about
Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistanceMutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active SiteStructure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-LactamaseCrystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibitionNDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanismComputational analysis of pathogen-borne metallo β-lactamases reveals discriminating structural features between B1 types.Enumerating pathways of proton abstraction based on a spatial and electrostatic analysis of residues in the catalytic site.Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesBacterial swarms recruit cargo bacteria to pave the way in toxic environments.Structural Insights into Recognition of Hydrolyzed Carbapenems and Inhibitors by Subclass B3 Metallo-β-Lactamase SMB-1.NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitorsTargeting metallo-β-lactamase enzymes in antibiotic resistance.The road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam.Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35.Structural and Biochemical Characterization of Rm3, a Subclass B3 Metallo-β-Lactamase Identified from a Functional Metagenomic Study.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.Danger lurking in the "unknowns": structure-to-function studies of hypothetical protein Bleg1_2437 from Bacillus lehensis G1 alkaliphile revealed an evolutionary divergent B3 metallo-beta-lactamase.Cephalosporins inhibit human metallo β-lactamase fold DNA repair nucleases SNM1A and SNM1B/apollo.A potential substrate binding conformation of β-lactams and insight into the broad spectrum of NDM-1 activityStructural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates.Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamaculans.Covalent docking of selected boron-based serine beta-lactamase inhibitors
P2860
Q27670888-22DB84DB-7B7C-47FD-9FA9-88727B8FB9F1Q27671609-0FF7A679-2E96-496A-A7F4-B177F2B40C11Q27674309-EE6090DE-8ABD-4E7B-96D4-2ED9C76B768BQ27679496-FD32C5F4-AC4C-40FD-ABCE-A66DF95725BFQ27684253-F59B0678-9D69-443A-A7E3-7ACDDF8FB6D5Q27696197-12812335-E29B-4046-AE73-3A11591D3F7DQ30539117-D3D764B7-8E05-43ED-ADDF-54995E2BB363Q34158563-5C4E54DE-F3F4-4C8C-9F71-60EEC46DA4DCQ34321556-47360077-5AF7-4580-96D0-6E3B812E4AACQ34443982-F55A1247-7492-4EF8-B08B-2C0E075DF6ECQ34505085-96B5CECF-840C-49F5-A092-064344516C45Q35620157-4346BF7B-F1E2-4F45-931C-C82CC5993564Q37023272-EE83873E-233F-4239-A96D-6F0BBA8D26EAQ37725029-8A7EFF2B-A868-40E9-A08C-1933CC86B349Q38121932-FE90FD20-D1F0-47BC-B260-2955E9B7AEFCQ38850240-4EE18E11-8445-4CBB-908B-512595385A2DQ39517261-EE4F225F-CE2B-445E-B96E-784C31295142Q39588086-452EEE45-8A72-4786-8421-33773BB1D873Q39729538-B81D08E8-C521-4653-A398-0DEE7025C0DAQ40340910-88A5DD9A-7A6E-41BA-8102-989481F8D465Q41453763-63ABECEA-B69D-4F7D-947A-205F3A4D2CBEQ41894059-C1C2AD2F-BC62-49BC-AEA2-3CAF9905B841Q41983307-75850F15-7DE5-414A-9796-299DA1F1740AQ46237711-640460D2-8423-4F59-B127-3605964A1096Q47686452-733EC2EB-60CE-4288-A229-B9B6BA8860F6Q57794478-DA5BE247-C6AF-4373-94E6-4EDABECCE3C2
P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
The mechanisms of catalysis by metallo beta-lactamases.
@en
The mechanisms of catalysis by metallo beta-lactamases.
@nl
type
label
The mechanisms of catalysis by metallo beta-lactamases.
@en
The mechanisms of catalysis by metallo beta-lactamases.
@nl
prefLabel
The mechanisms of catalysis by metallo beta-lactamases.
@en
The mechanisms of catalysis by metallo beta-lactamases.
@nl
P2860
P356
P1476
The mechanisms of catalysis by metallo beta-lactamases.
@en
P2093
Adriana Badarau
P2860
P304
P356
10.1155/2008/576297
P577
2008-01-01T00:00:00Z