

32 pilin production, biofilm formation, and NAD glycohydrolase activity, demonstrated the role that both

33 ed a complete loss of tissue-associated NAD+ glycohydrolase activity, showing that the classical NAD+

34 recombinant Rt6-2, but not Rt6-1, shows NAD+ glycohydrolase activity, which is inhibited by the argin

35 SPN, a detailed comparison of representative glycohydrolase activity-proficient and -deficient varian

36 main decreased transferase, but enhanced NAD glycohydrolase, activity.

37 anine spleen previously shown to contain NAD glycohydrolase, ADPR cyclase, and cADPR hydrolase activi

38 treatment with recombinant poly(ADP-ribose) glycohydrolase, an enzyme highly specific for ADP-ribose

39 duced by co-incubation with poly(ADP-ribose) glycohydrolase and a PARP inhibitor.

40 ymphoma cells or rabbit muscle increased NAD glycohydrolase and ADP-ribosyltransferase activities.

41 multifunctional enzyme and catalyzes NAD(+) glycohydrolase and base-exchange reactions to produce AD

42 Irradiation of recombinant poly(ADP-ribose) glycohydrolase and low concentrations of [alpha-32P]-8-N

43 somal region encoding secreted toxins NAD(+)-glycohydrolase and streptolysin O.

44 Putative glycohydrolases and an endoglucanase may enable cataboli

45 se activity, showing that the classical NAD+ glycohydrolases and CD38 are likely identical.

46 mia, the systemic release of eight different glycohydrolases and lipid peroxides into serum were dete

47 P-1 are reversed by PARG, a poly(ADP-ribose) glycohydrolase, and are inhibited by ATP.

48 such products, streptolysin O (SLO) and NAD+-glycohydrolase, appear to be functionally linked, in tha

49 We report here that the poly(ADP-ribose) glycohydrolase ARH3 hydrolyzed O-acetyl-ADP-ribose to pr

50 a carboxyl-terminal fragment that possesses glycohydrolase but not transferase activity, i.e. the ca

51 edominantly hydrolyzes it to ADP-ribose (NAD glycohydrolase), but a trace amount of cADPR is also pro

52 erfusion injury (45 minutes of ischemia) the glycohydrolases, but not AST, LDH, and GGT, declined aft

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

54 ial toxin and mammalian transferases and NAD glycohydrolases, consistent with the hypothesis that the

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

56 ation of overall fold amongst mammalian PARG glycohydrolase domains, whilst revealing additional flex

57 se (DRAT)/dinitrogenase reductase-activating glycohydrolase (DRAG) regulatory system.

58 forms of dinitrogenase reductase-activating glycohydrolase (DRAG) with D123A, H142L, H158N, D243G, a

59 iation of dinitrogenase reductase-activating glycohydrolase (DRAG) with membrane proteins of chromato

60 DRAT) and dinitrogenase reductase-activating glycohydrolase (DRAG), from Rhodospirillum rubrum, were

61 ed by the dinitrogenase reductase-activating glycohydrolase (DraG), promoting Fe protein reactivation

62 ansferase-dinitrogenase reductase-activating glycohydrolase (DRAT-DRAG) regulatory system, has been c

63 ansferase/dinitrogenase reductase activating glycohydrolase (DRAT/DRAG) system.

64 unctions exclusively as a strict beta-NAD(+) glycohydrolase during pathogenesis.

65 hibit a sequence match to the active site of glycohydrolase enzymes.

66 erase and dinitrogenase reductase-activating glycohydrolase, enzymes responsible for the reversible i

67 es from Drosophila melanogaster belonging to glycohydrolase family 38, namely Golgi alpha-mannosidase

68 This enzyme has a glycohydrolase family-74 CD that is a specific xylogluca

69 mploys membrane-bound hydrogenases and novel glycohydrolases for hydrogen production from cellulose.

70 owing hepatic ischemic injury; moreover, the glycohydrolases have the added value of serving as predi

71 iated by pathways besides CD38, the main NAD-glycohydrolase in mammals.

72 toxic to Saccharomyces cerevisiae, whereas a glycohydrolase-inactive SPN allowed for viability.

73 SPN is evolving and has diverged into NAD(+) glycohydrolase-inactive variants that correlate with tis

74 d in cytolysin-mediated translocation of NAD-glycohydrolase, including the immunity factor IFS and th

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

76 The rapid release of glycohydrolases into serum was directly proportional to

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

78 in Streptococcus pyogenes proposes that NAD-glycohydrolase is translocated through streptolysin O-ge

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

80 ibose) polymerases, and two poly(ADP-ribose) glycohydrolase isoforms are stress granule components.

81 enzyme and was shown to possess high NAD(+)-glycohydrolase (Km (NAD) = 68 +/- 3 mum; kcat = 94 +/- 2

82 In contrast, levels of poly(ADP-ribose) glycohydrolase mRNA were decreased in NBD hippocampi.

83 istent with the presence of cell surface NAD glycohydrolase (NADase) activities.

84 idylinositol (GPI)-anchored, whereas the NAD glycohydrolase (NADase) activity remained cell-associate

85 e activity, but indirectly through an NAD(+)-glycohydrolase (NADase) activity that releases free, rea

86 ferases in that it exhibited significant NAD glycohydrolase (NADase) activity.

87 with nicotinamide adenine dinucleotide (NAD) glycohydrolase (NADase) and auto-ADP-ribosyltransferase

88 egion encoding the extracellular toxins NAD+-glycohydrolase (NADase) and streptolysin O (SLO).

89 y, SLO mediates the translocation of GAS NAD-glycohydrolase (NADase) into human epithelial cells in v

90 ch proteins, streptolysin O (SLO) and NAD(+)-glycohydrolase (NADase), have been shown to interact fun

91 positive selection and diverging into NAD(+) glycohydrolase (NADase)-active and -inactive subtypes.

92 ardless of M type) and the production of NAD glycohydrolase (NADase).

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

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

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

96 ins deficient in the expression of SLO, NAD+-glycohydrolase or both proteins in the background of a v

97 he interactions of PAR with poly(ADP-ribose) glycohydrolase (PARG) and other binding proteins.

98 ) polymerase-1 (PARP-1) and poly(ADP-ribose) glycohydrolase (PARG) are enzymes that modify target pro

99 The enzyme poly(ADP-ribose) glycohydrolase (PARG) catalyzes the hydrolysis of glycos

100 Polyadenosine diphosphoribose glycohydrolase (PARG) catalyzes the intracellular hydrol

101 of disruption of the murine poly(ADP-ribose) glycohydrolase (PARG) gene unexpectedly causes early emb

102 PAR glycohydrolase (PARG) has been thought to be the only en

103 However, inhibiting its hydrolysis by PAR glycohydrolase (PARG) has therapeutic potential in cance

104 The role of poly(ADP-ribose) (PAR) glycohydrolase (PARG) in the pathophysiology of renal is

105 e) Polymerase 1 (PARP1) and Poly(ADP-ribose) Glycohydrolase (PARG) in vivo.

106 Poly(ADP-ribose) glycohydrolase (PARG) is the only enzyme known to cataly

107 PAR glycohydrolase (PARG) is the only protein capable of spe

108 We also observed that poly(ADP-ribose) glycohydrolase (Parg) loss-of-function, which caused inc

109 ilization of a new target, poly (ADP-ribose) glycohydrolase (PARG) mRNA, by binding a unique sequence

110 gradation of PAR polymer by poly(ADP-ribose) glycohydrolase (PARG) or phosphodiesterase 1 prevents PA

111 s discrete binding interface enables the PAR glycohydrolase (PARG) to completely disassemble the PARP

112 but there is only one known poly(ADP-ribose) glycohydrolase (PARG), a 111-kDa protein that degrades t

113 in turn rapidly degraded by poly(ADP-ribose) glycohydrolase (PARG), a ubiquitously expressed exo- and

114 ent, only a single enzyme, poly (ADP-ribose) glycohydrolase (PARG), has been identified to catalyze A

115 terization of cDNA encoding poly(ADP-ribose) glycohydrolase (PARG), the enzyme responsible for polyme

116 expression and function of poly(ADP-ribose) glycohydrolase (PARG), the primary enzyme responsible fo

117 the deribosylating enzyme poly-(ADP-ribose) glycohydrolase (PARG), which dynamically regulate ADP-ri

118 ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the un

119 AR) polymer is catalysed by poly(ADP-ribose) glycohydrolase (PARG), whose endo-glycohydrolase activit

120 hydrolysis of PAR chains is catalysed by PAR glycohydrolase (PARG).

121 ly be removed by the enzyme poly(ADP-ribose) glycohydrolase (PARG).

122 PAR is degraded by poly(ADP-ribose) glycohydrolase (PARG).

123 e polymer chains by the enzyme poly(ADP-Rib) glycohydrolase (PARG).

124 ADP-ribose by the action of poly(ADP-ribose) glycohydrolase (PARG).

125 rase (PARP) and degraded by poly(ADP-ribose) glycohydrolase (PARG).

126 cloning of TEJ identified a poly(ADP-ribose) glycohydrolase (PARG).

127 stream effector of the PARP/poly(ADP-ribose) glycohydrolase pathway through PARP-dependent formation

128 transglycosidase activity of solubilized NAD glycohydrolase (porcine brain) to incorporate caged nico

129 Preventing PAR formation with PAR glycohydrolase prevents the PAR-dependent inhibition of

130 y, depletion of cytosolic NAD(+) with NAD(+) glycohydrolase produced a block in glycolysis inhibition

131 reptolysin O (SLO) to translocate the NAD(+) glycohydrolase SPN into host cells during infection.

132 Streptococcus pyogenes injects a beta-NAD(+) glycohydrolase (SPN) into the cytosol of an infected hos

133 eptolysin O (SLO) to translocate the NAD(+) -glycohydrolase (SPN) into the host cell during infection

134 The S. pyogenes NAD(+) glycohydrolase (SPN) is a virulence factor that has been

135 The Streptococcus pyogenes NAD(+) glycohydrolase (SPN) is secreted from the bacterial cell

136 ector of the pathway, the S. pyogenes NAD(+) glycohydrolase (SPN), and a second secreted protein, the

137 tion protein, the Streptococcus pyogenes NAD-glycohydrolase (SPN).

138 ansferase-dinitrogenase reductase-activating glycohydrolase) system.

139 activities, making SPN the only beta-NAD(+) glycohydrolase that can catalyze all of these reactions.

140 uracil DNA glycosylase (UDG) is a powerful N-glycohydrolase that cleaves the glycosidic bond of deoxy

141 cto-nicotinamide adenine dinucleotide (NAD+) glycohydrolase that is expressed on multiple hematopoiet

142 se) (PAR), attached to p53 presumably by PAR glycohydrolase, the only reported enzyme to degrade PAR,

143 ow report that SLO-mediated delivery of NAD+-glycohydrolase to the cytoplasm of human keratinocytes r

144 tor of PARP activity, human poly(ADP-ribose) glycohydrolase, was coexpressed with PARP1 or PARP2, yea

145 bserved with ARH1; ARH2 and poly(ADP-ribose) glycohydrolase were inactive.

146 PAR glycohydrolase, which degrades PAR polymer, prevents PAR

147 RT6.1 (RT6.1) and rat RT6.2 (RT6.2) are NAD glycohydrolases, which catalyze auto-ADP-ribosylation, b