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1                                              ADPRT activity as well as cell death was suppressed by a
2  and further examined Bxa, a highly abundant ADPRT in Bacteroides.
3  that VgrG1 of A. hydrophila possessed actin ADPRT activity associated with its VIP-2 domain and that
4 ssesses key amino acid residues found in all ADPRTs that are essential for ADPRT activity.
5 ontributes to CaP susceptibility and altered ADPRT/PARP-1 enzyme function in response to oxidative da
6 ding to host cells while still exhibiting an ADPRT activity, suggesting that MYPE9110 is a member of
7 on vector effectively caused apoptosis in an ADPRT activity-dependent manner, indicating that ExoS al
8 nisms underlying the effects of ExoS GAP and ADPRT activities on P. aeruginosa internalization and T3
9 uginosa expressing ExoS lacking both GAP and ADPRT activities resulted in the highest level of T3S tr
10 eting and coordinate effects of ExoS GAP and ADPRT activity on Rac1 within the host cell.
11 o possible modulatory roles that the GAP and ADPRT domains might have on the function of each other.
12                           Using ExoS-GAP and ADPRT mutants to examine the coordinate effects of the t
13 at MYPE9110 is a member of the family of A-B ADPRT toxins.
14 active site, and similar to most biglutamate ADPRTs, was able to ADP-ribosylate poly-l-arginine.
15 strand of the NAD binding cleft of different ADPRT toxins was compared.
16                                     An E381A ADPRT mutation revealed that ExoS ADPRT activity was req
17 is rounding was eliminated by an E379A-E381A ADPRT double mutation, implying that residual ADPRT acti
18  outside the ADPRT region are affecting ExoS ADPRT activity.
19 n the increase in active Rac1 caused by ExoS ADPRT activity.
20 l, these findings reveal a function for ExoS ADPRT in regulating inflammasome subtype usage in neutro
21 udies draw attention to the key role of ExoS ADPRT activity in causing the effects of bacterially tra
22 ull-down assays identified an effect of ExoS ADPRT activity on RalA activation.
23                         Inactivation of ExoS ADPRT activity resulted in significantly enhanced T3S tr
24 the cellular basis for the targeting of ExoS ADPRT activity to Rac1, an inverse relationship was obse
25 provide insight into the enhancement of ExoS ADPRT activity within the eukaryotic cell microenvironme
26 tudy not only highlights the ability of ExoS ADPRT to modulate host cell signaling, eventually leadin
27 d T3S translocation, (iii) confirm that ExoS ADPRT activity targeted a cellular substrate that interr
28   An E381A ADPRT mutation revealed that ExoS ADPRT activity was required for effects of ExoS on DNA s
29 bstrates of TTS-translocated ExoS (TTS-ExoS) ADPRT activity include proteins in the Ras superfamily a
30 lls, but not B cells or macrophages, express ADPRT and are able to ADP-ribosylate cell surface protei
31 s found in all ADPRTs that are essential for ADPRT activity.
32 suppressed by an inhibitor specific for mono-ADPRT.
33 D-dependent reactions which may involve mono-ADPRT, function in signal transduction leading to activa
34 concluded that the cell surface protein mono-ADPRT regulates LFA-1 functions.
35 irement for intracellular NAD, activation of ADPRT, and subsequent NAD depletion during apoptosis in
36 vestigate the immunoregulatory importance of ADPRT on normal lymphocytes in vivo, NAD was injected in
37                         The higher levels of ADPRT activity of soil isolates reflected both the incre
38  to function became evident upon the loss of ADPRT activity when a conservative Val60-to-leucine muta
39 ld-type ExoS or ExoS defective in GAP and/or ADPRT activity.
40  strains that translocate ExoS having GAP or ADPRT mutations allowed the independent and coordinate f
41 DPRT double mutation, implying that residual ADPRT activity, rather than GAP activity, was effecting
42  Tyr54-to-phenylalanine DTA mutant to retain ADPRT activity.
43 d identity with the ADP-riboslytransferases (ADPRTs) Staphylococcus aureus EDIN and Clostridium botul
44 mily proteins and C-terminal ADP ribosylase (ADPRT) activity toward distinct and non-overlapping set
45 e forms the active site of ADP-ribosylating (ADPRT) toxins, the limited-sequence homology within this
46 s that is dependent on the ADP-ribosylation (ADPRT) activity of a type III secreted protein ExoS.
47 ses and a C-terminal ADP ribosyltransferase (ADPRT) domain with minimal activity towards a synthetic
48 bstrate for the ExoT ADP ribosyltransferase (ADPRT) domain.
49 activating (GAP) and ADP-ribosyltransferase (ADPRT) activities, and P. aeruginosa cells expressing wi
50 activating (GAP) and ADP-ribosyltransferase (ADPRT) activities.
51 the carboxy-terminal ADP-ribosyltransferase (ADPRT) activity of ExoS have been found to target but ex
52      We assessed the ADP-ribosyltransferase (ADPRT) activity of various domains of purified recombina
53 MWG) proteins and an ADP-ribosyltransferase (ADPRT) activity that targets LMWG proteins in the Ras, R
54 igher levels of ExoS ADP-ribosyltransferase (ADPRT) activity were detected in culture supernatants of
55 irulence factor with ADP-ribosyltransferase (ADPRT) and vacuolating activities.
56 ain and a C-terminal ADP-ribosyltransferase (ADPRT) domain.
57 activating (GAP) and ADP-ribosyltransferase (ADPRT) functional domains.
58                  The ADP-ribosyltransferase (ADPRT) gene encodes a zinc-finger DNA-binding protein, p
59                      ADP-ribosyltransferase (ADPRT) is a glycosylphosphatidylinositol-anchored cell s
60 ed substrates of the ADP-ribosyltransferase (ADPRT) portion of ExoS include low molecular weight G-pr
61 urface protein, mono-ADP-ribosyltransferase (ADPRT), on cytotoxic T cells and showed that it mediates
62 ent protein kinases, ADP-ribosyltransferase (ADPRT/PARP) and tau.
63           Bacterial ADP-ribosyltransferases (ADPRTs) have been described as toxins involved in pathog
64 similarity to known ADP-ribosyltransferases (ADPRTs) such as Bordetella pertussis pertussis toxin and
65 nal domain encoding the VIP-2 domain, showed ADPRT activity.
66 FA-1 requires expression of the cell surface ADPRT and causes the loss of epitopes recognized by alph
67     Moreover, cells lacking the cell surface ADPRT are not inhibited by NAD in the cell adhesion assa
68                         It is suggested that ADPRT regulates T cells on the level of transmembrane si
69                         Here, we report that ADPRTs are not pathogen restricted but widely prevalent
70            Altogether, our results show that ADPRTs are abundant in the microbiome and act as bacteri
71                                          The ADPRT activity of ExoS targeted Ras and RalA but not Rab
72                                          The ADPRT domain of ExoT induces atypical anoikis by transfo
73                           Alternatively, the ADPRT activity of ExoS altered cellular adherence and mo
74                                     Both the ADPRT and the GAP domain activities contribute to ExoT-i
75 gher percentage of the CaP cases carried the ADPRT 762 AA genotype than controls (4% versus 2%).
76 cterial internalization were observed in the ADPRT mutant forms.
77 role of the aromatic portion of Tyr54 in the ADPRT reaction was confirmed by the ability of a Tyr54-t
78        The lack of amino acid changes in the ADPRT region in association with a higher specific activ
79 sidues 234 to 438) or point mutations of the ADPRT catalytic site (residues 383 to 385) led to distin
80                Deletion of a majority of the ADPRT domain (residues 234 to 438) or point mutations of
81 dation is dependent upon the activity of the ADPRT domain.
82  well conserved, since the expression of the ADPRT-competent ExoS also induced rapid cell death in th
83 ced by P. aeruginosa or residues outside the ADPRT region are affecting ExoS ADPRT activity.
84 cancer-free subjects to demonstrate that the ADPRT 762 A allele contributed to significantly lower ad
85 ollectively, these data demonstrate that the ADPRT domain of ExoT is active in vivo and contributes t
86 dy is the first to provide evidence that the ADPRT V762A-genetic variant contributes to CaP susceptib
87                                Together, the ADPRT and the GAP domains make ExoT into a highly versat
88 effects are not seen in cells from which the ADPRT was removed by phospholipase C.
89 ain this property upon transfection with the ADPRT gene.
90 ame deletions and point mutations within the ADPRT domain in order to test whether this domain might
91 how an elevation of ADP-ribosyl transferase (ADPRT) in both the cytosol and nucleus after exposure to
92 r adenosine diphosphate ribosyl transferase (ADPRT)/PARP-1 activities in response to H2O2 in a gene d
93  whether an amino acid substitution variant, ADPRT V762A (T2444C), is associated with prostate cancer