Studies on ternary metallo-beta lactamase-inhibitor complexes using electrospray ionization mass spectrometry (Q51197571)

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title

Studies on ternary metallo-beta lactamase-inhibitor complexes using electrospray ionization mass spectrometry (English)

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main subject

electrospray ionization

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2

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Neil J Oldham

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Christopher J. Schofield

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Elmar Heinzle

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object named as

Elmar Heinzle

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author name string

Nathalie Selevsek

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Benoît M R Liénard

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Uwe Heinz

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Hans-Werner Adolph

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Jean-Marie Frère

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publication date

19 May 2006

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Journal of the American Society for Mass Spectrometry

published in

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volume

17

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issue

7

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page(s)

1000-1004

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Interactions of biapenem with active-site serine and metallo-beta-lactamases

cites work

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Carbapenemases: a problem in waiting?

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Metallo-beta-lactamases: two binding sites for one catalytic metal ion?

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Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.

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Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: kinetic and spectroscopic studies

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The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding

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Screening derivatized peptide libraries for tight binding inhibitors to carbonic anhydrase II by electrospray ionization-mass spectrometry

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Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism

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Overproduction and purification of the Aeromonas hydrophila CphA metallo-beta-lactamase expressed in Escherichia coli.

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Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase

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Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase

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Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry

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Using Electrospray Ionization FTICR Mass Spectrometry To Study Competitive Binding of Inhibitors to Carbonic Anhydrase

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Carbonic Anhydrase-Inhibitor Binding: From Solution to the Gas Phase

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Zn(II) Dependence of theAeromonas hydrophilaAE036 Metallo-β-lactamase Activity and Stability†

21 January 2018

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12 December 2020

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

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12 December 2020

Study of noncovalent enzyme-inhibitor complexes and metal binding stoichiometry of matrilysin by electrospray ionization mass spectrometry

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12 December 2020

Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor

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Carbapenem-hydrolyzing beta-lactamases

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Kinetic and spectroscopic characterization of native and metal-substituted β-lactamase from Aeromonas hydrophila AE036

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10.1016/J.JASMS.2006.03.010

Identifiers

DOI

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Dimensions Publication ID

1021494963

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