Marion Jaqueline Skalweit
Affiliations: | Case Western Reserve University School of Medicine, Cleveland, OH, United States |
Area:
infectious diseases; antibiotic resistanceGoogle:
"Marion Skalweit"Mean distance: (not calculated yet)
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Publications
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| Skalweit MJ, Li M. (2016) Bulgecin A as a β-lactam enhancer for carbapenem-resistant Pseudomonas aeruginosa and carbapenem-resistant Acinetobacter baumannii clinical isolates containing various resistance mechanisms. Drug Design, Development and Therapy. 10: 3013-3020 |
| Dumford DM, Skalweit MJ. (2016) Antibiotic-Resistant Infections and Treatment Challenges in the Immunocompromised Host. Infectious Disease Clinics of North America. 30: 465-489 |
| Skalweit MJ. (2016) An unusual case of underlying rilpivirine resistance in an antiretroviral-naïve man with AIDS. International Journal of Std & Aids. 27: 1346-1349 |
| Skalweit MJ. (2015) Profile of ceftolozane/tazobactam and its potential in the treatment of complicated intra-abdominal infections. Drug Design, Development and Therapy. 9: 2919-25 |
| Skalweit MJ, Li M, Taracila MA. (2015) Effect of asparagine substitutions in the YXN loop of a class C β-lactamase of Acinetobacter baumannii on substrate and inhibitor kinetics. Antimicrobial Agents and Chemotherapy. 59: 1472-7 |
| Khatri A, Skalweit MJ. (2015) A rare case of immune reconstitution inflammatory syndrome presenting as secondary syphilis International Journal of Std and Aids. 26: 749-751 |
| Skalweit MJ, Li M, Conklin BC, et al. (2013) N152G, -S, and -T substitutions in CMY-2 β-lactamase increase catalytic efficiency for cefoxitin and inactivation rates for tazobactam. Antimicrobial Agents and Chemotherapy. 57: 1596-602 |
| Li M, Conklin BC, Taracila MA, et al. (2012) Substitutions at position 105 in SHV family β-lactamases decrease catalytic efficiency and cause inhibitor resistance. Antimicrobial Agents and Chemotherapy. 56: 5678-86 |
| Papp-Wallace KM, Senkfor B, Gatta J, et al. (2012) Early insights into the interactions of different β-lactam antibiotics and β-lactamase inhibitors against soluble forms of Acinetobacter baumannii PBP1a and Acinetobacter sp. PBP3. Antimicrobial Agents and Chemotherapy. 56: 5687-92 |
| Ke W, Rodkey EA, Sampson JM, et al. (2012) The importance of the trans-enamine intermediate as a β-lactamase inhibition strategy probed in inhibitor-resistant SHV β-lactamase variants. Chemmedchem. 7: 1002-8 |