Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.
about
Use of ferrous iron by metallo-β-lactamasesOvercoming differences: The catalytic mechanism of metallo-β-lactamasesComparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesMeropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopyB1-Metallo-β-Lactamases: Where Do We Stand?Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysisInvestigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor bindingNMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitorsThe structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-1.Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7.Discovery of 1-Hydroxypyridine-2(1H)-thione-6-carboxylic Acid as a First-in-Class Low-Cytotoxic Nanomolar Metallo β-Lactamase Inhibitor.The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Rhodanine as a Potent Scaffold for the Development of Broad-Spectrum Metallo-β-lactamase Inhibitors.
P2860
Q27725877-943F03AC-3D96-4100-884C-9EAB2C0A4091Q28082109-14663F47-4FA7-4803-A007-8D4FB83EC9C0Q34505085-6127F286-678E-41E7-A8DB-8AF48A5174AEQ35746276-8CE2CC2D-B4A8-4628-A098-EE2E00BF90F6Q36428146-B288BB46-C51C-4D5E-A06F-DAC8725AD9C3Q36522851-5D4295B0-AAA2-4CE7-A672-AFCF7E61F518Q36746608-1B5D9EEB-9D3D-4FAF-AAEE-4D6E2F9D7787Q36795249-B437533C-DBBC-4391-BCE1-53519A8FD53DQ36832336-D9050228-2CF2-45C7-9EB4-4B51E1A6F438Q37725029-8FE492EE-B0CC-470B-9B0A-A50C160046A2Q40456289-7B056E04-CCAA-448F-BF3E-1100BBAF4452Q46032234-2B9D1930-66BF-482F-9688-04B43AAAD0A7Q47722687-7C226A17-01C0-44E3-8587-5C7885456ADFQ47893617-D1CC6AFA-1E33-4B09-8389-106E4B28547FQ52313487-E3199827-3B4B-4AA5-AFE2-C05925F81038Q52579068-E7E02E9E-D12F-48F9-AC4B-B9720F9054F1
P2860
Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.
description
2014 nî lūn-bûn
@nan
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@ast
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@en
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@nl
type
label
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@ast
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@en
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@nl
prefLabel
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@ast
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@en
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@nl
P2093
P2860
P356
P1433
P1476
Biochemical, mechanistic, and ...... of metallo-β-lactamase VIM-2.
@en
P2093
Abraham Jon Møller
Alex Bergstrom
Amy R Marts
David L Tierney
Lindsay Moritz
Lucien Turner
Mahesh Aitha
Michael W Crowder
Richard C Page
P2860
P304
P356
10.1021/BI500916Y
P407
P577
2014-11-13T00:00:00Z