J
John B. Rafferty
Researcher at University of Sheffield
Publications - 86
Citations - 3800
John B. Rafferty is an academic researcher from University of Sheffield. The author has contributed to research in topics: Enoyl-acyl carrier protein reductase & Holliday junction. The author has an hindex of 31, co-authored 84 publications receiving 3599 citations. Previous affiliations of John B. Rafferty include University of Nottingham & Durham University.
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Journal ArticleDOI
Molecular basis of triclosan activity
Colin Levy,Anna Roujeinikova,Svetlana E. Sedelnikova,Patrick J. Baker,Antoine R. Stuitje,Antoni R. Slabas,David W. Rice,John B. Rafferty +7 more
TL;DR: It is found that triclosan acts as a site-directed, very potent inhibitor of the enzyme by mimicking its natural substrate.
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A mechanism of drug action revealed by structural studies of enoyl reductase.
Clair Baldock,John B. Rafferty,Svetlana E. Sedelnikova,Patrick J. Baker,Antoine R. Stuitje,Antoni R. Slabas,Timothy Robert Hawkes,David W. Rice +7 more
TL;DR: Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazabadine revealed the formation of a covalent bond between the 2′ hydroxyl of the nicotinamia ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog.
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Triclosan inhibits the growth of Plasmodium falciparum and Toxoplasma gondii by inhibition of apicomplexan Fab I.
Rima McLeod,Stephen P. Muench,John B. Rafferty,Dennis E. Kyle,Ernest Mui,Michael J. Kirisits,Douglas G. Mack,Craig W. Roberts,Benjamin U. Samuel,Russell E. Lyons,Mark Dorris,Wilbur K. Milhous,David W. Rice +12 more
TL;DR: Discovery and characterisation of an apicomplexan Fab I and discovery of triclosan as lead compound provide means to rationally design novel inhibitory compounds.
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Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction.
John B. Rafferty,Svetlana E. Sedelnikova,David J. Hargreaves,Peter J. Artymiuk,Patrick J. Baker,Gary J. Sharples,Akeel A. Mahdi,Robert G. Lloyd,David W. Rice +8 more
TL;DR: The model presented reveals how a RuvAB-junction complex may also accommodate the resolvase RuvC, and reveals how four monomers of RuvA are related by fourfold symmetry in a manner reminiscent of a four-petaled flower.
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Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor.
TL;DR: The three-dimensional crystal structure of met repressor shows a dimer of intertwined monomers, which do not have the helix-turn-helix motif characteristic of other bacterial repressor and activator structures, and is proposed to be a model for binding of several dimers to met operator regions.