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   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
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