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Brendan J. McConkey

Researcher at University of Waterloo

Publications -  76
Citations -  5955

Brendan J. McConkey is an academic researcher from University of Waterloo. The author has contributed to research in topics: Proteome & Chinese hamster ovary cell. The author has an hindex of 34, co-authored 76 publications receiving 5320 citations. Previous affiliations of Brendan J. McConkey include Weizmann Institute of Science & McMaster University.

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TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

TL;DR: Findings further corroborate that TDP-43 is involved in ALS pathogenesis and reports eight missense mutations in nine individuals—six from individuals with sporadic ALS and three from those with familial ALS (FALS)—and a concurring increase of a smaller T DP-43 product.
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Promotion of Plant Growth by Bacterial ACC Deaminase

TL;DR: A review of the published work on the enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase, with an emphasis on its biochemistry, protein structure, genes, and regulation.
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The performance of current methods in ligand-protein docking

TL;DR: The methodologies discussed in detail here are generally intended for ligand–protein docking, and the methodology underlying single ligand –protein docking and database screening is quite similar, the criterion by which they are judged differs.
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Toxicity of a pah photooxidation product to the bacteria Photobacterium phosphoreum and the duckweed Lemna gibba: Effects of phenanthrene and its primary photoproduct, phenanthrenequinone

TL;DR: In this paper, the primary photoproduct of PHE, 9,10-phenanthrenequinone (PHEQ), contributes to the increased hazards of solutions containing photomodified PHE.
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New insights into 1-aminocyclopropane-1-carboxylate (ACC) deaminase phylogeny, evolution and ecological significance.

TL;DR: The results show that ACC deaminase may not only be related to plant growth promotion abilities, but may also play multiple roles in microorganism's developmental processes, and exploring the origin and functioning of this enzyme may be the key in a variety of important agricultural and biotechnological applications.