Search Results - "Yates, Susan P"
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1
Exotoxin A-eEF2 complex structure indicates ADP ribosylation by ribosome mimicry
Published in Nature (18-08-2005)“…The bacteria causing diphtheria, whooping cough, cholera and other diseases secrete mono-ADP-ribosylating toxins that modify intracellular proteins. Here, we…”
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2
Structural Basis of the Substrate Specificity of Bifunctional Isocitrate Dehydrogenase Kinase/Phosphatase
Published in Biochemistry (Easton) (27-09-2011)“…Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On…”
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3
Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa
Published in Biochemical journal (01-02-2005)“…The mono-ADPRT (mono-ADP-ribosyltransferase), Pseudomonas aeruginosa ETA (exotoxin A), catalyses the transfer of ADP-ribose from NAD+ to its protein substrate…”
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Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK
Published in Philosophical transactions of the Royal Society of London. Series B. Biological sciences (19-09-2012)“…The switch between the Krebs cycle and the glyoxylate bypass is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK). AceK, a bifunctional enzyme,…”
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Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae
Published in The Journal of biological chemistry (29-10-2004)“…The crystal structure of ADP-ribosylated yeast elongation factor 2 in the presence of sordarin and GDP has been determined at 2.6 Ã resolution. The…”
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Stealth and mimicry by deadly bacterial toxins
Published in Trends in biochemical sciences (Amsterdam. Regular ed.) (01-02-2006)“…Diphtheria toxin and exotoxin A are well-characterized members of the ADP-ribosyltransferase toxin family that function as virulence factors in the pathogenic…”
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Overexpression of cardiac actin with baculovirus is promoter dependent
Published in Archives of biochemistry and biophysics (01-10-2007)“…The influence of the promoter and an N-terminal hexahistidine tag on human cardiac actin (ACTC) expression and function was investigated using four baculovirus…”
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Actin polymerization is controlled by residue size at position 204
Published in Biochemistry and cell biology (01-12-2009)“…Previous work has shown that purified double mutant A204C/C374A yeast actin is polymerization-deficient in vitro under physiological concentrations. To…”
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Characterization of oxidized nicotinamide adenine dinucleotide (NAD +) analogues using a high-pressure-liquid-chromatography-based NAD +-glycohydrolase assay and comparison with fluorescence-based measurements
Published in Analytical biochemistry (01-05-2005)“…A high-pressure-liquid-chromatography (HPLC)-based technique was developed to assess the oxidized nicotinamide adenine dinucleotide (NAD +)-glycohydrolase…”
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10
Elucidation of eukaryotic elongation factor-2 contact sites within the catalytic domain of Pseudomonas aeruginosa exotoxin A
Published in Biochemical journal (01-05-2004)“…Pseudomonas aeruginosa produces the virulence factor, ETA (exotoxin A), which catalyses an ADP-ribosyltransferase reaction of its target protein, eEF2…”
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Insight into the catalytic mechanism of Pseudomonas aeruginosa exotoxin A. Studies of toxin interaction with eukaryotic elongation factor-2
Published in The Journal of biological chemistry (29-11-2002)“…The molecular nature of the protein-protein interactions between the catalytic domain from Pseudomonas aeruginosa exotoxin A (PE24H) and its protein substrate,…”
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12
A Catalytic Loop within Pseudomonas aeruginosa Exotoxin A Modulates Its Transferase Activity
Published in The Journal of biological chemistry (14-09-2001)“…Mutagenesis techniques were used to replace two loop regions within the catalytic domain of Pseudomonas aeruginosa exotoxin A (ETA) with functionally silent…”
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13
Insight into the Catalytic Mechanism of Pseudomonas aeruginosa Exotoxin A
Published in The Journal of biological chemistry (29-11-2002)“…The molecular nature of the protein-protein interactions between the catalytic domain from Pseudomonas aeruginosa exotoxin A (PE24H) and its protein substrate,…”
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