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Full-Text Articles in Molecular Biology
Probing Interactions Between Canonical Nox Domains, Akua Acheampong
Probing Interactions Between Canonical Nox Domains, Akua Acheampong
Master of Science in Integrative Biology Theses
NAPDH oxidase enzymes (NOXes) reduce molecular oxygen to superoxide and other ROS. NOXes contain a catalytic core comprising a heme-containing transmembrane (TM) domain and a cytoplasmic dehydrogenase (DH) domain that binds the substrate NADPH and the cofactor. Previously, NOXes were only characterized in eukaryotes, but have recently been identified in prokaryotes, namely bacteria. Due to their constitutive activity and solubility in detergent, bacterial NOXes, such as Streptococcus Pneumoniae NOX, have emerged as a model for studying NOXes. Past research studies in NOXes have identified conserved, putative interacting regions at the interface of the TM and DH domains: the TM B-loop, …
Virulence Factors Of Aeromonas Hydrophila: In The Wake Of Reclassification, Cody R. Rasmussen-Ivey, Maria J. Figueras, Donald Mcgarey, Mark R. Liles
Virulence Factors Of Aeromonas Hydrophila: In The Wake Of Reclassification, Cody R. Rasmussen-Ivey, Maria J. Figueras, Donald Mcgarey, Mark R. Liles
Faculty Articles
The ubiquitous “jack-of-all-trades,” Aeromonas hydrophila, is a freshwater, Gram-negative bacterial pathogen under revision in regard to its phylogenetic and functional affiliation with other aeromonads. While virulence factors are expectedly diverse across A. hydrophila strains and closely related species, our mechanistic knowledge of the vast majority of these factors is based on the molecular characterization of the strains A. hydrophila AH-3 and SSU, which were reclassified as A. piscicola AH-3 in 2009 and A. dhakensis SSU in 2013. Individually, these reclassifications raise important questions involving the applicability of previous research on A. hydrophila virulence mechanisms; however, this issue is exacerbated by …