コーパス検索結果 (1語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 osyltransferase designated SpyA (S. pyogenes ADP-ribosyltransferase).
2 the C-terminus (residues 232-453) encodes an ADP-ribosyltransferase.
3 ibose antibodies, suggesting that Sir2 is an ADP-ribosyltransferase.
4 ivation of phospholipase D and cholera toxin ADP-ribosyltransferase.
5 in blocking ARF stimulation of cholera toxin ADP-ribosyltransferase.
6 he potential for ExoS to function as an ecto-ADP-ribosyltransferase.
7 was characterized as a diphthamide dependent ADP-ribosyltransferase.
8 he ability of 14-3-3 to activate exoenzyme S ADP-ribosyltransferase.
9 express on their surfaces arginine-specific ADP ribosyltransferases.
10 h the enzymatic activity of deacetylases and ADP ribosyltransferases.
11 oiety into hydrophobic subpockets in various ADP-ribosyltransferases.
12 y link between bacterial and vertebrate mono-ADP-ribosyltransferases.
13 nzylguanidine, inhibitors of endogenous mono-ADP-ribosyltransferases.
14 o-ADP-ribosyltransferases than the bacterial ADP-ribosyltransferases.
15 t have been attributed to several vertebrate ADP-ribosyltransferases.
16 catalyzed by a family of amino acid-specific ADP-ribosyltransferases.
17 mechanism of NAD binding and catalysis among ADP-ribosyltransferases.
18 omology (DNA or amino acid) with other known ADP-ribosyltransferases.
19 of ADP-ribose are conjugated to proteins by ADP-ribosyltransferases.
20 r tested against a panel of homologous human ADP-ribosyltransferases.
21 ng loops, L1 and L4, not found in other mono-ADP-ribosyltransferases.
24 First, IENK cells express high levels of ADP-ribosyltransferase 2 (a marker of regulatory T cells
25 uitously expressed CD38 and T cell-expressed ADP-ribosyltransferase 2 (ART2) are ectoenzymes competin
27 itive to NAD-induced cell death activated by ADP ribosyltransferase-2 (ART2)-mediated ADP ribosylatio
30 Among these were genes encoding additional ADP-ribosyltransferases, a homolog of SrfC (a candidate
31 hat have two amino acid substitutions in the ADP-ribosyltransferase active center (E112K) and COOH-te
33 ut also carrying out ADP-ribosyl cyclase and ADP-ribosyltransferase activities, making SPN the only b
40 solated B-oligomer subunit of PTX that lacks ADP ribosyltransferase activity nor the related cholera
41 tudy, we have used LFnDTA and its associated ADP-ribosyltransferase activity (DTA) to determine the r
42 e effector proteins include two enzymes with ADP-ribosyltransferase activity (ExoS and ExoT) and an a
43 of mutagenesis were quantified by measuring ADP-ribosyltransferase activity (i.e., auto-ADP-ribosyla
45 protein toxin that has diphthamide-specific ADP-ribosyltransferase activity against eukaryotic elong
46 , inhibition of ARF-stimulated cholera toxin ADP-ribosyltransferase activity and effects of ARF on mu
48 minal domain of ExoS possesses FAS-dependent ADP-ribosyltransferase activity and is cytotoxic to euka
49 by their ability to stimulate cholera toxin ADP-ribosyltransferase activity and later recognized as
50 by their ability to stimulate cholera toxin ADP-ribosyltransferase activity and now recognized as cr
51 ed that V. fischeri hvn null still possessed ADP-ribosyltransferase activity and that this activity i
52 duction of ExoS was monitored by a sensitive ADP-ribosyltransferase activity assay, and specific acti
54 id homology, Exo53 has been shown to express ADP-ribosyltransferase activity at about 0.2% of the spe
55 ExoT also affects PI3K signaling via its ADP-ribosyltransferase activity but does not act directl
56 hat a E379D mutation inhibited expression of ADP-ribosyltransferase activity but had little effect on
58 ase activity, and in J744-Eclone cells, ExoS ADP-ribosyltransferase activity caused a more severe inh
59 protein (GAP) activity, or ExoS defective in ADP-ribosyltransferase activity demonstrated that the vi
61 e protein stimulated cholera-toxin-catalyzed ADP-ribosyltransferase activity in a reaction that was d
62 investigate the structural requirements for ADP-ribosyltransferase activity in human PARP13 and two
63 We suggest that the reported histone/protein ADP-ribosyltransferase activity is a low-efficiency side
66 and purified by their ability to enhance the ADP-ribosyltransferase activity of cholera toxin and mor
67 identified by their ability to stimulate the ADP-ribosyltransferase activity of cholera toxin in vitr
68 ditions, the initial rate of FAS-independent ADP-ribosyltransferase activity of DeltaN222 was not lin
72 Here, two aspects of the activation of the ADP-ribosyltransferase activity of ExoS by 14-3-3 protei
77 nt Exo53 possessed approximately 0.2% of the ADP-ribosyltransferase activity of recombinant ExoS.
78 used NAD analogues and 32P-NAD to study the ADP-ribosyltransferase activity of several different sir
79 other sirtuins, we propose that the reported ADP-ribosyltransferase activity of sirtuins is likely so
80 the factor-activating-exoenzyme-S-dependent ADP-ribosyltransferase activity of the 53-kDa form of ex
81 t, E387A, E399A, and E414A mutants possessed ADP-ribosyltransferase activity similar to that of wild-
82 These findings suggest that Sir2 contains an ADP-ribosyltransferase activity that is essential for it
83 quenced, and deletion analysis localized the ADP-ribosyltransferase activity to one of the three poss
84 cal studies have localized the FAS-dependent ADP-ribosyltransferase activity to the carboxyl-terminus
85 genesis and analyzed both NAD(+) binding and ADP-ribosyltransferase activity using a fluorescence-bas
89 oxin (LT), and LTK63 (an LT mutant devoid of ADP-ribosyltransferase activity) to elicit murine CD8(+)
90 Inactivation of Rab5 was dependent on ExoS ADP-ribosyltransferase activity, and in J744-Eclone cell
91 in after PTX and were dependent on intrinsic ADP-ribosyltransferase activity, as neither the cell bin
92 s not inhibited by mutant LT with attenuated ADP-ribosyltransferase activity, CT B or LT B subunit, w
93 their ability to activate cholera toxin (CT) ADP-ribosyltransferase activity, have a critical role in
95 ither mutant CT nor mutant LTh-1, which lack ADP-ribosyltransferase activity, redirected TT antigen i
112 is concluded that ecto-NAD, as substrate of ADP ribosyltransferase, acts on naive, but not on activa
113 ity domain mutants of exoS revealed that the ADP-ribosyltransferase (ADP-r) activity of ExoS, but not
117 towards Rho family GTPases and a C-terminal ADP ribosyltransferase (ADPRT) domain with minimal activ
119 oS includes both GTPase-activating (GAP) and ADP-ribosyltransferase (ADPRT) activities, and P. aerugi
121 ting (GAP) activity and the carboxy-terminal ADP-ribosyltransferase (ADPRT) activity of ExoS have bee
123 ow-molecular-weight G (LMWG) proteins and an ADP-ribosyltransferase (ADPRT) activity that targets LMW
125 ae is a 591-amino-acid virulence factor with ADP-ribosyltransferase (ADPRT) and vacuolating activitie
131 ently described a cell surface protein, mono-ADP-ribosyltransferase (ADPRT), on cytotoxic T cells and
132 tation as found in the A chain of CRM197, an ADP-ribosyltransferase (ADPrT)-deficient form of DTx, we
134 , that exhibits sequence similarity to known ADP-ribosyltransferases (ADPRTs) such as Bordetella pert
135 This post-translational modification and the ADP-ribosyltransferases (also known as PARPs) responsibl
136 activities from a single Sde polypeptide: an ADP-ribosyltransferase and a nucleotidase/phosphohydrola
137 a bioinformatic strategy as a putative mono-ADP-ribosyltransferase and a possible virulence factor f
138 ble poly(ADP-ribose) polymerase (Tiparp), an ADP-ribosyltransferase and AHR repressor, increases sens
140 e dra operon encodes dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activ
143 e modification of proteins with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolas
145 ic cross talk exists between bacterial toxin ADP-ribosyltransferases and host ADP-ribosylation cycles
148 is pathologic process, PARP-1 and other poly(ADP-ribosyltransferases) are also localized within mitoc
149 y epithelial cells express arginine-specific ADP ribosyltransferase (ART)-1, a GPI-anchored ART that
153 ation is catalyzed by ART2.2, a GPI-anchored ADP-ribosyltransferase (ART) that is constitutively expr
154 presence of NAD-metabolizing enzymes (e.g., ADP-ribosyltransferase (ART)2) on the surface of immune
155 NAD but not ADPR provides the substrate for ADP-ribosyltransferase (ART-2)-mediated attachment of AD
160 and HvnB were presumptively designated mono-ADP-ribosyltransferases (ARTases), and it was hypothesiz
164 rgely mediated by a family of mammalian ecto-ADP-ribosyltransferases (ARTs) that covalently modify ta
166 are similarly ADP-ribosylated by endogenous ADP-ribosyltransferase, but only one arginine is modifie
168 by microinjection of a Clostridium botulinum ADP-ribosyltransferase (C3) and treatment with a ROCK sp
172 mary adenocarcinoma) cells with NAD:arginine ADP-ribosyltransferase cDNAs from Yac-1 murine lymphoma
175 This protein modification is often added by ADP-ribosyltransferases, commonly known as PARPs, but it
176 P gamma ADP-ribosylation, indicates that rod ADP-ribosyltransferase contains two isozymes, and that t
178 se findings reveal links between a mammalian ADP ribosyltransferase, cytokine-regulated metabolic act
180 Streptococcus pyogenes produces a C3 family ADP-ribosyltransferase designated SpyA (S. pyogenes ADP-
181 ed by the DRAT-DRAG (dinitrogenase reductase ADP-ribosyltransferase-dinitrogenase reductase-activatin
182 , independent of the dinitrogenase reductase ADP-ribosyltransferase/dinitrogenase reductase activatin
183 Furthermore, comparing with a bacterial ADP-ribosyltransferase diphtheria toxin, the observed ra
184 nas aeruginosa, which comprises a C-terminal ADP ribosyltransferase domain and an N-terminal Rho GTPa
185 oenzyme S, which represent the FAS-dependent ADP-ribosyltransferase domain (termed deltaN222), and a
186 t form of ExoS rounded cells, indicating the ADP-ribosyltransferase domain alone is sufficient to eli
187 of this study was to define the role of the ADP-ribosyltransferase domain in the modulation of eukar
188 , these data indicate that expression of the ADP-ribosyltransferase domain of exoenzyme S is cytotoxi
189 A single amino acid mutation in the putative ADP-ribosyltransferase domain of SIRT1 inhibits the inte
190 rminus (residues 233-453) is a FAS-dependent ADP-ribosyltransferase domain that targets Ras and Ras-l
191 onal mapping has localized the FAS-dependent ADP-ribosyltransferase domain to the carboxyl-terminus o
201 e-regulating enzymes dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductas
202 form a complex with dinitrogenase reductase ADP-ribosyltransferase (DRAT) from Rhodospirillum rubrum
203 genase reductase and dinitrogenase reductase ADP-ribosyltransferase (DRAT) from Rhodospirillum rubrum
204 sibly inactivated by dinitrogenase reductase ADP-ribosyltransferase (DraT) in response to an increase
205 ionally regulated by dinitrogenase reductase ADP-ribosyltransferase (DRAT) via ADP-ribosylation of th
209 the first structure of a DNA-targeting mono-ADP-ribosyltransferase enzyme; the structures of the apo
211 with a nonphosphorylated protein ligand, the ADP-ribosyltransferase Exoenzyme S (ExoS) from Pseudomon
212 structural genes, exoS, encoding the 49-kDa ADP-ribosyltransferase (ExoS), and exoT, encoding the 53
215 wed that CerADPr possessed several conserved ADP-ribosyltransferase features, including an alpha-3 he
217 other target protein, exoenzyme S (ExoS), an ADP-ribosyltransferase from Pseudomonas aeruginosa.
218 , and initial characterization of a secreted ADP-ribosyltransferase, halovibrin (gene designation hvn
220 re recognized by specific antibodies against ADP-ribosyltransferase in the coronary arterial homogena
221 ences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential
222 tion of P gamma arginine mutants, effects of ADP-ribosyltransferase inhibitors on the P gamma ADP-rib
223 conserved NAD(+)-dependent deacetylases and ADP-ribosyltransferases involved in the regulation of ce
226 3, which is ADP-ribosylated by an endogenous ADP-ribosyltransferase, is required for the phosphorylat
227 seudomonas aeruginosa exoenzyme S (ExoS), an ADP-ribosyltransferase, is translocated into eukaryotic
229 ses a 591-aa virulence factor with both mono-ADP ribosyltransferase (mART) and vacuolating activities
231 is a substrate for two enzyme families, mono-ADP-ribosyltransferases (mARTs) and poly(ADP-ribose) pol
234 ylase activity but functions as an efficient ADP-ribosyltransferase on histones and bovine serum albu
240 gh the activation of the nuclear enzyme poly-ADP ribosyltransferase (PARS) in the pathogenesis of cel
241 s, activating the nuclear repair enzyme poly(ADP)ribosyltransferase (PARS), which results in ADP ribo
243 ermeable pores through which iota a (Ia), an ADP-ribosyltransferase, presumably enters the cytosol.
246 f conserved NAD(+)-dependent deacetylases or ADP-ribosyltransferases, promote longevity in diverse or
247 e catalytic domains of the nuclear-localized ADP-ribosyltransferase proteins (Adprt), two recently id
248 analyses of Tse6 show that it resembles mono-ADP-ribosyltransferase proteins, such as diphtheria toxi
250 e type III-secreted effector HopU1 is a mono-ADP-ribosyltransferase required for full virulence on Ar
251 f membrane proteins on mouse T cells by ecto-ADP-ribosyltransferase(s) (ARTs) can down-regulate proli
254 oning, and deduced amino acid sequence of an ADP-ribosyltransferase secreted from the marine bacteriu
255 owever, inhibition of adenosine diphosphate (ADP) ribosyltransferase significantly decreased the resp
258 cient in the production of the streptococcal ADP-ribosyltransferase SpyA generates lesions of reduced
259 bonded heterohexamers in which the catalytic ADP-ribosyltransferase subunit is activated when exposed
263 amino acid homology with the vertebrate mono-ADP-ribosyltransferases than the bacterial ADP-ribosyltr
264 amily of macrodomain-containing PARPs--is an ADP ribosyltransferase that interacts with Stat6, enhanc
265 acetylases (HDACs), are protein deacetylases/ADP ribosyltransferases that target a wide range of cell
266 tify EspJ as a unique adenosine diphosphate (ADP) ribosyltransferase that directly inhibits Src kinas
268 experiments identify CerADPr as a cytotoxic ADP-ribosyltransferase that disrupts the host cytoskelet
269 subgenomic recombinant Sindbis virus C3), an ADP-ribosyltransferase that inactivates Rho, or dominant
270 s syringae type III effector HopU1 is a mono-ADP-ribosyltransferase that is injected into plant cells
271 a binary toxin consisting of iota a (Ia), an ADP-ribosyltransferase that modifies actin, and iota b (
272 udomonas aeruginosa exoenzyme S (ExoS) is an ADP-ribosyltransferase that modifies low-molecular-weigh
274 SIRT3-5, are NAD(+)-dependent deacylases and ADP-ribosyltransferases that are critical for stress res
277 ily of protein deacetylases, deacylases, and ADP-ribosyltransferases that regulate life span, control
278 er reduced liver injury, and animals lacking ADP-ribosyltransferase, the enzyme that uses NAD to atta
280 xigenic Escherichia coli (ETEC) produces the ADP-ribosyltransferase toxin known as heat-labile entero
284 n of these toxins requires their activity as ADP-ribosyltransferases, transferring the ADP-ribose moi
285 ase features, including an alpha-3 helix, an ADP-ribosyltransferase turn-turn loop, and a "Gln-XXX-Gl
286 tive insecticidal protein 2 (VIP2), an actin ADP-ribosyltransferase, unexpectedly implicates two adja
289 24 mum PJ34, a well known inhibitor of poly-ADP-ribosyltransferases, was shown to be the most potent
290 unusual target for modification by bacterial ADP-ribosyltransferases, we quantitatively compared the
291 rase (PDE), is ADP-ribosylated by endogenous ADP-ribosyltransferase when P gamma is free or complexed
292 hese data identify ExoS as a biglutamic acid ADP-ribosyltransferase, where E381 is the catalytic resi
293 7) are NAD(+)-dependent protein deacetylases/ADP ribosyltransferases, which play decisive roles in ch
295 Exoenzyme S of Pseudomonas aeruginosa is an ADP-ribosyltransferase, which is secreted via a type III
296 e T cells expressing the cell surface enzyme ADP ribosyltransferase with nicotinamide adenine dinucle
297 Sirtuins are a family of deacylases and ADP-ribosyltransferases with clear links to regulation o
298 DP-ribose) polymerase (PARP) family includes ADP-ribosyltransferases with diphtheria toxin homology (
299 was generated in NMU cells by proteolysis of ADP-ribosyltransferase, with release of a carboxyl-termi
300 here the cloning and characterization of an ADP-ribosyltransferase (Yac-2), also from Yac-1 lymphoma
WebLSDに未収録の専門用語(用法)は "新規対訳" から投稿できます。