Physician
Emergency Medicine
Dr. Michael W. Crowder, MD
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Michael Crowder works in the field of Emergency Medicine. He attended Drexel University College of Medicine. Michael W. Crowder, MD is a published physician as well. He has 71 publications published. The latest was: Kinetic mechanism of metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.
Publications
- Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding.
- Targeting metallo-carbapenemases via modulation of electronic properties of cephalosporins.
- Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-β-lactamase VIM-2.
- Spectroscopic and Mechanistic Studies of Heterodimetallic Forms of Metallo-β-lactamase NDM-1.
- Dilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies.
- New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases.
- Raman Spectra of Interchanging ?-Lactamase Inhibitor Intermediates on the Millisecond Time Scale.
- Novel fluorescent risedronates: Synthesis, photodynamic inactivation and imaging of Bacillus subtilis.
- A novel fluorogenic substrate for dinuclear Zn(II)-containing metallo-?-lactamases.
- Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1.
- Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli.
- Zn(II) Binding to Escherichia coli 70S Ribosomes.
- Structural and Kinetic Studies on Metallo-?-lactamase IMP-1.
- Converting GLX2-1 into an active glyoxalase II.
- Arabidopsis thaliana mitochondrial glyoxalase 2-1 exhibits beta-lactamase activity.
- Motion of the zinc ions in catalysis by a dizinc metallo-beta-lactamase.
- Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.
- Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme.
- Structure and mechanism of copper- and nickel-substituted analogues of metallo-beta-lactamase L1.
- Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.
- Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein.
- Metal content of metallo-beta-lactamase L1 is determined by the bioavailability of metal ions.
- Folding strategy to prepare Co(II)-substituted metallo-beta-lactamase L1.
- Conformational changes in the metallo-beta-lactamase ImiS during the catalytic reaction: an EPR spectrokinetic study of Co(II)-spin label interactions.
- Structural basis for the role of Asp-120 in metallo-beta-lactamases.
- Time-dependent translational response of E. coli to excess Zn(II).
- X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria.
- Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid-freeze quench EPR studies on the Co(II)-substituted enzyme.
- Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
- Mechanistic studies on the mononuclear ZnII-containing metallo-beta-lactamase ImiS from Aeromonas sobria.
- Transcriptional response of Escherichia coli to TPEN.
- Over-expression, purification, and characterization of aminopeptidase N from Escherichia coli.
- Sequential binding of cobalt(II) to metallo-beta-lactamase CcrA.
- Structural studies on a mitochondrial glyoxalase II.
- Spectroscopic studies on cobalt(II)-substituted metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria.
- A five-coordinate metal center in Co(II)-substituted VanX.
- Direct evidence that the reaction intermediate of metallo-beta-lactamase L1 is metal bound.
- Probing the dynamics of a mobile loop above the active site of L1, a metallo-beta-lactamase from Stenotrophomonas maltophilia, via site-directed mutagenesis and stoppe...
- Fractionation of soluble proteins in Escherichia coli using DEAE-, SP-, and phenyl sepharose chromatographies.
- L-alanine-p-nitroanilide is not a substrate for VanX.
- In vivo folding of recombinant metallo-beta-lactamase L1 requires the presence of Zn(II).
- Over-expression, purification, and characterization of metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria.
- A method for removing ethylenediaminetetraacetic acid from apo-proteins.
- Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis.
- Explaining the inhibition of glyoxalase II by 9-fluorenylmethoxycarbonyl-protected glutathione derivatives.
- Characterization of chromodulin by X-ray absorption and electron paramagnetic resonance spectroscopies and magnetic susceptibility measurements.
- Characterization of monomeric L1 metallo-beta -lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis.
- Control and statistical analysis of in vitro reporter gene assays.
- 3-alkoxy-5-isoxazolidinones mimic beta-lactams.
- Analysis of three overexpression systems for VanX, the Zinc(II) dipeptidase required for high-level vancomycin resistance in bacteria.
- Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo.
- Mutational analysis of metallo-beta-lactamase CcrA from Bacteroides fragilis.
- Kinetic mechanism of metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.
- Phosphonamidate and phosphothioate dipeptides as potential inhibitors of VanX.
- Inhibition studies on the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.
- Continuous assay for VanX, the D-alanyl-D-alanine dipeptidase required for high-level vancomycin resistance.
- The problem of a solvent exposable disulfide when preparing Co(II)-substituted metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.
- Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis.
- Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis.
- Phosphinate, sulfonate, and sulfonamidate dipeptides as potential inhibitors of Escherichia coli aminopeptidase N.
- Probing the adaptive response of Escherichia coli to extracellular Zn(II).
- Homo-cysteinyl peptide inhibitors of the L1 metallo-beta-lactamase, and SAR as determined by combinatorial library synthesis.
- Combating vancomycin resistance in bacteria: targeting the D-ala-D-ala dipeptidase VanX.
- Site-selective binding of Zn(II) to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.
- Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli.
- Arabidopsis thaliana GLX2-1 contains a dinuclear metal binding site, but is not a glyoxalase 2.
- Molecular dynamic simulations of the metallo-beta-lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor.
- The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family.
- The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity.
- Absence of ZnuABC-mediated zinc uptake affects virulence-associated phenotypes of uropathogenic Escherichia coli CFT073 under Zn(II)-depleted conditions.
Schools
Drexel University College of Medicine
Doctors Specialties
- Emergency Medicine
Accepted Insurances
Education
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Wright State University -
David Grant Medical Center -
Drexel University College of Medicine
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