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pro vyhledávání: '"Stephen J. Hearnshaw"'
Autor:
Lesley A. Mitchenall, Paul J. McDermott, Anthony Maxwell, Lesley A. Howell, Mark Searcey, Michael J. Austin, Stephen J. Hearnshaw
Publikováno v:
MedChemComm. 7:1387-1391
The discovery of new antibiotics with novel modes of action to combat antimicrobial resistance (AMR) is of vital importance. The natural product simocyclinone D8 (SD8) is a potent inhibitor of DNA gyrase. Its bi-functional structure and novel mode of
Autor:
Stephen J. Hearnshaw, Mark J. Buttner, Barrie Wilkinson, Martin Schäfer, Tung B. K. Le, Anthony Maxwell, Gregory L. Challis
Publikováno v:
Journal of Molecular Biology
Simocyclinone D8 (SD8) is a potent DNA gyrase inhibitor produced by Streptomyces antibioticus Tü6040. The simocyclinone (sim) biosynthetic gene cluster has been sequenced and a hypothetical biosynthetic pathway has been proposed. The tetraene linker
Autor:
Anthony Maxwell, Stephen J. Hearnshaw, David M. Lawson, Clare E. M. Stevenson, Terence Tsz-Hong Chung
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
New structures of the N-terminal 43 kDa fragment of the E. coli DNA gyrase B subunit reveal two discrete monovalent cation-binding sites that could have functional roles.
Four new crystal structures of the ATPase domain of the GyrB subunit of Es
Four new crystal structures of the ATPase domain of the GyrB subunit of Es
Autor:
David M. Lawson, Marcus J. Edwards, Anthony Maxwell, Stephen J. Hearnshaw, Clare E. M. Stevenson
Publikováno v:
Journal of Molecular Biology
Simocyclinone D8 (SD8) is an antibiotic produced by Streptomyces antibioticus that targets DNA gyrase. A previous structure of SD8 complexed with the N-terminal domain of the DNA gyrase A protein (GyrA) suggested that four SD8 molecules stabilized a
Autor:
Peter B. Madrid, Kamel Djaout, Victoria Katawera, Hannu Myllykallio, Natassja G. Bush, Hubert F. Becker, Sean Ekins, Stephen J. Hearnshaw, Vinayak Singh, Valerie Mizrahi, Yap Boum, Anthony Maxwell, Pauline Bourbon, Jennifer E. Pritchard
Publikováno v:
Scientific Reports
Scientific Reports, 2016, 6, pp.27792. ⟨10.1038/srep27792⟩
Scientific Reports, Nature Publishing Group, 2016, 6, pp.27792. ⟨10.1038/srep27792⟩
Scientific Reports, 2016, 6, pp.27792. ⟨10.1038/srep27792⟩
Scientific Reports, Nature Publishing Group, 2016, 6, pp.27792. ⟨10.1038/srep27792⟩
There is an urgent need to identify new treatments for tuberculosis (TB), a major infectious disease caused by Mycobacterium tuberculosis (Mtb), which results in 1.5 million deaths each year. We have targeted two essential enzymes in this organism th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::763f239d7bcb00db373cb3988355ece1
https://hal.sorbonne-universite.fr/hal-01332296
https://hal.sorbonne-universite.fr/hal-01332296
Autor:
Stephen J. Hearnshaw, Clare E. M. Stevenson, Dmitry S. Volkov, David M. Lawson, Marina V. Serebryakova, Dmitry Ghilarov, Konstantin Severinov, Anthony Maxwell
Publikováno v:
Structure(London, England:1993)
Summary TldD and TldE proteins are involved in the biosynthesis of microcin B17 (MccB17), an Escherichia coli thiazole/oxazole-modified peptide toxin targeting DNA gyrase. Using a combination of biochemical and crystallographic methods we show that E