Artykuły w czasopismach na temat „Lactams”
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Li, Lu, Qiyao Wang, Hui Zhang, Minjun Yang, Mazhar I. Khan i 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 (1.02.2016): 1648–53. http://dx.doi.org/10.1073/pnas.1520300113.
Pełny tekst źródłaMedina, Marjorie B., Dana J. Poole i 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 (1.09.1998): 963–72. http://dx.doi.org/10.1093/jaoac/81.5.963.
Pełny tekst źródłaAlves, Américo J. S., Nuno G. Alves, Cátia C. Caratão, Margarida I. M. Esteves, Diana Fontinha, Inês Bártolo, Maria I. L. Soares i in. "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.
Pełny tekst źródłaLi, Xian-Zhi, Li Zhang, Ramakrishnan Srikumar i Keith Poole. "β-Lactamase Inhibitors Are Substrates for the Multidrug Efflux Pumps of Pseudomonas aeruginosa". Antimicrobial Agents and Chemotherapy 42, nr 2 (1.02.1998): 399–403. http://dx.doi.org/10.1128/aac.42.2.399.
Pełny tekst źródłaBrilhante, 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 i in. "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.
Pełny tekst źródłaSekiguchi, Jun-ichiro, Koji Morita, Tomoe Kitao, Noboru Watanabe, Mitsuhiro Okazaki, Tohru Miyoshi-Akiyama, Masato Kanamori i Teruo Kirikae. "KHM-1, a Novel Plasmid-Mediated Metallo-β-Lactamase from a Citrobacter freundii Clinical Isolate". Antimicrobial Agents and Chemotherapy 52, nr 11 (2.09.2008): 4194–97. http://dx.doi.org/10.1128/aac.01337-07.
Pełny tekst źródłaGlen, Karl A., i 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.
Pełny tekst źródłaLi, Fu, Li Wan, Tongyang Xiao, Haican Liu, Yi Jiang, Xiuqin Zhao, Ruibai Wang i Kanglin Wan. "In Vitro Activity of β-Lactams in Combination with β-Lactamase Inhibitors against Mycobacterium tuberculosis Clinical Isolates". BioMed Research International 2018 (2.07.2018): 1–8. http://dx.doi.org/10.1155/2018/3579832.
Pełny tekst źródłaMukhopadhyay, S., i P. Chakrabarti. "Altered permeability and beta-lactam resistance in a mutant of Mycobacterium smegmatis." Antimicrobial Agents and Chemotherapy 41, nr 8 (sierpień 1997): 1721–24. http://dx.doi.org/10.1128/aac.41.8.1721.
Pełny tekst źródłaYin, Jianhua, Yiyang Sun, Yinting Mao, Miao Jin i 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.
Pełny tekst źródłaAsgarali, Azizah, Keith A. Stubbs, Antonio Oliver, David J. Vocadlo i Brian L. Mark. "Inactivation of the Glycoside Hydrolase NagZ Attenuates Antipseudomonal β-Lactam Resistance in Pseudomonas aeruginosa". Antimicrobial Agents and Chemotherapy 53, nr 6 (9.03.2009): 2274–82. http://dx.doi.org/10.1128/aac.01617-08.
Pełny tekst źródłaSayed, Alaa R. M., Nirav R. Shah, Kari B. Basso, Manasi Kamat, Yuanyuan Jiao, Bartolome Moya, Dhruvitkumar S. Sutaria i in. "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.
Pełny tekst źródłaYuan, Qinghui, Lin He i 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.
Pełny tekst źródłaTarui, Atsushi, Yukiko Karuo, Kazuyuki Sato, Kentaro Kawai i 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.
Pełny tekst źródłaNagira, Yu, Keiko Yamada, Hayato Okade, Nami Senju, Yuko Tsutsumi, Yuji Tabata i 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 (1.10.2020): S655. http://dx.doi.org/10.1093/ofid/ofaa439.1462.
Pełny tekst źródłaSrivastava, 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.
Pełny tekst źródłaPapp-Wallace, Krisztina M., Baui Senkfor, Julian Gatta, Weirui Chai, Magdalena A. Taracila, Veerabahu Shanmugasundaram, Seungil Han i in. "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.
Pełny tekst źródłaPatel, Twisha S., Vince Marshall, Keith S. Kaye, Aaron Smith, Carol Young, Paul Lephart i 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 (październik 2019): S583—S584. http://dx.doi.org/10.1093/ofid/ofz360.1464.
Pełny tekst źródłaGangadharappa, Bhavya, Manjunath Dammalli i 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.
Pełny tekst źródłaKadry, Ashraf. "Lacking of efflux mechanism in clinical isolate of Pseudomonas aerupinosa highly resistant to β-Lactams And imimnem". Scientia Pharmaceutica 71, nr 2 (4.05.2003): 89–100. http://dx.doi.org/10.3797/scipharm.aut-03-10.
Pełny tekst źródłaNagpal, Reshma, Jitender Bhalla i Shamsher S. Bari. "A Comprehensive Review on C-3 Functionalization of β-Lactams". Current Organic Synthesis 16, nr 1 (4.02.2019): 3–16. http://dx.doi.org/10.2174/1570179415666181116103341.
Pełny tekst źródłaDousa, Khalid M., Barry N. Kreiswirth, Sebastian Kurz i Robert A. Bonomo. "786. Ceftaroline and Avibactam? Is This a Potential Combination for Mycobacterium abscessus Infection?" Open Forum Infectious Diseases 5, suppl_1 (listopad 2018): S281. http://dx.doi.org/10.1093/ofid/ofy210.793.
Pełny tekst źródłaTherien, Alex G., Joann L. Huber, Kenneth E. Wilson, Patrick Beaulieu, Alexandre Caron, David Claveau, Kathleen Deschamps i in. "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.
Pełny tekst źródłaMacDougall, 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 (1.01.2011): 23–30. http://dx.doi.org/10.5863/1551-6776-16.1.23.
Pełny tekst źródłaKidwai, M., P. Sapra i K. R. Shushan. "Synthetic Strategies and Medicinal Properties of β-Lactams". Current Medicinal Chemistry 6, nr 3 (marzec 1999): 195–215. http://dx.doi.org/10.2174/0929867306666220208205333.
Pełny tekst źródłaGostev, Vladimir V., O. E. Punchenko i 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.
Pełny tekst źródłaTsang, Wing Y., Naveed Ahmed, Karl Hemming i 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 (1.09.2005): 1432–39. http://dx.doi.org/10.1139/v05-153.
Pełny tekst źródłaDrawz, Sarah M., i Robert A. Bonomo. "Three Decades of β-Lactamase Inhibitors". Clinical Microbiology Reviews 23, nr 1 (styczeń 2010): 160–201. http://dx.doi.org/10.1128/cmr.00037-09.
Pełny tekst źródłaMasuda, Nobuhisa, Naomasa Gotoh, Chie Ishii, Eiko Sakagawa, Satoshi Ohya i 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 (1.02.1999): 400–402. http://dx.doi.org/10.1128/aac.43.2.400.
Pełny tekst źródłaKimura, Soichiro, Masaji Ishiguro, Yoshikazu Ishii, Jimena Alba i Keizo Yamaguchi. "Role of a Mutation at Position 167 of CTX-M-19 in Ceftazidime Hydrolysis". Antimicrobial Agents and Chemotherapy 48, nr 5 (maj 2004): 1454–60. http://dx.doi.org/10.1128/aac.48.5.1454-1460.2004.
Pełny tekst źródłaTajada, P., J. L. Gomez-Graces, J. I. Alós, D. Balas i 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 (sierpień 1996): 1924–25. http://dx.doi.org/10.1128/aac.40.8.1924.
Pełny tekst źródłaValtonen, Satu J., Jussi S. Kurittu i Matti T. Karp. "A Luminescent Escherichia coli Biosensor for the High Throughput Detection of β-Lactams". Journal of Biomolecular Screening 7, nr 2 (kwiecień 2002): 127–34. http://dx.doi.org/10.1177/108705710200700205.
Pełny tekst źródłaHussan, Jagir R., Stuart G. Irwin, Brya Mathews, Simon Swift, Dustin L. Williams i 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.
Pełny tekst źródłaHamerníková, Michaela, Jaroslav Havlíček, Romana Bláhová, Helena Pospíšilová, Hana Votavová i 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.
Pełny tekst źródłaHark-Khan, Raida, i 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 (1.07.1995): 978–86. http://dx.doi.org/10.1093/jaoac/78.4.978.
Pełny tekst źródłaTribuddharat, Chanwit, Richard A. Moore, Patricia Baker i 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 (lipiec 2003): 2082–87. http://dx.doi.org/10.1128/aac.47.7.2082-2087.2003.
Pełny tekst źródłaBryan, L. E., A. J. Godfrey i 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 (1.04.1985): 377–80. http://dx.doi.org/10.1139/m85-072.
Pełny tekst źródłaKrey, Steven C., Jeff Waise i 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.
Pełny tekst źródłaLagacé-Wiens, P. R. S., F. Tailor, P. Simner, M. DeCorby, J. A. Karlowsky, A. Walkty, D. J. Hoban i 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.
Pełny tekst źródłaStory-Roller, Elizabeth, i Gyanu Lamichhane. "803. Overcoming β-Lactam Resistance in Mycobacterium abscessus". Open Forum Infectious Diseases 5, suppl_1 (listopad 2018): S288. http://dx.doi.org/10.1093/ofid/ofy210.810.
Pełny tekst źródłaBarba, Victor, Cecilia Hernández, Susana Rojas-Lima, Norberto Farfán i Rosa Santillan. "Preparation of N-aryl-substituted spiro-β-lactams via Staudinger cycloaddition". Canadian Journal of Chemistry 77, nr 12 (5.12.1999): 2025–32. http://dx.doi.org/10.1139/v99-212.
Pełny tekst źródłaStover, Kayla R., Katie E. Barber i 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.
Pełny tekst źródłaSun, Shuhai, Zhuang Li, Zhixing Ren i 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 (2.12.2022): 8434. http://dx.doi.org/10.3390/molecules27238434.
Pełny tekst źródłaCremniter, Julie, Jean-Luc Mainardi, Nathalie Josseaume, Jean-Charles Quincampoix, Lionel Dubost, Jean-Emmanuel Hugonnet, Arul Marie, Laurent Gutmann, Louis B. Rice i 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.
Pełny tekst źródłaIsoda, Motoyuki, Kazuyuki Sato, Yurika Kunugi, Satsuki Tokonishi, Atsushi Tarui, Masaaki Omote, Hideki Minami i 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.
Pełny tekst źródłaSkoglund, Erik, Henrietta Abodakpi, Rafael Rios, Lorena Diaz, Elsa De La Cadena, An Q. Dinh, Javier Ardila i in. "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.
Pełny tekst źródłaGostev, Vladimir, Olga Kalinogorskaya, Ksenia Ivanova, Ekaterina Kalisnikova, Irina Lazareva, Polina Starkova i 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.
Pełny tekst źródłaWachino, Jun-ichi, Yoshihiro Yamaguchi, Shigetarou Mori, Hiromasa Kurosaki, Yoshichika Arakawa i 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.
Pełny tekst źródłaKaur Mann, Maninderjeet, Rupesh Kumar i 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.
Pełny tekst źródłaBayles, Thibault, i 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.
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