Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution
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Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesisCrystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities.Structural effects of the active site mutation cysteine to serine inBacillus cereuszinc-β-lactamaseSuccinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamaseThe 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captoprilMalignant brain tumor repeats: a three-leaved propeller architecture with ligand/peptide binding pocketsStructure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-LactamaseSolution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidIdentification of residues critical for metallo-beta-lactamase function by codon randomization and selectionThe catalytic Tyr-9 of glutathione S-transferase A1-1 controls the dynamics of the C terminusMetallo-beta-lactamases: the quiet before the storm?Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensisOvercoming antimicrobial resistance by targeting resistance mechanisms.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Dilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies.Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopyB1-Metallo-β-Lactamases: Where Do We Stand?Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) InhibitorsConformational changes in the metallo-beta-lactamase ImiS during the catalytic reaction: an EPR spectrokinetic study of Co(II)-spin label interactions.Buffer interference with protein dynamics: a case study on human liver fatty acid binding protein.An Update on the Status of Potent Inhibitors of Metallo-β-Lactamases.Fragment-based inhibitor discovery against β-lactamaseFunctional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.The mechanisms of catalysis by metallo beta-lactamases.Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases.Functional analysis of the active site of a metallo-beta-lactamase proliferating in Japan.Standard numbering scheme for class B beta-lactamasesThe Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.MOPS and coxsackievirus B3 stability.Effect of Tris, MOPS, and phosphate buffers on the hydrolysis of polyethylene terephthalate films by polyester hydrolases.Pneumococcal phosphorylcholine esterase, Pce, contains a metal binuclear center that is essential for substrate binding and catalysisBulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases.Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase.Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: kinetic and spectroscopic studies.Binding of D- and L-captopril inhibitors to metallo-beta-lactamase studied by polarizable molecular mechanics and quantum mechanics.Molecular dynamics simulations of the dinuclear zinc-beta-lactamase from Bacteroides fragilis complexed with imipenem.The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.Biochemical requirements for inhibition of Connexin26-containing channels by natural and synthetic taurine analogs.Modeling of the metallo-beta-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding.
P2860
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P2860
Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@ast
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@en
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@nl
type
label
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@ast
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@en
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@nl
prefLabel
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@ast
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
@en
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
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P2093
P3181
P356
P1433
P1476
Unanticipated inhibition of th ...... hic study at 1.85-A resolution
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P2093
P304
P3181
P356
10.1021/BI9730339
P407
P577
1998-05-12T00:00:00Z