Zobrazeno 1 - 10
of 13
pro vyhledávání: '"J. T. Barbieri"'
Autor:
M R, Baldwin, J T, Barbieri
Publikováno v:
Current topics in microbiology and immunology. 291
Initial studies of how bacterial toxins modulate the actin cytoskeleton have focused primarily on the mode of action of these toxins. More recently, studies have addressed the molecular interactions of these toxins with host cell signaling pathways a
Autor:
M, Würtele, E, Wolf, K J, Pederson, G, Buchwald, M R, Ahmadian, J T, Barbieri, A, Wittinghofer
Publikováno v:
Nature structural biology. 8(1)
Pseudomonas aeruginosa is an opportunistic bacterial pathogen. One of its major toxins, ExoS, is translocated into eukaryotic cells by a type III secretion pathway. ExoS is a dual function enzyme that affects two different Ras-related GTP binding pro
Publikováno v:
The Journal of biological chemistry. 269(14)
We report the purification and proteolytic characterization of the 49-kDa form of exoenzyme S and the cloning of the structural gene for the 49-kDa form of exoenzyme S (exoS). The 49-kDa form of exoenzyme S was purified from SDS-polyacrylamide gels.
Autor:
K M, Krueger, J T, Barbieri
Publikováno v:
The Journal of biological chemistry. 268(17)
Pertussis toxin (PT)-catalyzed ADP-ribosylation of transducin (Gt) is stimulated by ATP. In the absence of ATP, PT exhibited an approximately 20-fold lower linear velocity than the recombinant S1 subunit (rS1) in catalyzing the ADP-ribosylation of Gt
Autor:
G. N. Stowe, Kim D. Janda, P. Silhár, N. R. Silvaggi, M. S. Hixon, S. T. Moe, A. R. Jacobson, J. T. Barbieri, K. N. Allen
Publikováno v:
Synfacts. 2010:0502-0502
Publikováno v:
The Journal of biological chemistry. 266(35)
The kinetic constants for the ADP-ribosylation of transducin were determined for the recombinant S1 subunit of pertussis toxin (rS1, composed of 235 amino acids) and two genetically derived deletion peptides, C180 and C195, which are composed of the
Publikováno v:
The Journal of biological chemistry. 266(13)
Trypsin digestion of pertussis toxin (PT) preferentially cleaved the S1 subunit at Arg-218 without detectable degradation of the B oligomer. The fragment produced, termed the tryptic S1 fragment, appears to remain associated with the B oligomer. Chym
Autor:
G, Cortina, J T, Barbieri
Publikováno v:
The Journal of biological chemistry. 266(5)
Purified recombinant S1 subunit of pertussis toxin (rS1) possessed similar NAD glycohydrolase and ADP-ribosyltransferase activities as S1 subunit purified from pertussis toxin. Purified rS1 and C180 peptide, a deletion peptide which contains amino ac
Publikováno v:
The Journal of biological chemistry. 259(24)
Purified diphtheria toxin from various sources contains tightly, but noncovalently, bound nucleotides, the major component of which is adenylyl-(3',5')-uridine 3'-monophosphate (ApUp). We used ApUp radiolabeled with 32P to measure equilibrium dissoci
Publikováno v:
The Journal of biological chemistry. 256(23)
Diphtheria toxin has recently been fractionated into two forms, one of which contains tightly but noncovalently bound nucleotide-like material. Here we report identification of the major nucleotide constituent (comprising 80% of the total extractable