ライフサイエンスコーパス: ADPRT

1 ADPRT activity as well as cell death was suppressed by a

2 that VgrG1 of A. hydrophila possessed actin ADPRT activity associated with its VIP-2 domain and that

3 ssesses key amino acid residues found in all ADPRTs that are essential for ADPRT activity.

4 ontributes to CaP susceptibility and altered ADPRT/PARP-1 enzyme function in response to oxidative da

5 ding to host cells while still exhibiting an ADPRT activity, suggesting that MYPE9110 is a member of

6 on vector effectively caused apoptosis in an ADPRT activity-dependent manner, indicating that ExoS al

7 nisms underlying the effects of ExoS GAP and ADPRT activities on P. aeruginosa internalization and T3

8 uginosa expressing ExoS lacking both GAP and ADPRT activities resulted in the highest level of T3S tr

9 eting and coordinate effects of ExoS GAP and ADPRT activity on Rac1 within the host cell.

10 o possible modulatory roles that the GAP and ADPRT domains might have on the function of each other.

11 Using ExoS-GAP and ADPRT mutants to examine the coordinate effects of the t

12 at MYPE9110 is a member of the family of A-B ADPRT toxins.

13 active site, and similar to most biglutamate ADPRTs, was able to ADP-ribosylate poly-l-arginine.

14 strand of the NAD binding cleft of different ADPRT toxins was compared.

15 An E381A ADPRT mutation revealed that ExoS ADPRT activity was req

16 is rounding was eliminated by an E379A-E381A ADPRT double mutation, implying that residual ADPRT acti

17 outside the ADPRT region are affecting ExoS ADPRT activity.

18 n the increase in active Rac1 caused by ExoS ADPRT activity.

19 udies draw attention to the key role of ExoS ADPRT activity in causing the effects of bacterially tra

20 ull-down assays identified an effect of ExoS ADPRT activity on RalA activation.

21 Inactivation of ExoS ADPRT activity resulted in significantly enhanced T3S tr

22 the cellular basis for the targeting of ExoS ADPRT activity to Rac1, an inverse relationship was obse

23 provide insight into the enhancement of ExoS ADPRT activity within the eukaryotic cell microenvironme

24 tudy not only highlights the ability of ExoS ADPRT to modulate host cell signaling, eventually leadin

25 d T3S translocation, (iii) confirm that ExoS ADPRT activity targeted a cellular substrate that interr

26 An E381A ADPRT mutation revealed that ExoS ADPRT activity was required for effects of ExoS on DNA s

27 bstrates of TTS-translocated ExoS (TTS-ExoS) ADPRT activity include proteins in the Ras superfamily a

28 lls, but not B cells or macrophages, express ADPRT and are able to ADP-ribosylate cell surface protei

29 s found in all ADPRTs that are essential for ADPRT activity.

30 suppressed by an inhibitor specific for mono-ADPRT.

31 D-dependent reactions which may involve mono-ADPRT, function in signal transduction leading to activa

32 concluded that the cell surface protein mono-ADPRT regulates LFA-1 functions.

33 irement for intracellular NAD, activation of ADPRT, and subsequent NAD depletion during apoptosis in

34 vestigate the immunoregulatory importance of ADPRT on normal lymphocytes in vivo, NAD was injected in

35 The higher levels of ADPRT activity of soil isolates reflected both the incre

36 to function became evident upon the loss of ADPRT activity when a conservative Val60-to-leucine muta

37 ld-type ExoS or ExoS defective in GAP and/or ADPRT activity.

38 strains that translocate ExoS having GAP or ADPRT mutations allowed the independent and coordinate f

39 DPRT double mutation, implying that residual ADPRT activity, rather than GAP activity, was effecting

40 Tyr54-to-phenylalanine DTA mutant to retain ADPRT activity.

41 d identity with the ADP-riboslytransferases (ADPRTs) Staphylococcus aureus EDIN and Clostridium botul

42 mily proteins and C-terminal ADP ribosylase (ADPRT) activity toward distinct and non-overlapping set

43 e forms the active site of ADP-ribosylating (ADPRT) toxins, the limited-sequence homology within this

44 s that is dependent on the ADP-ribosylation (ADPRT) activity of a type III secreted protein ExoS.

45 ses and a C-terminal ADP ribosyltransferase (ADPRT) domain with minimal activity towards a synthetic

46 bstrate for the ExoT ADP ribosyltransferase (ADPRT) domain.

47 activating (GAP) and ADP-ribosyltransferase (ADPRT) activities, and P. aeruginosa cells expressing wi

48 activating (GAP) and ADP-ribosyltransferase (ADPRT) activities.

49 the carboxy-terminal ADP-ribosyltransferase (ADPRT) activity of ExoS have been found to target but ex

50 We assessed the ADP-ribosyltransferase (ADPRT) activity of various domains of purified recombina

51 MWG) proteins and an ADP-ribosyltransferase (ADPRT) activity that targets LMWG proteins in the Ras, R

52 igher levels of ExoS ADP-ribosyltransferase (ADPRT) activity were detected in culture supernatants of

53 irulence factor with ADP-ribosyltransferase (ADPRT) and vacuolating activities.

54 ain and a C-terminal ADP-ribosyltransferase (ADPRT) domain.

55 activating (GAP) and ADP-ribosyltransferase (ADPRT) functional domains.

56 The ADP-ribosyltransferase (ADPRT) gene encodes a zinc-finger DNA-binding protein, p

57 ADP-ribosyltransferase (ADPRT) is a glycosylphosphatidylinositol-anchored cell s

58 ed substrates of the ADP-ribosyltransferase (ADPRT) portion of ExoS include low molecular weight G-pr

59 urface protein, mono-ADP-ribosyltransferase (ADPRT), on cytotoxic T cells and showed that it mediates

60 ent protein kinases, ADP-ribosyltransferase (ADPRT/PARP) and tau.

61 similarity to known ADP-ribosyltransferases (ADPRTs) such as Bordetella pertussis pertussis toxin and

62 nal domain encoding the VIP-2 domain, showed ADPRT activity.

63 FA-1 requires expression of the cell surface ADPRT and causes the loss of epitopes recognized by alph

64 Moreover, cells lacking the cell surface ADPRT are not inhibited by NAD in the cell adhesion assa

65 It is suggested that ADPRT regulates T cells on the level of transmembrane si

66 The ADPRT activity of ExoS targeted Ras and RalA but not Rab

67 The ADPRT domain of ExoT induces atypical anoikis by transfo

68 Alternatively, the ADPRT activity of ExoS altered cellular adherence and mo

69 Both the ADPRT and the GAP domain activities contribute to ExoT-i

70 gher percentage of the CaP cases carried the ADPRT 762 AA genotype than controls (4% versus 2%).

71 cterial internalization were observed in the ADPRT mutant forms.

72 role of the aromatic portion of Tyr54 in the ADPRT reaction was confirmed by the ability of a Tyr54-t

73 The lack of amino acid changes in the ADPRT region in association with a higher specific activ

74 sidues 234 to 438) or point mutations of the ADPRT catalytic site (residues 383 to 385) led to distin

75 Deletion of a majority of the ADPRT domain (residues 234 to 438) or point mutations of

76 dation is dependent upon the activity of the ADPRT domain.

77 well conserved, since the expression of the ADPRT-competent ExoS also induced rapid cell death in th

78 ced by P. aeruginosa or residues outside the ADPRT region are affecting ExoS ADPRT activity.

79 cancer-free subjects to demonstrate that the ADPRT 762 A allele contributed to significantly lower ad

80 ollectively, these data demonstrate that the ADPRT domain of ExoT is active in vivo and contributes t

81 dy is the first to provide evidence that the ADPRT V762A-genetic variant contributes to CaP susceptib

82 Together, the ADPRT and the GAP domains make ExoT into a highly versat

83 effects are not seen in cells from which the ADPRT was removed by phospholipase C.

84 ain this property upon transfection with the ADPRT gene.

85 ame deletions and point mutations within the ADPRT domain in order to test whether this domain might

86 how an elevation of ADP-ribosyl transferase (ADPRT) in both the cytosol and nucleus after exposure to

87 r adenosine diphosphate ribosyl transferase (ADPRT)/PARP-1 activities in response to H2O2 in a gene d

88 whether an amino acid substitution variant, ADPRT V762A (T2444C), is associated with prostate cancer