ライフサイエンスコーパス: glycohydrolase

1 ed to as POLtheta], RAD51, poly [ADP-ribose] glycohydrolase).

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

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

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

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

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

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

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

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

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

11 2'-P-ADPR by the action of canine spleen NAD glycohydrolase.

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

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

14 olymerases or, conversely, upon knockdown of glycohydrolase.

15 fornica ADP-ribosyl cyclase or mammalian NAD glycohydrolase.

16 factor, thus classifying it as a beta-NAD(+) glycohydrolase.

17 te-binding sites characteristic of family 18 glycohydrolases.

18 o the previously known six human ADP-ribosyl glycohydrolases.

19 in GSL catabolism, including those encoding glycohydrolases.

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

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

22 rties distinct from those of other bacterial glycohydrolases.

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

24 Increases in serum glycohydrolase activities appear to provide sensitive an

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

26 transcriptomic findings, showing heightened glycohydrolase activities, particularly in mature astroc

27 compare their ADP-ribosyltransferase and NAD glycohydrolase activities.

28 d regions that regulated transferase and NAD glycohydrolase activities.

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

30 ss distinct CTs which both display NAD(P)(+) glycohydrolase activity but belong to different subgroup

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

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

33 TIR-1/SARM1 as a prerequisite for its NAD(+) glycohydrolase activity is strongly conserved across mil

34 ealed that, like mammalian SARM1, the NAD(+) glycohydrolase activity of C. elegans TIR-1 is dramatica

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

36 tation of PARP9 strongly reduced ADP-ribosyl glycohydrolase activity of the respective macrodomains,

37 The enhanced glycohydrolase activity of the shorter mutants indicates

38 y block either multimerization or the NAD(+) glycohydrolase activity of TIR-1/SARM1 fail to induce p3

39 hat both macrodomains display an ADP-ribosyl glycohydrolase activity that is not directed toward spec

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

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

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

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

44 RM1 oligomerization and its intrinsic NAD(+) glycohydrolase activity, and reduces pathogen accumulati

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

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

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

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

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

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

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

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

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

54 , we conclude that BST1 plays a dual role as glycohydrolase and base-exchange enzyme during oral NR s

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

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

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

58 Putative glycohydrolases and an endoglucanase may enable cataboli

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

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

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

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

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

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

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

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

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

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

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

70 One of these, Rv0060 (DNA ADP-ribosyl glycohydrolase, DarG(Mtb) ), functions along with its co

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

86 1 receptor domain protein (TIR-1), an NAD(+) glycohydrolase homologous to mammalian sterile alpha and

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

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

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

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

91 Interestingly, PARG [Poly(ADP-Ribose) Glycohydrolase] inhibitor (PDD00017273) [but not PARP1 i

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

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

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

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

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

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

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

99 creased resistance to human poly(ADP-ribose) glycohydrolase-mediated degradation.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

117 (PARP1) and dePARylation by poly(ADP-ribose) glycohydrolase (PARG) are equally important for the dyna

118 bose) polymerase (PARP) and poly(ADP-ribose) glycohydrolase (PARG) are key enzymes in BER that elonga

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

120 Polyadenosine diphosphoribose glycohydrolase (PARG) catalyzes the intracellular hydrol

121 ) and PARylation removal by poly(ADP-ribose) glycohydrolase (PARG) critically regulate DNA damage res

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

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

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

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

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

127 biopsies are sensitive to a poly(ADP-ribose) glycohydrolase (PARG) inhibitor.

128 Poly (ADP-ribose) glycohydrolase (PARG) is a dePARylating enzyme which pro

129 e recently identified that poly (ADP) ribose glycohydrolase (PARG) is a strong candidate target due t

130 PAR degradation by poly(ADP-ribose) glycohydrolase (PARG) is essential for progression and c

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

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

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

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

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

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

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

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

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

140 dily revealed by inhibiting poly(ADP-ribose) glycohydrolase (PARG), indicating the otherwise transien

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

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

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

144 transferases and removed by poly(ADP-ribose) glycohydrolase (PARG), which plays important roles in DN

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

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

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

148 ts them from degradation by poly(ADP-ribose) glycohydrolase (PARG).

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

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

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

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

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

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

155 se) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs) and plays a key role in multiple

156 se) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs), which remove the modification,

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

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

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

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

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

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

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

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

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

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

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

168 ansferase-dinitrogenase reductase-activating glycohydrolase) system.

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

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

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

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

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

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

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

176 PAR glycohydrolase, which degrades PAR polymer, prevents PAR

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

178 n 1 (SARM1) is a neuronally expressed NAD(+) glycohydrolase whose activity is increased in response t

179 unctionally pleiotropic ectoenzyme CD38 is a glycohydrolase widely expressed on immune and non-hemato

180 Our findings also show that TNT is an NAD(+) glycohydrolase with properties distinct from those of ot