Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.
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Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionHow structural and physicochemical determinants shape sequence constraints in a functional enzymeQuantitative Description of a Protein Fitness Landscape Based on Molecular Features.Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.B1-Metallo-β-Lactamases: Where Do We Stand?Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamaseCrystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Insights into an evolutionary strategy leading to antibiotic resistance.Progress toward inhibitors of metallo-β-lactamases.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.19 F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-Lactamase.Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation.Shaping substrate selectivity in a broad spectrum metallo-β-lactamase.
P2860
Q34418071-C02C2516-50E3-4971-B6D3-E0C1E0A46FE7Q35565904-EC9F06F3-612A-4148-A628-9A0FDC8EAC9BQ35765112-E0ABE25D-8D21-4E9A-B77F-78C9A58C8472Q36428146-EAD8D2AB-3509-40D5-B031-0AF9471BF423Q36571912-D1095A08-3C4A-4EB0-8787-45665C046D36Q36746608-ACA7EAEF-3033-4636-9F66-DB4AE67569A0Q37017171-97A098B7-A6AC-4632-978D-DCB3192AD266Q37287914-BAF71493-096C-4D31-A9BE-5C358FB295A1Q37578905-10CA00E1-AB66-42BB-A645-23B65C15115BQ38683817-78E43EC0-3F98-48E8-9FC3-1FEF68E7FD50Q40040050-624FD558-098B-45A6-96A4-63CA8C43EF79Q41775520-69BF31AC-92EE-4E51-92AB-C92F9725B864Q46237711-D8A54631-CFBA-4E55-8012-1D07620ACF47Q47737111-AB8C9F74-DBDC-4EC2-BA36-C51F2F10A238Q49874620-8FEF90DC-B2E7-495C-891D-4924E2D018DF
P2860
Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին 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
Host-specific enzyme-substrate ...... ted by second sphere residues.
@ast
Host-specific enzyme-substrate ...... ted by second sphere residues.
@en
type
label
Host-specific enzyme-substrate ...... ted by second sphere residues.
@ast
Host-specific enzyme-substrate ...... ted by second sphere residues.
@en
prefLabel
Host-specific enzyme-substrate ...... ted by second sphere residues.
@ast
Host-specific enzyme-substrate ...... ted by second sphere residues.
@en
P2093
P2860
P1433
P1476
Host-specific enzyme-substrate ...... ted by second sphere residues.
@en
P2093
Alejandro J Vila
Diego M Moreno
Lisandro J González
P2860
P304
P356
10.1371/JOURNAL.PPAT.1003817
P577
2014-01-02T00:00:00Z