Profiling interactions of vaborbactam with metallo-β-lactamases

Profiling interactions of vaborbactam with metallo-β-lactamases

Bibliografski detalji
Glavni autori:	Langley, G, Cain, R, Tyrrell, J, Hinchliffe, P, Calvopiña, K, Tooke, C, Widlake, E, Dowson, C, Spencer, J, Walsh, T, Schofield, C, Brem, J
Format:	Journal article
Jezik:	English
Izdano:	Elsevier 2019

Slični predmeti

Bicyclic boronate VNRX-5133 inhibits metallo- and serine-β-lactamases
od: Krajnc, A, i dr.
Izdano: (2019)

Faropenem reacts with serine and metallo-β-lactamases to give multiple products
od: Lucic, A, i dr.
Izdano: (2021)

Cyclobutanone mimics of intermediates in metallo-β-lactamase catalysis.
od: Abboud, M, i dr.
Izdano: (2017)

Assay platform for clinically relevant metallo-β-lactamases.
od: van Berkel, S, i dr.
Izdano: (2013)

Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
od: Brem, J, i dr.
Izdano: (2016)

Use of ferrous iron by metallo-β-lactamases.
od: Cahill, S, i dr.
Izdano: (2016)

Interaction of Avibactam with Class B Metallo-β-Lactamases.
od: Abboud, M, i dr.
Izdano: (2016)

Structural basis of metallo-β-lactamase inhibition by N-sulfamoylpyrrole-2-carboxylates
od: Farley, AJM, i dr.
Izdano: (2021)

New Delhi metallo-β-lactamase-1 catalyses avibactam and aztreonam hydrolysis.
od: Lohans, C, i dr.
Izdano: (2017)

Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases
od: Salimraj, R, i dr.
Izdano: (2018)

The chemical biology of human metallo-β-lactamase fold proteins.
od: Pettinati, I, i dr.
Izdano: (2016)

Interactions of hydrolyzed β-lactams with the L1 metallo-β-lactamase: Crystallography supports stereoselective binding of cephem/carbapenem products
od: Hinchliffe, P, i dr.
Izdano: (2023)

Structural basis of metallo-β-lactamase inhibition by captopril stereoisomers
od: Brem, J, i dr.
Izdano: (2015)

Cyclic boronates as versatile scaffolds for KPC-2 β-lactamase inhibition
od: Tooke, C, i dr.
Izdano: (2020)

Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors
od: Brem, J, i dr.
Izdano: (2021)

Chromophore-linked substrate (CLS405): probing metallo-β-lactamase activity and inhibition.
od: Makena, A, i dr.
Izdano: (2013)

Chromophore-linked substrate (CLS405): Probing metallo-β-lactamase activity and inhibition
od: Makena, A, i dr.
Izdano: (2013)

Mechanistic insights into β-lactamase-catalysed carbapenem degradation through product characterisation
od: Lohans, C, i dr.
Izdano: (2019)

In silico fragment based design identifies subfamily B1 metallo-β-lactamase inhibitors
od: Cain, R, i dr.
Izdano: (2017)

Studies on the inhibition of AmpC and other β-lactamases by cyclic boronates
od: Cahill, S, i dr.
Izdano: (2019)

Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition.
od: Brem, J, i dr.
Izdano: (2014)

Molecular basis of class A β-lactamase inhibition by relebactam
od: Tooke, C, i dr.
Izdano: (2019)

NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitors
od: Li, G, i dr.
Izdano: (2017)

“To cross-seed or not to cross-seed”: A pilot study using metallo-β-lactamases
od: Abuhammad, A, i dr.
Izdano: (2016)

Structural and Biochemical Characterization of Rm3, a SubClass B3 Metallo-β-Lactamase Identified from a Functional Metagenomic Study.
od: Salimraj, R, i dr.
Izdano: (2016)

19F-NMR reveals the role of mobile loops in product and inhibitor binding by the São Paolo metallo-β-lactamase
od: Abboud, M, i dr.
Izdano: (2017)

Comparison of verona integron-borne metallo-β-lactamase (VIM) variants reveals differences in stability and inhibition profiles
od: Makena, A, i dr.
Izdano: (2016)

Structural/mechanistic insights into the efficacy of nonclassical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates
od: Calvopiña, K, i dr.
Izdano: (2017)

Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy.
od: Rydzik, A, i dr.
Izdano: (2014)

Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition
od: Li, G, i dr.
Izdano: (2017)

New Delhi metallo-beta-lactamase 1 catalyzes avibactam and aztreonam hydrolysis
od: Lohans, C, i dr.
Izdano: (2017)

Synthesis of metallo-beta-lactamase inhibitors
od: Walter, M, i dr.
Izdano: (1997)

Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.
od: Makena, A, i dr.
Izdano: (2014)

In vitro and in vivo activity of ML302F: a thioenolate inhibitor of VIM-subfamily metallo β-lactamases
od: Betts, J, i dr.
Izdano: (2015)

A new mechanism for β-lactamases: Class D enzymes degrade 1β-methyl carbapenems through lactone formation
od: Lohans, C, i dr.
Izdano: (2018)

Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-β-lactamases
od: Zhang, D, i dr.
Izdano: (2018)

Structural and biochemical characterisation of bacterial metallo-β-lactamases
od: Makena, A
Izdano: (2016)

Broad spectrum β-lactamase inhibition by a thioether substituted bicyclic boronate
od: Parkova, A, i dr.
Izdano: (2019)

Metallo-β-lactamase-mediated antimicrobial resistance and progress in inhibitor discovery
od: Yang, Y, i dr.
Izdano: (2023)

Inhibitors of the FEZ-1 metallo-beta-lactamase.
od: Liénard, B, i dr.
Izdano: (2007)