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Subject Areas on Research
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De Novo
Design, Solution Characterization, and Crystallographic Structure of an Abiological Mn-Porphyrin-Binding Protein Capable of Stabilizing a Mn(V) Species.
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A genetic analysis of nitrosative stress.
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Activated conformers of Escherichia coli sulfite reductase heme protein subunit.
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Alkaline low spin form of sulfite reductase hemeprotein subunit.
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Bacterial flavohemoglobin: a molecular tool to probe mammalian nitric oxide biology.
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Biochemistry of soluble guanylate cyclase.
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Biological chemistry of carbon monoxide.
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Carbon monoxide binding by simple heme proteins under photodissociating conditions.
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Carbon monoxide, reactive oxygen signaling, and oxidative stress.
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Carbon monoxide-driven reduction of ferric heme and heme proteins.
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Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase.
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Compartmentalized nitrosation and nitration in mitochondria.
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Differential regulation of beta-chemokines in children with Plasmodium falciparum malaria.
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Electron acceptor function of O2 in radical N-demethylation reactions catalyzed by hemeproteins.
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Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and Fe4S4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit.
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Elevated nitric oxide production in children with malarial anemia: hemozoin-induced nitric oxide synthase type 2 transcripts and nitric oxide in blood mononuclear cells.
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Engineered modular recombinant transporters: application of new platform for targeted radiotherapeutic agents to alpha-particle emitting 211 At.
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Enzymes that counteract nitrosative stress promote fungal virulence.
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Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes.
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HGT in the human and skin commensal Malassezia: A bacterially derived flavohemoglobin is required for NO resistance and host interaction.
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Heme proteins and nitric oxide (NO): the neglected, eloquent chemistry in NO redox signaling and regulation.
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Increasing a microscope's effective field of view via overlapped imaging and machine learning.
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Induction of Neuroinflammation and Neurotoxicity by Synthetic Hemozoin.
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Intraleucocyte malaria pigment in asymptomatic and uncomplicated malaria.
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Intraleucocytic malaria pigment and clinical severity of malaria in children.
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On the reaction of ferric heme proteins with nitrite and sulfite.
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Oxygen toxicity and iron accumulation in the lungs of mice lacking heme oxygenase-2.
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Preliminary X-ray diffraction studies on the hemoprotein subunit of Escherichia coli sulfite reductase.
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Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.
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Protection from nitrosative stress by yeast flavohemoglobin.
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Protection from nitrosative stress: a central role for microbial flavohemoglobin.
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Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands.
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Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit.
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Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow.
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Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components.
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Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. V. Studies with the Escherichia coli hemoflavoprotein depleted of flavin mononucleotide: distinct roles for the flavin adenine dinucleotide and flavin mononucleotide prosthetic groups in catalysis.
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Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme.
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Reduced peripheral PGE2 biosynthesis in Plasmodium falciparum malaria occurs through hemozoin-induced suppression of blood mononuclear cell cyclooxygenase-2 gene expression via an interleukin-10-independent mechanism.
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Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.
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Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.
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Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes.
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Siroheme and sirohydrochlorin. The basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases.
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Siroheme: a new prosthetic group participating in six-electron reduction reactions catalyzed by both sulfite and nitrite reductases.
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Spectroelectrochemistry of heme proteins: effects of active-site heterogeneity on Nernst plots.
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Suppression of prostaglandin E2 by malaria parasite products and antipyretics promotes overproduction of tumor necrosis factor-alpha: association with the pathogenesis of childhood malarial anemia.
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The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo.