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Ian Chopra

Researcher at University of Leeds

Publications -  159
Citations -  13589

Ian Chopra is an academic researcher from University of Leeds. The author has contributed to research in topics: Antibacterial agent & Escherichia coli. The author has an hindex of 56, co-authored 159 publications receiving 12349 citations. Previous affiliations of Ian Chopra include University of Ljubljana & British Society for Antimicrobial Chemotherapy.

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Distribution of Fusidic Acid Resistance Determinants in Methicillin-Resistant Staphylococcus aureus

TL;DR: The distribution of fusB and fusC across several genetic lineages, and their presence on multiple genetic elements, indicates that horizontal transmission of fUSidic acid resistance genes has also played an important role in the increasing prevalence offusidic Acid resistance in MRSA.
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Antimicrobial activity and mechanisms of resistance to cephalosporin P1, an antibiotic related to fusidic acid

TL;DR: Although complete cross-resistance between fusidic acid and cephalosporin P1 was demonstrated, the nature and location of fusA mutations in S. aureus when cep HALP1 was the selective agent frequently differed from those selected with fusIDic acid, which may reflect differences in the interaction of the two antibiotics with the translational apparatus.
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New Approaches to the Control of Infections Caused by Antibiotic-Resistant Bacteria: An Industry Perspective

TL;DR: The emergence of Antibiotic-Resistant Bacteria and its Consequences One of the most remarkable accomplishments of this century has been the successful development of antibiotics for the chemotherapy of bacterial infections.
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Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening.

TL;DR: This work has used the molecular docking programme eHiTS for the virtual screening of 1990 compounds from the National Cancer Institute 'Diversity Set' on MurD and MurF and provided four novel MurD inhibitors and one novel MurF inhibitor.
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Analysis of mutational resistance to trimethoprim in Staphylococcus aureus by genetic and structural modelling techniques

TL;DR: Reduced susceptibility to trimethoprim of DHFR enzymes carrying substitutions L(41)F, F(99)S, F (99)Y and H(150)R appears to result from structural changes that reduce trimethiprim binding to the enzyme, suggesting that the survival of trimETHoprim-resistant strains emerging in the clinic may not be subject to a fitness disadvantage.