2011 - Fellow of the Royal Society of Canada Academy of Science
Joel H. Weiner mainly focuses on Escherichia coli, Biochemistry, Enzyme, Redox and Fumarate reductase. The study incorporates disciplines such as Molecular biology, Reductase and Plasmid in addition to Escherichia coli. His studies in Reductase integrate themes in fields like Dimethyl sulfoxide and Mutant.
His work is connected to Protein subunit, Cofactor, Periplasmic space, Peptide sequence and Secretion, as a part of Biochemistry. His Redox study integrates concerns from other disciplines, such as Glutathione, Electron transfer and Nitrate reductase. In his study, which falls under the umbrella issue of Fumarate reductase, Molecular mass is strongly linked to Membrane.
Joel H. Weiner mainly investigates Biochemistry, Escherichia coli, Stereochemistry, Fumarate reductase and Enzyme. His Biochemistry research focuses on Protein subunit, Succinate dehydrogenase, Cofactor, Periplasmic space and Heme. His Escherichia coli research integrates issues from Molecular biology, Mutant, Plasmid and Reductase.
His studies deal with areas such as Sulfide quinone oxidoreductase, Oxidoreductase, Crystal structure, Nitrate reductase and Electron transfer as well as Stereochemistry. His research integrates issues of Electron paramagnetic resonance, Redox and Electron transport chain in his study of Electron transfer. The Fumarate reductase study combines topics in areas such as Crystallography, Membrane and Flavin group.
Joel H. Weiner spends much of his time researching Stereochemistry, Cofactor, Biochemistry, Acidithiobacillus ferrooxidans and Sulfide quinone oxidoreductase. His Stereochemistry research is multidisciplinary, incorporating elements of Sulfite oxidase, Molybdenum, Oxidoreductase, Heme and Electron transfer. His research in Cofactor intersects with topics in Protein subunit and Quinone oxidoreductase.
His Protein subunit research incorporates themes from Periplasmic space, Reductase and Titration. His study in Biochemistry concentrates on Fumarate reductase, Flavin adenine dinucleotide, Succinate dehydrogenase, Quinone binding and Escherichia coli. His biological study spans a wide range of topics, including Chromatography, Reproducibility and Liquid chromatography–mass spectrometry.
The scientist’s investigation covers issues in Enzyme, Cofactor, Biochemistry, Stereochemistry and Electron transfer. His study in Cofactor is interdisciplinary in nature, drawing from both Cytochrome, Protein subunit and Biosynthesis. His Biochemistry research includes themes of Metabolome and Bioinformatics.
His research in Stereochemistry intersects with topics in Oxidoreductase, Organic chemistry and Sulfite oxidase. His work carried out in the field of Electron transfer brings together such families of science as Inorganic chemistry, Redox and Sulfur. His research on Escherichia coli focuses in particular on Bacterial outer membrane.
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Reversible Electrochemistry of Fumarate Reductase Immobilized on an Electrode Surface. Direct Voltammetric Observations of Redox Centers and Their Participation in Rapid Catalytic Electron Transport
Artur Sucheta;Richard Cammack;Joel Weiner;Fraser A. Armstrong.
Biochemistry (1993)
Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli.
Stewart T. Cole;Caro Condon;Bernard D. Lemire;Joel H. Weiner.
Biochimica et Biophysica Acta (1985)
Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli.
Guijin Zhang;Stephen Brokx;Joel H Weiner.
Nature Biotechnology (2006)
Overproduction of fumarate reductase in Escherichia coli induces a novel intracellular lipid-protein organelle.
J H Weiner;B D Lemire;M L Elmes;R D Bradley.
Journal of Bacteriology (1984)
Purification and characterization of membrane-bound fumarate reductase from anaerobically grown Escherichia coli
Peter Dickie;Joel H. Weiner.
Biochemistry and Cell Biology (1979)
Glutathione is a target in tellurite toxicity and is protected by tellurite resistance determinants in Escherichia coli
Raymond J Turner;Yair Aharonowitz;Joel H Weiner;Diane E Taylor.
Canadian Journal of Microbiology (2001)
The entericidin locus of Escherichia coli and its implications for programmed bacterial cell death.
Russell E Bishop;Brenda K Leskiw;Robert S Hodges;Cyril M Kay.
Journal of Molecular Biology (1998)
Structural and biochemical identification of a novel bacterial oxidoreductase.
Lodovica Loschi;Stephen J. Brokx;Tanya L. Hills;Glen Zhang.
Journal of Biological Chemistry (2004)
Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli.
A Schryvers;E Lohmeier;J H Weiner.
Journal of Biological Chemistry (1978)
Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein.
Gillian D. Henry;Joel H. Weiner;Brian D. Sykes.
Biochemistry (1986)
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