D
David I. Roper
Researcher at University of Warwick
Publications - 127
Citations - 3930
David I. Roper is an academic researcher from University of Warwick. The author has contributed to research in topics: Peptidoglycan & FtsZ. The author has an hindex of 34, co-authored 119 publications receiving 3399 citations. Previous affiliations of David I. Roper include Hammersmith Hospital & University of Oxford.
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Journal ArticleDOI
Bacterial cell wall assembly: still an attractive antibacterial target
TL;DR: Recent developments in the availability of peptidoglycan biosynthetic intermediates, the identification of lead compounds for both the earlier cytoplasmic steps and the later lipid-linked steps, and the application of new methods such as structure-based drug design, phage display and surface science are discussed.
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Vancomycin resistance in enterococci: reprogramming of the d-Ala–d-Ala ligases in bacterial peptidoglycan biosynthesis
TL;DR: The enzymes involved in cell-wall biosynthesis are potential targets for combating vancomycin-resistant enterococci as discussed by the authors, and recent biochemical and crystallographic results are providing mechanistic and structural details about some of these targets.
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Phospho-MurNAc-pentapeptide translocase (MraY) as a target for antibacterial agents and antibacterial proteins.
TL;DR: The mechanisms of enzyme inhibition by these agents are discussed, and the state of knowledge regarding the transmembrane structure, active site, and catalytic mechanism of MraY are discussed.
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Understanding the mechanism of ice binding by type III antifreeze proteins.
Alfred A. Antson,Derek Smith,David I. Roper,Sally J. Lewis,Leo S. D. Caves,Chandra S. Verma,Sarah L. Buckley,Peter J. Lillford,Roderick E. Hubbard +8 more
TL;DR: In this paper, a high-resolution X-ray structure of type III antifreeze proteins (AFPs) was refined at 1.15 A resolution with individual anisotropic temperature factors.
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Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases.
H.S. Subramanya,David I. Roper,Z. Dauter,Eleanor J. Dodson,Gideon J. Davies,Keith S. Wilson,Dale B. Wigley +6 more
TL;DR: The region of greatest similarity between the two enzymes is a large pocket that is proposed to be the active site, and the possible role of residues in this pocket is discussed in view of this idea.