https://matthewslab.org/publication/hydrazines-as-versatile-chemical-biology-probes-and-drug-discovery-tools-for-cofactor-dependent-enzymes/2020-09-28T18:18:41+00:00https://matthewslab.org/publication/metal-free-class-ie-ribonucleotide-reductase-from-pathogens-initiates-catalysis-with-a-tyrosine-derived-dihydroxyphenylalanine-radical/2020-10-15T19:33:54+00:00https://matthewslab.org/publication/evidence-for-modulation-of-oxygen-rebound-rate-in-control-of-outcome-by-ironii-and-2-oxogl-utarate-dependent-oxygenases/2020-09-28T18:19:21+00:00https://matthewslab.org/publication/vanadyl-as-a-stable-structural-mimic-of-reactive-ferryl-intermediates-in-mononuclear-nonheme-iron-enzymes/2020-09-28T18:17:47+00:00https://matthewslab.org/publication/design-of-benzoxathiazin-3-one-11-dioxides-as-a-new-class-of-irreversible-serine-hydrolase-inhibitors-discovery-of-a-uniquely-selective-pnpla4-inhibitor/2020-09-28T18:17:09+00:00https://matthewslab.org/publication/chemoproteomic-profiling-and-discovery-of-protein-electrophiles-in-human-cells/2020-10-15T19:34:56+00:00https://matthewslab.org/publication/chemical-proteomic-profiling-of-human-methyltransferases/2020-09-28T18:16:26+00:00https://matthewslab.org/publication/design-of-activated-serine-containing-catalytic-triads-with-atomic-level-accuracy/2020-10-15T19:35:29+00:00https://matthewslab.org/publication/highly-selective-inhibitors-of-monoacylglycerol-lipase-bearing-a-reactive-group-that-is-bioisosteric-with-endocannabinoid-substrates/2020-09-28T18:15:21+00:00https://matthewslab.org/publication/electronic-structure-of-the-ferryl-intermediate-in-the-a-ketoglutarate-dependent-non-heme-iron-halogenase-syrb2-contributions-to-h-atom-abstraction-reactivity/2020-09-28T18:14:41+00:00https://matthewslab.org/publication/direct-nitration-and-azidation-of-aliphatic-carbons-by-an-iron-dependent-halogenase/2020-10-15T19:35:47+00:00https://matthewslab.org/publication/elucidation-of-the-feivo-intermediate-in-the-catalytic-cycle-of-the-halogenase-syrb2/2020-10-15T19:39:10+00:00https://matthewslab.org/publication/novel-approaches-for-the-accumulation-of-oxygenated-intermediates-to-multi-millimolar-concentrations/2020-09-24T15:29:54+00:00https://matthewslab.org/publication/the-nonribosomal-peptide-synthetase-enzyme-ddad-tethers-nb-fumaramoyl-l-23-diaminopropionate-for-feii-a-ketoglutarate-dependent-epoxidation-by-ddac-during-dapdiamide-antibiotic-biosynthesis/2020-09-28T18:25:32+00:00https://matthewslab.org/publication/remote-enzyme-microsurgery/2020-09-24T15:23:10+00:00https://matthewslab.org/publication/substrate-positioning-controls-the-partition-between-halogenation-and-hydroxylation-in-the-aliphatic-halogenase-syrb2/2020-10-16T18:51:31+00:00https://matthewslab.org/publication/substrate-triggered-formation-and-remarkable-stability-of-the-c-h-bond-cleaving-chloroferryl-intermediate-in-the-aliphatic-halogenase-syrb2/2020-09-28T18:26:54+00:00https://matthewslab.org/publication/myo-inositol-oxygenase-a-radical-new-pathway-for-o2/2020-10-15T19:40:12+00:00https://matthewslab.org/publication/aurf-from-streptomyces-thioluteus-and-a-possible-new-family-of-manganese-iron-oxygenases/2020-09-28T18:28:31+00:00https://matthewslab.org/publication/spectroscopic-evidence-for-a-high-spin-br-feiv-oxo-intermediate-in-the-a-ketoglutarate-dependent-halogenase-cytc3-from-streptomyces/2020-09-28T18:14:02+00:00https://matthewslab.org/publication/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-coii-substituted-enzyme/2020-09-28T18:29:30+00:00https://matthewslab.org/publication/a-five-coordinate-metal-center-in-coii-substituted-vanx/2020-10-16T18:52:03+00:00https://matthewslab.org/publication/mechanisms-of-2-oxoglutarate-dependent-oxygenases-the-hydroxylation-paradigm-and-beyond/2020-10-16T18:56:24+00:00https://matthewslab.org/publication/aza-b-lactam-compounds-and-methods-of-using/2020-09-23T23:42:42+00:00https://matthewslab.org/publication/discovery-of-electrophiles-and-profiling-of-enzyme-cofactors/2021-02-10T18:37:39+00:00https://matthewslab.org/publication/chemoproteomic-profiling-of-protein-electrophilic-and-oxidative-post-translational-modifications/2020-10-05T12:36:23+00:00https://matthewslab.org/publication/activity-based-hydrazine-probes-for-protein-profiling-of-electrophilic-functionality-in-therapeutic-targets/2021-11-09T20:10:14+00:00https://matthewslab.org/publication/discovery-of-potent-and-selective-inhibitors-against-protein-derived-electrophilic-cofactors/2023-01-30T15:09:24+00:00https://matthewslab.org/publication/characterizing-metabolic-drivers-of-clostridioides-difficile-infection-with-activity-based-hydrazine-probes/2023-01-30T15:15:56+00:00