Zobrazeno 1 - 10
of 203
pro vyhledávání: '"Merrill Ar"'
Autor:
Merrill Ar, Elke Genersch, Julia Ebeling, Franziska Pieper, Monica Goncalves, Michael McCarthy, Josefine Göbel, Henriette Knispel, Madison Turner
Publikováno v:
Toxins, Vol 13, Iss 607, p 607 (2021)
Toxins
Volume 13
Issue 9
Toxins
Volume 13
Issue 9
American Foulbrood, caused by Paenibacillus larvae, is the most devastating bacterial honey bee brood disease. Finding a treatment against American Foulbrood would be a huge breakthrough in the battle against the disease. Recently, small molecule inh
Autor:
Merrill Ar, Miguel R. Lugo
Publikováno v:
Toxins
Toxins, Vol 13, Iss 16, p 16 (2021)
Toxins, Vol 13, Iss 16, p 16 (2021)
Mono-ADP-ribosyltransferase toxins are often key virulence factors produced by pathogenic bacteria as tools to compromise the target host cell. These toxins are enzymes that use host cellular NAD+ as the substrate to modify a critical macromolecule t
Autor:
Bronwyn Lyons, R. Ravulapalli, Merrill Ar, Miguel R. Lugo, S. Carlin, Debajyoti Dutta, Jason Lanoue
Publikováno v:
Journal of Biological Chemistry. 291:11198-11215
A bioinformatics strategy was used to identify Scabin, a novel DNA-targeting enzyme from the plant pathogen 87.22 strain of Streptomyces scabies Scabin shares nearly 40% sequence identity with the Pierisin family of mono-ADP-ribosyltransferase toxins
Publikováno v:
Journal of biomolecular structuredynamics. 34(12)
C3larvin toxin is a new member of the C3 class of the mono-ADP-ribosyltransferase toxin family. The C3 toxins are known to covalently modify small G-proteins, e.g. RhoA, impairing their function, and serving as virulence factors for an offending path
Autor:
Emil F. Pai, R. Ravulapalli, Danielle D. Visschedyk, Merrill Ar, Robert J. Fieldhouse, Roland Pfoh, Miguel R. Lugo, A. Poole
Publikováno v:
Biochemistry. 54(38)
Vis toxin was identified by a bioinformatics strategy as a putative virulence factor produced by Vibrio splendidus with mono-ADP-ribosyltransferase activity. Vis was purified to homogeneity as a 28 kDa single-domain enzyme and was shown to possess NA
Publikováno v:
Biochemistry. 40:10273-10283
Previously, we characterized the role of the three naturally occurring Trp residues (W-417, -466, and -558) in the catalytic mechanism of the toxin-enzyme produced by Pseudomonas aeruginosa [Beattie and Merrill (1999) J. Biol. Chem. 274, 15646-15654]
Publikováno v:
Biochemical Journal. 340:631-638
Unfolding of the soluble colicin E1 channel peptide was examined with the use of urea as a denaturant; it was shown that it unfolds to an intermediate state in 8.5 M urea, equivalent to a dimeric species previously observed in 4 M guanidinium chlorid
Autor:
Merrill Ar, Bryan Kent Beattie
Publikováno v:
Journal of Biological Chemistry. 274:15646-15654
Single tryptophan mutant proteins of a catalytically active domain III recombinant protein (PE24) from Pseudomonas aeruginosa exotoxin A were prepared by site-directed mutagenesis. The binding of the dinucleotide substrate, NAD+, to the PE24 active s
Autor:
Steer Ba, Merrill Ar
Publikováno v:
Biochemistry. 36:3037-3046
The equilibrium unfolding pathway of the colicin E1 channel peptide was shown in a previous study to involve an unfolding intermediate, stable in approximately 4 M guanidine hydrochloride, which comprised primarily the C-terminal hydrophobic alpha-he
Autor:
Beattie Bk, Merrill Ar
Publikováno v:
Biochemistry. 35:9042-9051
Pseudomonas aeruginosa exotoxin A(ETA) and its C-terminal, enzymatically active fragment (PE40, 375 residues) were studied by high-performance size-exclusion chromatography, steady-state and stopped-flow fluorescence spectroscopy, and circular dichro