Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.
about
Susceptibilities of 123 strains of Xanthomonas maltophilia to eight beta-lactams (including beta-lactam-beta-lactamase inhibitor combinations) and ciprofloxacin tested by five methodsbeta-Lactamases in laboratory and clinical resistanceA functional classification scheme for beta-lactamases and its correlation with molecular structureProbing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesisChemistry and biosynthesis of clavulanic acid and other clavamsPenicillin-binding proteins and bacterial resistance to beta-lactamsThe Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases.Activities of three quinolones, alone and in combination with extended-spectrum cephalosporins or gentamicin, against Stenotrophomonas maltophiliaEvolution and spread of SHV extended-spectrum beta-lactamases in gram-negative bacteria.Identification of TEM-26 beta-lactamase responsible for a major outbreak of ceftazidime-resistant Klebsiella pneumoniaeMetallo-beta-lactamases: the quiet before the storm?Molecular and genetic analysis of the Bacteroides uniformis cephalosporinase gene, cblA, encoding the species-specific beta-lactamase.Cloning and expression of a cloxacillin-hydrolyzing enzyme and a cephalosporinase from Aeromonas sobria AER 14M in Escherichia coli: requirement for an E. coli chromosomal mutation for efficient expression of the class D enzymeMechanism of tonB-dependent transport of KP-736, a 1,5-dihydroxy-4-pyridone-substituted cephalosporin, into Escherichia coli K-12 cellsIn vitro activities of antimicrobial combinations against Stenotrophomonas (Xanthomonas) maltophilia.Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli.Beta-lactamase production in members of the family Enterobacteriaceae and resistance to beta-lactam-enzyme inhibitor combinations.Nucleotide sequence and phylogeny of SHV-2 beta-lactamase.Sequence analysis and evolutionary perspectives of ROB-1 beta-lactamaseBiochemical properties of a carbapenem-hydrolyzing beta-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli.Characterization of a novel extended-spectrum beta-lactamase from Pseudomonas aeruginosa.Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 beta-lactamase conferring resistance to beta-lactamase inhibitors.Incidence and susceptibility of aerobic Gram-negative bacilli from 20 Canadian intensive care units: 1989-1993.Diffusion of meropenem and imipenem through the outer membrane of Escherichia coli K-12 and correlation with their antibacterial activities.Dissemination of Pseudomonas aeruginosa producing bla IMP-1 and bla VIM-1 in Qazvin and Alborz educational hospitals, Iran.Branhamella catarrhalis: an organism gaining respect as a pathogenOXA-11, an extended-spectrum variant of OXA-10 (PSE-2) beta-lactamase from Pseudomonas aeruginosa.Cloning and characterization of the endogenous cephalosporinase gene, cepA, from Bacteroides fragilis reveals a new subgroup of Ambler class A beta-lactamases.Genetic and biochemical analysis of a novel Ambler class A beta-lactamase responsible for cefoxitin resistance in Bacteroides species.Metallo beta lactamases in Pseudomonas aeruginosa and Acinetobacter species.Molecular evolution of ubiquitous beta-lactamases towards extended-spectrum enzymes active against newer beta-lactam antibiotics.A dramatic change in the rate-limiting step of beta-lactam hydrolysis results from the substitution of the active-site serine residue by a cysteine in the class-C beta-lactamase of Enterobacter cloacae 908RPurification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance.Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis.Characterization of beta-lactamases.Classification of beta-lactamases: groups 1, 2a, 2b, and 2b'.Relative importances of outer membrane permeability and group 1 beta-lactamase as determinants of meropenem and imipenem activities against Enterobacter cloacae.Comparative in vitro activities of L-695,256, a novel carbapenem, against gram-positive bacteria.Purification and characterization of a new beta-lactamase from Bacteroides uniformis.Effect of pH on activities of novel beta-lactamases and beta-lactamase inhibitors against these beta-lactamases.
P2860
Q24609449-D605FA32-AEB9-41B0-ADBC-F6EF122B1C82Q24669605-6BE3F162-B346-40B1-881E-FDFE1883BC88Q24677460-E750A164-D4C0-4459-A917-9B3662F42DE6Q24802987-79B4B0F7-79F9-4525-903D-BF8AA6C2E578Q28247865-E30CBDCF-0F15-4F49-BD21-F88A9E82EBD7Q28257231-CC7C2924-2DF1-4A35-8BF4-5BCB91AF4F1EQ33344627-0B9A0AAC-618C-4339-AB1C-9C8C2F8020A4Q33694859-EFE7BD5D-FE0B-4B89-BEC8-9ECD00265B6FQ33746844-C0F093BD-4C5D-43EE-80C6-092579E73551Q33750083-C6CA4200-8753-412C-A510-104D757ED17CQ33755227-A5C5CAF7-EA4D-4038-AF74-47F15BCAC917Q33756292-46CB08E3-B7AF-4F10-B6A1-9554D13261F9Q33758728-CD85EAFA-4729-494B-A297-76C3E38DBF70Q35112175-2FF351B5-13AE-42C1-9FE7-6B0A1BC58E64Q35119342-8202C5CB-5A79-4457-83BE-232542BB375CQ35119621-AF3109D5-003F-4A81-97FA-39C4CCA7723DQ35252346-5FF085AE-595F-485D-9089-BEBB51F849EFQ35272574-083C086F-B568-4B58-A72F-78B924F9A247Q35565171-6E85EA70-BFAB-408B-A3CA-DE8C2F4DF22EQ35813844-C2632896-706C-448B-9EE9-5C3CC73478DFQ35814019-14B2D182-A2DF-4BCA-8333-B929B5A95E8EQ35820623-CEFE9C30-1B5E-4214-92FD-45F66FF82553Q35891383-580572D9-9012-4EA1-A618-EB0F67FF89EFQ35897020-7E68FE16-1BBF-4B8D-988C-B1D915C351B5Q36577462-8896E7B1-470F-45D5-A2CB-BE61FD79D443Q36636508-40F2009B-F5B5-4F8E-90CB-2A70405D5347Q36753213-82830193-A63E-4A34-97BE-BBD7C695AD47Q36760263-67C4B8A6-3A32-4584-904D-ADE552F990F3Q36785845-FCDBCCD1-F1BD-412F-B889-D39EC3125796Q37071179-227A561E-35AE-4B93-BE5E-F72D7D04A19AQ37782936-91720A4C-064E-4CC4-B2A4-BBDB140BEBF5Q38318627-2CE66A83-EF32-4E66-BBBC-B51FF2D5CA42Q38334197-1103A7A5-A01B-4CEB-B7E8-9F14FBE97896Q38338744-6D545855-81F7-47F4-AEB3-7AB1ECD89503Q38640000-DF998AFC-E285-4882-B308-BE3C74C6E190Q38640013-12808536-FE9E-45C9-9172-DD1BCEEE434DQ39779077-50FD54A2-B204-4164-B2E9-C28EF97C3784Q39779619-DF56208C-2749-435C-AF52-670EAB1F7B30Q39779988-A57BD08E-1508-459C-93DF-5E829A4B962CQ39780263-E92D92E4-8FAE-4E11-B404-613C15C0EC09
P2860
Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.
@en
type
label
Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.
@en
prefLabel
Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.
@en
P2860
P356
P1476
Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.
@en
P2093
P2860
P304
P356
10.1128/AAC.33.3.271
P407
P577
1989-03-01T00:00:00Z