D
David W. Rice
Researcher at University of Sheffield
Publications - 254
Citations - 12437
David W. Rice is an academic researcher from University of Sheffield. The author has contributed to research in topics: Glutamate dehydrogenase & Enzyme. The author has an hindex of 55, co-authored 247 publications receiving 11927 citations. Previous affiliations of David W. Rice include Massey University & Bristol-Myers Squibb.
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Journal ArticleDOI
Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolution
TL;DR: The structure of human lactoferrin has been refined crystallographically at 2.8 A (1 A = 0.1 nm) resolution using restrained least squares methods, and details of the secondary structure and tertiary interactions have been clarified.
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Ferritin: Design and Formation of an Iron-Storage Molecule
G. C. Ford,Pauline M. Harrison,David W. Rice,J. M. A. Smith,Amyra Treffry,J. L. White,J. Yariv +6 more
TL;DR: The structure of horse spleen apoferritin, which has recently been refined, consists of 24 symmetrically related subunits forming a near-spherical hollow shell, and the protein influences both the rate of FeII-oxidation and the form of oxide produced.
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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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Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme.
R. D. Banks,Colin C.F. Blake,Philip R. Evans,Philip R. Evans,R. Haser,R. Haser,David W. Rice,G. W. Hardy,M. Merrett,A. W. Phillips +9 more
TL;DR: The fitting of sequenced peptides to a high-resolution X-ray map of phosphoglycerate kinase has yielded the complete sequence and structure of the horse muscle enzyme.
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The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
Kitty S. P. Yip,Timothy J. Stillman,K.L. Britton,Peter J. Artymiuk,Patrick J. Baker,Svetlana E. Sedelnikova,Paul C. Engel,A. Pasquo,Roberta Chiaraluce,Valerio Consalvi,Roberto Scandurra,David W. Rice +11 more
TL;DR: The structure determination of glutamate dehydrogenase from P. furiosus contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces, which suggest that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.