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His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7Trojan Horse Antibiotics-A Novel Way to Circumvent Gram-Negative Bacterial Resistance?A Review of SHV Extended-Spectrum β-Lactamases: Neglected Yet UbiquitousInsights on the Horizontal Gene Transfer of Carbapenemase Determinants in the Opportunistic Pathogen Acinetobacter baumanniiCarbapenem-Resistant Bacteria Recovered from Faeces of Dairy Cattle in the High Plains Region of the USAPlanctomycetes do possess a peptidoglycan cell wall.Lethal neonatal meningoencephalitis caused by multi-drug resistant, highly virulent Escherichia coli.A qPCR and multiplex pyrosequencing assay combined with automated data processing for rapid and unambiguous detection of ESBL-producers Enterobacteriaceae.Three Novel Species with Peptidoglycan Cell Walls form the New Genus Lacunisphaera gen. nov. in the Family Opitutaceae of the Verrucomicrobial Subdivision 4.Fluorescent TEM-1 β-lactamase with wild-type activity as a rapid drug sensor for in vitro drug screening.Ceftazidime-avibactam: an evidence-based review of its pharmacology and potential use in the treatment of Gram-negative bacterial infections.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.Amino Acid Thioester Derivatives: A Highly Promising Scaffold for the Development of Metallo-β-lactamase L1 Inhibitors.Inhibition of Klebsiella β-Lactamases (SHV-1 and KPC-2) by Avibactam: A Structural Study.Draft Genome Sequence of Strain ATCC 33958, Reported To Be Elizabethkingia miricola.Genetic and Biochemical Characterization of FRI-1, a Carbapenem-Hydrolyzing Class A β-Lactamase from Enterobacter cloacaeCharacterization and distribution of drug resistance associated β-lactamase, membrane porin and efflux pump genes in MDR A. baumannii isolated from Zhenjiang, ChinaDilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies.Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Intestinal Carriage of Carbapenemase-Producing Organisms: Current Status of Surveillance MethodsProbing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysisTriazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) InhibitorsTracking Cefoperazone/Sulbactam Resistance Development In vivo in A. baumannii Isolated from a Patient with Hospital-Acquired Pneumonia by Whole-Genome SequencingEstablishment of a Simple and Quick Method for Detecting Extended-Spectrum β-Lactamase (ESBL) Genes in BacteriaEfficacy of humanized carbapenem and ceftazidime regimens against Enterobacteriaceae producing OXA-48 carbapenemase in a murine infection model.In vivo efficacy of human simulated regimens of carbapenems and comparator agents against NDM-1-producing Enterobacteriaceae.Extended-spectrum beta-lactamase-producing Pseudomonas aeruginosa in camel in Egypt: potential human hazard.One ring to rule them all: Current trends in combating bacterial resistance to the β-lactamsCeftazidime-avibactam: novel antimicrobial combination for the treatment of complicated urinary tract infections.Acquired Class D β-Lactamases.Ceftazidime-avibactam (CTZ-AVI) as a treatment for hospitalized adult patients with complicated intra-abdominal infections.Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.Novel β-Lactamase blaARL in Staphylococcus arlettae.Characterisation of extended-spectrum β-lactamase and AmpC β-lactamase-producing Enterobacteriaceae isolated from companion animals in New Zealand.The Resistant-Population Cutoff (RCOFF): a New Concept for Improved Characterization of Antimicrobial Susceptibility Patterns of Non-Wild-Type Bacterial Populations.Evaluation of the Rapidec Carba NP Test for Detection of Carbapenemases in EnterobacteriaceaeIn vitro activity of aztreonam-avibactam against a global collection of Gram-negative pathogens from 2012 and 2013.
P2860
Q27684253-E5D5C12F-F395-438C-9BAB-29A80D600F7CQ28067116-5F04F8B0-437D-4C0A-9FED-1BE34D9B460FQ28076260-8F7F5F75-9C54-4896-B1FD-7C07D73DF096Q28078376-B46341F9-9631-43A8-B609-0BBBC935F1A0Q28552964-FC21F49E-5D5F-43FB-939F-E366C6AF0A38Q30650621-26E6AB17-4C15-4538-B1E1-F11B7E1FA928Q30736329-EAD6F4C9-7F3F-4C64-8A17-2A22914796A1Q30986331-C66F1AB7-6406-447A-AB16-34BDD054ADD0Q31167555-9ABB2452-A9A7-4C9B-A43D-CD93BE9F6D73Q34139889-4622FCF5-548B-44D8-9518-F9B78FA53C57Q34402134-3C01BC17-ECAB-4FBD-8495-16D6E3D02C3CQ34579901-ED52FE40-1E80-4FF4-8D1D-592C775CBC64Q35379053-40D05D0A-04E7-4B07-A077-4AAD7BDB1EBEQ35745140-5C2D07D3-0E1D-4130-AF82-0835D241C39AQ35764780-FA919ABC-D04B-40D5-BA88-8617297583E5Q35883986-87309C31-529D-4982-BBE5-6EDA542C7907Q36290715-E4E4E480-4F86-4058-9E9A-78493A169EE4Q36317521-0C281E5A-D5C7-49B3-ABEB-CC56A586928DQ36522810-FBAD6D50-8E2E-43E1-A846-5D6D59DEF167Q36571912-9DF7E373-AAF1-49C0-A82E-FE5A68969BE8Q36630989-D6382B77-9736-44DA-9395-A966A1B3C6A2Q36631019-DA5FB12A-C8A6-4133-8C48-F96B1DD93D49Q36795249-CA582304-FB47-4FAB-B2B0-F5BB5415F539Q36806776-FB158665-6442-44A0-AE67-050B15B7D6A6Q37188148-6D2A9909-C987-4F20-87A7-9C03ADF3B18DQ37262542-2A2F5009-17C9-4044-951B-ECE13FD170DCQ37643634-E695B713-89A8-40AE-BBCF-0DCF67826FDAQ37643705-F368CF35-48D6-4318-AF9E-5A1B91A7B91FQ37731567-A32430DB-4564-42AF-A89E-45CC411DD9C4Q38712471-C6D96E91-6CB3-43E8-BF88-6279A9834C92Q38740494-584C701C-FDD3-4C2E-BAD0-9F308C8ABB7CQ38792886-9734E4E5-F7FE-4202-85C0-2C26892F4C26Q38797485-521FC3B2-40D3-430B-8339-C03ACE28EC92Q40064693-5F193D42-F974-4531-8EFC-F54C6DDC0E5CQ40192465-7CDDBD0A-33E2-4AAE-95A3-790F2A1B0146Q40215901-CCB57CCD-47E7-4009-BD0B-F81896359219Q40410184-A72F7B3D-4FA4-4DF0-96A5-397C3D97FEF1Q40672387-533AAAEE-141E-49D3-B4C9-B3BF8DE78494Q40971653-BDF5F4C2-9213-4285-A066-F9FC4DEA5DF5Q41240109-A167A5C5-D39C-437D-9A7B-625B45D4A8BC
P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
The ABCD's of β-lactamase nomenclature.
@en
type
label
The ABCD's of β-lactamase nomenclature.
@en
prefLabel
The ABCD's of β-lactamase nomenclature.
@en
P1476
The ABCD's of β-lactamase nomenclature.
@en
P2093
Karen Bush
P2888
P304
P356
10.1007/S10156-013-0640-7
P577
2013-07-05T00:00:00Z