On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
about
Three decades of beta-lactamase inhibitorsSuccinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamaseAsp-120 locates Zn2 for optimal metallo-beta-lactamase activityMutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active SiteCrystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157A designed supramolecular protein assembly with in vivo enzymatic activityOvercoming differences: The catalytic mechanism of metallo-β-lactamasesStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceBiapenem inactivation by B2 metallo β-lactamases: energy landscape of the post-hydrolysis reactionsBiochemical characteristics of New Delhi metallo-β-lactamase-1 show unexpected difference to other MBLsEvolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.Evolution of broad spectrum β-lactam resistance in an engineered metallo-β-lactamase.Effect of Zn...Zn separation on the hydrolytic activity of model dizinc phosphodiesterases.Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Metallo-beta-lactamases: the quiet before the storm?Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum.Molecular basis of NDM-1, a new antibiotic resistance determinantMolecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamaseComputational analysis of pathogen-borne metallo β-lactamases reveals discriminating structural features between B1 types.One origin for metallo-β-lactamase activity, or two? An investigation assessing a diverse set of reconstructed ancestral sequences based on a sample of phylogenetic trees.QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screeningCrystal Structure of DIM-1, an Acquired Subclass B1 Metallo-β-Lactamase from Pseudomonas stutzeri.Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopyProbing the role of Met221 in the unusual metallo-β-lactamase GOB-18.B1-Metallo-β-Lactamases: Where Do We Stand?Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysisEngineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Mechanistic studies on the mononuclear ZnII-containing metallo-beta-lactamase ImiS from Aeromonas sobria.Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes.Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1Bisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase.Insights into an evolutionary strategy leading to antibiotic resistance.Metallo-β-lactamase structure and function.A variety of roles for versatile zinc in metallo-β-lactamases.Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.Characterization of monomeric L1 metallo-beta -lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis.The mechanisms of catalysis by metallo beta-lactamases.
P2860
Q24646623-067D632B-0F21-43A8-86DB-B028B16E4523Q27632353-268B128E-473E-4EC8-A02B-70AC55D9AD6CQ27644399-6DC60358-D94E-44B3-BC24-99635C9467D5Q27671609-A4320E13-79A8-419C-A19A-D60927EAD559Q27679496-0C30C06F-232F-43EE-9EF8-4D672C757DB2Q27696882-088F5E76-0B88-43ED-B361-C00CF7E8105AQ28082109-F5F597DD-C5C8-4C20-BA59-E07DFC1C9BA0Q28084628-4BFBCDFF-E278-4DCE-A73E-FDB178900CFEQ28478901-0183FCDE-641D-4691-8327-51D40B1BF345Q28486166-99A59A95-5567-49B3-ADB8-DABE1E0589CCQ28752557-E14FEB5B-5507-4968-87C3-E6B5AB4590BFQ30486102-3D990AEA-F0D1-485A-A1EE-A4CBBC91710EQ31108106-235CDD02-6C80-418D-95C2-1604CFE1294CQ33214803-34D98339-5532-4FAE-B256-E9878D0AA575Q33715941-2619CD89-585D-47A4-844E-E96FA6D48C3FQ33755227-FAA47DE8-0628-4895-BFB5-D653C831FE66Q33980022-7422E800-E84A-4024-9C41-FC352E4FF6A4Q34009443-3241C5B3-5BE3-409D-A65A-2A193CCBCA16Q34057408-453BF74A-E21A-47C0-9A3A-536454686757Q34158563-D8911924-8C56-420B-9147-D19C525CFD04Q34436730-3EEE7097-7003-43D2-8505-C5BD0F3C14B7Q34438621-AF49D5C6-C28E-4449-9C12-84AF84F05F3FQ34571608-BF87DD8A-AC7D-4E1C-B61A-0074D2AA963DQ34671008-1D777729-68AF-4479-97F3-250DE8477882Q35801593-24AD5B2F-86AC-435B-8E9F-6C96D8076EBDQ36522851-2D3A1D91-F651-465D-A2BC-58F863810298Q36673614-BDCBD60E-06BD-42E7-852D-FFA81F14F2F6Q36746608-50E466C9-D5E9-466B-B3A4-3B1937D4D38EQ36795249-1B47E9F5-ECA4-4D57-B640-13D191FD2FA4Q36932331-2F2F6BB3-59DB-4ED1-A7A8-8DC7937F7EBCQ37003125-7F4ECC67-F587-480D-A3B3-9DDA7B67EDD7Q37065167-87616C45-7BEE-4926-8D56-EA7FA1FD10BCQ37182382-05738B92-5382-4870-91F5-EC9FE9E3E650Q37340068-D364EC43-8D30-4579-9FB0-406A61D650A3Q37578905-466F0857-E7DD-46D0-B44B-A7EE877C04A3Q38060809-E11434CB-35BB-43D6-BEDC-85F9F97E72C7Q38201660-E56B6806-3D4D-4120-86D7-8D31C9744E1AQ38269060-D5B2DE2B-5B87-4FD2-94D5-C44272EA88D6Q38290404-9C36CE2D-F383-457B-AFD0-1CC9790A7AB3Q39019943-DC6AB612-3BAA-459E-8584-14B2545DC118
P2860
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@ast
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@en
type
label
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@ast
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@en
prefLabel
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@ast
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@en
P2093
P356
P1433
P1476
On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.
@en
P2093
P304
10013-10023
P356
10.1021/BI990356R
P407
P577
1999-08-01T00:00:00Z