about
The β-Lactams Strike Back: Ceftazidime-AvibactamStructural Origins of Oxacillinase Specificity in Class D -LactamasesStructural Basis for Different Substrate Profiles of Two Closely Related Class D β-Lactamases and Their Inhibition by HalogensRemoval of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric StrainThe structure of a doripenem-bound OXA-51 class D β-lactamase variant with enhanced carbapenemase activityStructural basis of activity against aztreonam and extended spectrum cephalosporins for two carbapenem-hydrolyzing class D β-lactamases from Acinetobacter baumannii.Class D β-lactamases do exist in Gram-positive bacteria.Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme accessClinical Variants of the Native Class D β-Lactamase of Acinetobacter baumannii Pose an Emerging Threat through Increased Hydrolytic Activity against CarbapenemsIntraclonal Genome Stability of the Metallo-β-lactamase SPM-1-producing Pseudomonas aeruginosa ST277, an Endemic Clone Disseminated in Brazilian Hospitals.The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine.Fragment-based inhibitor discovery against β-lactamaseβ-lactam/β-lactamase inhibitor combinations: from then to now.Molecular Targets of β-Lactam-Based Antimicrobials: Beyond the Usual Suspects.Characterization of the redox transition of the XRCC1 N-terminal domain.β-Lactamases: A Focus on Current Challenges.Activity of the β-Lactamase inhibitor LN-1-255 against carbapenem-hydrolyzing class D β-lactamases from Acinetobacter baumannii.ETX2514 is a broad-spectrum β-lactamase inhibitor for the treatment of drug-resistant Gram-negative bacteria including Acinetobacter baumannii.Exploring the potential of boronic acids as inhibitors of OXA-24/40 β-lactamase.Multiple substitutions lead to increased loop flexibility and expanded specificity in Acinetobacter baumannii carbapenemase OXA-239.
P2860
Q26796425-3FE0D5CA-BB2C-48DF-9B56-F8A01853FE27Q27680475-F5FD31C3-B0C7-474B-9A21-71CF035D720AQ27700611-B4744218-B154-4895-9B44-0F689D2551D2Q27704563-95119526-0AF3-4E59-821E-8E0D1129459BQ27728076-2304EF9D-1C2A-41B8-A277-738156B4A20AQ35765638-6EB22DB4-CB6C-413C-A1D4-56219BCDDEFFQ36386436-A584CCCD-A4A6-4CC3-92FF-D333FBC3E8A9Q36555388-2A5A730C-5A81-49DA-9201-595B7430E794Q37287767-3164A6BB-AFC9-4C5A-8AC1-993584493CA7Q37471259-186F55C5-5B0C-4152-981E-61F1FAF5C2F6Q37608564-A5541D99-AD47-42AE-A6C8-3DB17F84B4A9Q38196443-85C1946C-BC01-486D-8DD6-88BCD0A5BDD0Q38264182-C8103896-CD70-43D4-B024-1D13FAD13421Q38792863-AF581D4B-68B6-4462-8C2E-6520DF1AA056Q38933989-680D9C14-A8AE-4033-A588-39CAA843C155Q38981257-E11D8D9D-3E27-4661-A10B-A1A24A0888A5Q40083229-3BB39B5C-9DD8-4685-8626-1D481F7E0545Q40152356-281E1089-A6B5-4E45-87F6-297103C1E51CQ40402495-4B0C18A9-87D4-467E-B6AD-00D671751B40Q47305062-760008F7-C203-493D-95B5-1A3B85610B46
P2860
description
2013 nî lūn-bûn
@nan
2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Class D β-lactamases: a reappraisal after five decades
@ast
Class D β-lactamases: a reappraisal after five decades
@en
Class D β-lactamases: a reappraisal after five decades
@nl
type
label
Class D β-lactamases: a reappraisal after five decades
@ast
Class D β-lactamases: a reappraisal after five decades
@en
Class D β-lactamases: a reappraisal after five decades
@nl
prefLabel
Class D β-lactamases: a reappraisal after five decades
@ast
Class D β-lactamases: a reappraisal after five decades
@en
Class D β-lactamases: a reappraisal after five decades
@nl
P2860
P356
P1476
Class D β-lactamases: a reappraisal after five decades
@en
P2093
David A Leonard
Rachel A Powers
P2860
P304
P356
10.1021/AR300327A
P407
P577
2013-11-19T00:00:00Z