Zeitschriftenartikel zum Thema „Lactams“
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Li, Lu, Qiyao Wang, Hui Zhang, Minjun Yang, Mazhar I. Khan und Xiaohui Zhou. „Sensor histidine kinase is a β-lactam receptor and induces resistance to β-lactam antibiotics“. Proceedings of the National Academy of Sciences 113, Nr. 6 (01.02.2016): 1648–53. http://dx.doi.org/10.1073/pnas.1520300113.
Medina, Marjorie B., Dana J. Poole und M. Ranae Anderson. „A Screening Method for β-Lactams in Tissues Hydrolyzed with Penicillinase I and Lactamase II“. Journal of AOAC INTERNATIONAL 81, Nr. 5 (01.09.1998): 963–72. http://dx.doi.org/10.1093/jaoac/81.5.963.
Alves, Américo J. S., Nuno G. Alves, Cátia C. Caratão, Margarida I. M. Esteves, Diana Fontinha, Inês Bártolo, Maria I. L. Soares et al. „Spiro-Lactams as Novel Antimicrobial Agents“. Current Topics in Medicinal Chemistry 20, Nr. 2 (19.02.2020): 140–52. http://dx.doi.org/10.2174/1568026619666191105110049.
Li, Xian-Zhi, Li Zhang, Ramakrishnan Srikumar und Keith Poole. „β-Lactamase Inhibitors Are Substrates for the Multidrug Efflux Pumps of Pseudomonas aeruginosa“. Antimicrobial Agents and Chemotherapy 42, Nr. 2 (01.02.1998): 399–403. http://dx.doi.org/10.1128/aac.42.2.399.
Brilhante, R. S. N., L. G. A. Valente, M. F. G. Rocha, T. J. P. G. Bandeira, R. A. Cordeiro, R. A. C. Lima, J. J. G. Leite et al. „Sesquiterpene Farnesol Contributes to Increased Susceptibility to β-Lactams in Strains of Burkholderia pseudomallei“. Antimicrobial Agents and Chemotherapy 56, Nr. 4 (30.01.2012): 2198–200. http://dx.doi.org/10.1128/aac.05885-11.
Sekiguchi, Jun-ichiro, Koji Morita, Tomoe Kitao, Noboru Watanabe, Mitsuhiro Okazaki, Tohru Miyoshi-Akiyama, Masato Kanamori und Teruo Kirikae. „KHM-1, a Novel Plasmid-Mediated Metallo-β-Lactamase from a Citrobacter freundii Clinical Isolate“. Antimicrobial Agents and Chemotherapy 52, Nr. 11 (02.09.2008): 4194–97. http://dx.doi.org/10.1128/aac.01337-07.
Glen, Karl A., und Iain L. Lamont. „β-lactam Resistance in Pseudomonas aeruginosa: Current Status, Future Prospects“. Pathogens 10, Nr. 12 (18.12.2021): 1638. http://dx.doi.org/10.3390/pathogens10121638.
Li, Fu, Li Wan, Tongyang Xiao, Haican Liu, Yi Jiang, Xiuqin Zhao, Ruibai Wang und Kanglin Wan. „In Vitro Activity of β-Lactams in Combination with β-Lactamase Inhibitors against Mycobacterium tuberculosis Clinical Isolates“. BioMed Research International 2018 (02.07.2018): 1–8. http://dx.doi.org/10.1155/2018/3579832.
Mukhopadhyay, S., und P. Chakrabarti. „Altered permeability and beta-lactam resistance in a mutant of Mycobacterium smegmatis.“ Antimicrobial Agents and Chemotherapy 41, Nr. 8 (August 1997): 1721–24. http://dx.doi.org/10.1128/aac.41.8.1721.
Yin, Jianhua, Yiyang Sun, Yinting Mao, Miao Jin und Haichun Gao. „PBP1a/LpoA but Not PBP1b/LpoB Are Involved in Regulation of the Major β-Lactamase GeneblaAin Shewanella oneidensis“. Antimicrobial Agents and Chemotherapy 59, Nr. 6 (30.03.2015): 3357–64. http://dx.doi.org/10.1128/aac.04669-14.
Asgarali, Azizah, Keith A. Stubbs, Antonio Oliver, David J. Vocadlo und Brian L. Mark. „Inactivation of the Glycoside Hydrolase NagZ Attenuates Antipseudomonal β-Lactam Resistance in Pseudomonas aeruginosa“. Antimicrobial Agents and Chemotherapy 53, Nr. 6 (09.03.2009): 2274–82. http://dx.doi.org/10.1128/aac.01617-08.
Sayed, Alaa R. M., Nirav R. Shah, Kari B. Basso, Manasi Kamat, Yuanyuan Jiao, Bartolome Moya, Dhruvitkumar S. Sutaria et al. „First Penicillin-Binding Protein Occupancy Patterns for 15 β-Lactams and β-Lactamase Inhibitors in Mycobacterium abscessus“. Antimicrobial Agents and Chemotherapy 65, Nr. 1 (26.10.2020): e01956-20. http://dx.doi.org/10.1128/aac.01956-20.
Yuan, Qinghui, Lin He und Hengming Ke. „A Potential Substrate Binding Conformation of β-Lactams and Insight into the Broad Spectrum of NDM-1 Activity“. Antimicrobial Agents and Chemotherapy 56, Nr. 10 (23.07.2012): 5157–63. http://dx.doi.org/10.1128/aac.05896-11.
Tarui, Atsushi, Yukiko Karuo, Kazuyuki Sato, Kentaro Kawai und Masaaki Omote. „Stereoselective Synthesis of Multisubstituted α-fluoro-β-lactams“. Current Organic Chemistry 24, Nr. 18 (18.11.2020): 2169–80. http://dx.doi.org/10.2174/1385272824666200221114707.
Nagira, Yu, Keiko Yamada, Hayato Okade, Nami Senju, Yuko Tsutsumi, Yuji Tabata und Kazuhiko Kato. „1279. In Vitro Activity of Nacubactam (OP0595) Alone and in Combination with β-Lactams against β-Lactamase-Producing Enterobacterales Isolated in Japan“. Open Forum Infectious Diseases 7, Supplement_1 (01.10.2020): S655. http://dx.doi.org/10.1093/ofid/ofaa439.1462.
Srivastava, Nitin. „Key Role of Ionic Liquids in the Cleaner and Greener Synthesis of Lactams“. Research Journal of Chemistry and Environment 26, Nr. 1 (25.12.2021): 125–30. http://dx.doi.org/10.25303/2601rjce125130.
Papp-Wallace, Krisztina M., Baui Senkfor, Julian Gatta, Weirui Chai, Magdalena A. Taracila, Veerabahu Shanmugasundaram, Seungil Han et al. „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, Nr. 11 (20.08.2012): 5687–92. http://dx.doi.org/10.1128/aac.01027-12.
Patel, Twisha S., Vince Marshall, Keith S. Kaye, Aaron Smith, Carol Young, Paul Lephart und Jason M. Pogue. „1600. Susceptibility of β-Lactam-Resistant Pseudomonas aeruginosa to Other β-Lactams: Is There Truly a Lack of Cross-Resistance?“ Open Forum Infectious Diseases 6, Supplement_2 (Oktober 2019): S583—S584. http://dx.doi.org/10.1093/ofid/ofz360.1464.
Gangadharappa, Bhavya, Manjunath Dammalli und Sharath Rajashekarappa. „β-Lactams and β-Lactamase Inhibitors: Unlocking their potential to address drug resistance“. Research Journal of Biotechnology 16, Nr. 8 (25.07.2021): 151–58. http://dx.doi.org/10.25303/168rjbt15121.
Kadry, Ashraf. „Lacking of efflux mechanism in clinical isolate of Pseudomonas aerupinosa highly resistant to β-Lactams And imimnem“. Scientia Pharmaceutica 71, Nr. 2 (04.05.2003): 89–100. http://dx.doi.org/10.3797/scipharm.aut-03-10.
Nagpal, Reshma, Jitender Bhalla und Shamsher S. Bari. „A Comprehensive Review on C-3 Functionalization of β-Lactams“. Current Organic Synthesis 16, Nr. 1 (04.02.2019): 3–16. http://dx.doi.org/10.2174/1570179415666181116103341.
Dousa, Khalid M., Barry N. Kreiswirth, Sebastian Kurz und Robert A. Bonomo. „786. Ceftaroline and Avibactam? Is This a Potential Combination for Mycobacterium abscessus Infection?“ Open Forum Infectious Diseases 5, suppl_1 (November 2018): S281. http://dx.doi.org/10.1093/ofid/ofy210.793.
Therien, Alex G., Joann L. Huber, Kenneth E. Wilson, Patrick Beaulieu, Alexandre Caron, David Claveau, Kathleen Deschamps et al. „Broadening the Spectrum of β-Lactam Antibiotics through Inhibition of Signal Peptidase Type I“. Antimicrobial Agents and Chemotherapy 56, Nr. 9 (18.06.2012): 4662–70. http://dx.doi.org/10.1128/aac.00726-12.
MacDougall, Conan. „Beyond Susceptible and Resistant, Part I: Treatment of Infections Due to Gram-Negative Organisms With Inducible β-Lactamases“. Journal of Pediatric Pharmacology and Therapeutics 16, Nr. 1 (01.01.2011): 23–30. http://dx.doi.org/10.5863/1551-6776-16.1.23.
Kidwai, M., P. Sapra und K. R. Shushan. „Synthetic Strategies and Medicinal Properties of β-Lactams“. Current Medicinal Chemistry 6, Nr. 3 (März 1999): 195–215. http://dx.doi.org/10.2174/0929867306666220208205333.
Gostev, Vladimir V., O. E. Punchenko und Sergey V. Sidorenko. „The current view on betalactam resistance in Staphylococcus aureus“. Clinical Microbiology and Antimicrobial Chemotherapy 23, Nr. 4 (2021): 375–87. http://dx.doi.org/10.36488/cmac.2021.4.375-387.
Tsang, Wing Y., Naveed Ahmed, Karl Hemming und Michael I. Page. „Competitive endo- and exo-cyclic CN fission in the hydrolysis of N-aroyl β-lactams“. Canadian Journal of Chemistry 83, Nr. 9 (01.09.2005): 1432–39. http://dx.doi.org/10.1139/v05-153.
Drawz, Sarah M., und Robert A. Bonomo. „Three Decades of β-Lactamase Inhibitors“. Clinical Microbiology Reviews 23, Nr. 1 (Januar 2010): 160–201. http://dx.doi.org/10.1128/cmr.00037-09.
Masuda, Nobuhisa, Naomasa Gotoh, Chie Ishii, Eiko Sakagawa, Satoshi Ohya und Takeshi Nishino. „Interplay between Chromosomal β-Lactamase and the MexAB-OprM Efflux System in Intrinsic Resistance to β-Lactams inPseudomonas aeruginosa“. Antimicrobial Agents and Chemotherapy 43, Nr. 2 (01.02.1999): 400–402. http://dx.doi.org/10.1128/aac.43.2.400.
Kimura, Soichiro, Masaji Ishiguro, Yoshikazu Ishii, Jimena Alba und Keizo Yamaguchi. „Role of a Mutation at Position 167 of CTX-M-19 in Ceftazidime Hydrolysis“. Antimicrobial Agents and Chemotherapy 48, Nr. 5 (Mai 2004): 1454–60. http://dx.doi.org/10.1128/aac.48.5.1454-1460.2004.
Tajada, P., J. L. Gomez-Graces, J. I. Alós, D. Balas und R. Cogollos. „Antimicrobial susceptibilities of Campylobacter jejuni and Campylobacter coli to 12 beta-lactam agents and combinations with beta-lactamase inhibitors.“ Antimicrobial Agents and Chemotherapy 40, Nr. 8 (August 1996): 1924–25. http://dx.doi.org/10.1128/aac.40.8.1924.
Valtonen, Satu J., Jussi S. Kurittu und Matti T. Karp. „A Luminescent Escherichia coli Biosensor for the High Throughput Detection of β-Lactams“. Journal of Biomolecular Screening 7, Nr. 2 (April 2002): 127–34. http://dx.doi.org/10.1177/108705710200700205.
Hussan, Jagir R., Stuart G. Irwin, Brya Mathews, Simon Swift, Dustin L. Williams und Jillian Cornish. „Optimal dose of lactoferrin reduces the resilience of in vitro Staphylococcus aureus colonies“. PLOS ONE 17, Nr. 8 (12.08.2022): e0273088. http://dx.doi.org/10.1371/journal.pone.0273088.
Hamerníková, Michaela, Jaroslav Havlíček, Romana Bláhová, Helena Pospíšilová, Hana Votavová und Karel Kefurt. „6-Amino-2,6-dideoxy- or -2,3,6-trideoxyhexono-1,6-lactams: Synthesis and Conformation“. Collection of Czechoslovak Chemical Communications 69, Nr. 4 (2004): 867–84. http://dx.doi.org/10.1135/cccc20040867.
Hark-Khan, Raida, und William A. Moats. „Identification and Measurement of β-Lactam Antibiotic Residues in Milk: Integration of Screening Kits with Liquid Chromatography“. Journal of AOAC INTERNATIONAL 78, Nr. 4 (01.07.1995): 978–86. http://dx.doi.org/10.1093/jaoac/78.4.978.
Tribuddharat, Chanwit, Richard A. Moore, Patricia Baker und Donald E. Woods. „Burkholderia pseudomallei Class A β-Lactamase Mutations That Confer Selective Resistance against Ceftazidime or Clavulanic Acid Inhibition“. Antimicrobial Agents and Chemotherapy 47, Nr. 7 (Juli 2003): 2082–87. http://dx.doi.org/10.1128/aac.47.7.2082-2087.2003.
Bryan, L. E., A. J. Godfrey und T. Schollardt. „Virulence of Pseudomonas aeruginosa strains with mechanisms of microbial persistence for β-lactam and aminoglycoside antibiotics in a mouse infection model“. Canadian Journal of Microbiology 31, Nr. 4 (01.04.1985): 377–80. http://dx.doi.org/10.1139/m85-072.
Krey, Steven C., Jeff Waise und Lee P. Skrupky. „Confronting the Challenge of Beta-Lactam Allergies: A Quasi-Experimental Study Assessing Impact of Pharmacy-Led Interventions“. Journal of Pharmacy Practice 32, Nr. 2 (21.11.2017): 139–46. http://dx.doi.org/10.1177/0897190017743154.
Lagacé-Wiens, P. R. S., F. Tailor, P. Simner, M. DeCorby, J. A. Karlowsky, A. Walkty, D. J. Hoban und G. G. Zhanel. „Activity of NXL104 in Combination with β-Lactams against Genetically Characterized Escherichia coli and Klebsiella pneumoniae Isolates Producing Class A Extended-Spectrum β-Lactamases and Class C β-Lactamases“. Antimicrobial Agents and Chemotherapy 55, Nr. 5 (28.02.2011): 2434–37. http://dx.doi.org/10.1128/aac.01722-10.
Story-Roller, Elizabeth, und Gyanu Lamichhane. „803. Overcoming β-Lactam Resistance in Mycobacterium abscessus“. Open Forum Infectious Diseases 5, suppl_1 (November 2018): S288. http://dx.doi.org/10.1093/ofid/ofy210.810.
Barba, Victor, Cecilia Hernández, Susana Rojas-Lima, Norberto Farfán und Rosa Santillan. „Preparation of N-aryl-substituted spiro-β-lactams via Staudinger cycloaddition“. Canadian Journal of Chemistry 77, Nr. 12 (05.12.1999): 2025–32. http://dx.doi.org/10.1139/v99-212.
Stover, Kayla R., Katie E. Barber und Jamie L. Wagner. „Allergic Reactions and Cross-Reactivity Potential with Beta-Lactamase Inhibitors“. Pharmacy 7, Nr. 3 (28.06.2019): 77. http://dx.doi.org/10.3390/pharmacy7030077.
Sun, Shuhai, Zhuang Li, Zhixing Ren und Yu Li. „Multi-Dimensional Elimination of β-Lactams in the Rural Wetland: Molecule Design and Screening for More Antibacterial and Degradable Substitutes“. Molecules 27, Nr. 23 (02.12.2022): 8434. http://dx.doi.org/10.3390/molecules27238434.
Cremniter, Julie, Jean-Luc Mainardi, Nathalie Josseaume, Jean-Charles Quincampoix, Lionel Dubost, Jean-Emmanuel Hugonnet, Arul Marie, Laurent Gutmann, Louis B. Rice und Michel Arthur. „Novel Mechanism of Resistance to Glycopeptide Antibiotics in Enterococcus faecium“. Journal of Biological Chemistry 281, Nr. 43 (29.08.2006): 32254–62. http://dx.doi.org/10.1074/jbc.m606920200.
Isoda, Motoyuki, Kazuyuki Sato, Yurika Kunugi, Satsuki Tokonishi, Atsushi Tarui, Masaaki Omote, Hideki Minami und Akira Ando. „Rh-Catalyzed reductive Mannich-type reaction and its application towards the synthesis of (±)-ezetimibe“. Beilstein Journal of Organic Chemistry 12 (27.07.2016): 1608–15. http://dx.doi.org/10.3762/bjoc.12.157.
Skoglund, Erik, Henrietta Abodakpi, Rafael Rios, Lorena Diaz, Elsa De La Cadena, An Q. Dinh, Javier Ardila et al. „In Vivo Resistance to Ceftolozane/Tazobactam in Pseudomonas aeruginosa Arising by AmpC- and Non-AmpC-Mediated Pathways“. Case Reports in Infectious Diseases 2018 (23.12.2018): 1–4. http://dx.doi.org/10.1155/2018/9095203.
Gostev, Vladimir, Olga Kalinogorskaya, Ksenia Ivanova, Ekaterina Kalisnikova, Irina Lazareva, Polina Starkova und Sergey Sidorenko. „In Vitro Selection of High-Level Beta-Lactam Resistance in Methicillin-Susceptible Staphylococcus aureus“. Antibiotics 10, Nr. 6 (26.05.2021): 637. http://dx.doi.org/10.3390/antibiotics10060637.
Wachino, Jun-ichi, Yoshihiro Yamaguchi, Shigetarou Mori, Hiromasa Kurosaki, Yoshichika Arakawa und Keigo Shibayama. „Structural Insights into the Subclass B3 Metallo-β-Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo-β-Lactamase Inhibitor Mercaptoacetate“. Antimicrobial Agents and Chemotherapy 57, Nr. 1 (15.10.2012): 101–9. http://dx.doi.org/10.1128/aac.01264-12.
Kaur Mann, Maninderjeet, Rupesh Kumar und Gaurav Bhargava. „Facially Selective Oxo-Diels-Alder Cycloadditions of α-Dienyl-β-Lactam: An Entry to Pyrano Tethered β-Lactams Bifunctional Hybrids“. Oriental Journal Of Chemistry 38, Nr. 3 (30.06.2022): 790–95. http://dx.doi.org/10.13005/ojc/380334.
Bayles, Thibault, und Catherine Guillou. „Trifluoroethanol Promoted Castagnoli–Cushman Cycloadditions of Imines with Homophthalic Anhydride“. Molecules 27, Nr. 3 (27.01.2022): 844. http://dx.doi.org/10.3390/molecules27030844.