Angela L. Woods
Novartis
9 Papers
62 Citations
Angela L. Woods is an academic researcher from Novartis. The author has contributed to research in topics: Mutant & Bacterial outer membrane. The author has an hindex of 5, co-authored 7 publications.
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Papers
Identification of elongation factor G as the conserved cellular target of argyrin B.
Beat Nyfeler,Dominic Hoepfner,Deborah Palestrant,Christina A. Kirby,Lewis Whitehead,Robert Yu,Gejing Deng,Ruth E. Caughlan,Angela L. Woods,Adriana K. Jones,S. Whitney Barnes,John R. Walker,Swann Gaulis,Ervan Hauy,Saskia M. Brachmann,Philipp Krastel,Christian Studer,Ralph Riedl,David Estoppey,Thomas Aust,N. Rao Movva,Zuncai Wang,Michael Salcius,Gregory A. Michaud,Gregory McAllister,Leon Murphy,John A. Tallarico,Christine D. Wilson,Charles R. Dean +28 more
TL;DR: It is shown that argyrin B is an antibacterial and cytotoxic agent that inhibits the evolutionarily conserved target EF-G, blocking protein synthesis in bacteria and mitochondrial translation in yeast and mammalian cells.
Fmt bypass in Pseudomonas aeruginosa causes induction of MexXY efflux pump expression.
Ruth E. Caughlan,Shubha Sriram,Denis M. Daigle,Angela L. Woods,Jennifer Buco,Ron L. Peterson,JoAnn Dzink-Fox,Susan Walker,Charles R. Dean +8 more
TL;DR: Transcriptional profiling and/or mexX::lux promoter fusion analysis revealed that fmt and folD mutants were strongly upregulated for mexXY and another gene known to be required for upregulation of the pump, PA5471, which supports the notion that MexXY has a natural physiological function responding to impairment of ribosome function or protein synthesis and that fmt mutation (Fmt bypass) and fol D mutation generate the intracellular mex XY-inducing signal.
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Determinants of Antibacterial Spectrum and Resistance Potential of the Elongation Factor G Inhibitor Argyrin B in Key Gram-Negative Pathogens.
Adriana K. Jones,Angela L. Woods,Kenneth T. Takeoka,Xiaoyu Shen,Jun-Rong Wei,Ruth E. Caughlan,Charles R. Dean +6 more
TL;DR: Argyrins are natural products with antibacterial activity against Gram-negative pathogens, such as Pseudomonas aeruginosa, Burkholderia multivorans, and Stenotrophomonas maltophilia, and it is shown that argyrin B targets elongation factor G (FusA) and activity against P. baumannii was inactive and resistance occurred at high frequency through loss of the sensitive FusA1.
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Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase.
Naomi N. K. Kreamer,Rajiv Chopra,Ruth E. Caughlan,Doriano Fabbro,Eric Fang,Patricia Gee,Ian Hunt,Min Li,Barbara C. Leon,Lionel Muller,Brian Edward Vash,Angela L. Woods,Travis Stams,Charles R. Dean,Tsuyoshi Uehara +14 more
TL;DR: The crystal structure of the LPS heptose kinase WaaP, which is essential for growth of P. aeruginosa, is solved and it is demonstrated that acyl-ACP is required for WAAP protein solubility and kinase function.
Defects in Efflux (oprM), β-Lactamase (ampC), and Lipopolysaccharide Transport (lptE) Genes Mediate Antibiotic Hypersusceptibility of Pseudomonas aeruginosa Strain Z61.
Xiaoyu Shen,Nicole V Johnson,Naomi N. K. Kreamer,S. Whitney Barnes,John R. Walker,Angela L. Woods,David A. Six,Charles R. Dean +7 more
TL;DR: Pseudomonas aeruginosa Z61 showed that disruption of oprM increased susceptibility to pump substrate antibiotics, that inactivation of the inducible β-lactamase gene ampC contributed to β- lactam susceptibility, and that mutation of the lipopolysaccharide transporter gene lptE strongly altered the outer membrane permeability barrier, causing susceptibility to large antibiotics such as rifampin and also to β -lactams.
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