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Full-Text Articles in Chemistry

Dominant Negative Effects By Inactive Spa47 Mutants Inhibit T3ss Function And Shigella Virulence, Jamie L. Burgess, Heather B. Case, R. Alan Burgess, Nicholas E. Dickenson Jan 2020

Dominant Negative Effects By Inactive Spa47 Mutants Inhibit T3ss Function And Shigella Virulence, Jamie L. Burgess, Heather B. Case, R. Alan Burgess, Nicholas E. Dickenson

Chemistry and Biochemistry Faculty Publications

Type three secretion systems (T3SS) are complex nano-machines that evolved to inject bacterial effector proteins directly into the cytoplasm of eukaryotic cells. Many high-priority human pathogens rely on one or more T3SSs to cause disease and evade host immune responses, underscoring the need to better understand the mechanisms through which T3SSs function and their role(s) in supporting pathogen virulence. We recently identified the Shigella protein Spa47 as an oligomerization-activated T3SS ATPase that fuels the T3SS and supports overall Shigella virulence. Here, we provide both in vitro and in vivo characterization of Spa47 oligomerization and activation in the presence and absence …


Design, Synthesis, And Characterization Of Chemical Tools To Study Peroxisomal Import, Jhalak N. Timilsena Jan 2020

Design, Synthesis, And Characterization Of Chemical Tools To Study Peroxisomal Import, Jhalak N. Timilsena

Masters Theses

Peroxisomes are dynamic and interconnected single lipid membrane bound organelles found in the eukaryotic cells which are involved in various biochemical processes including the b-oxidation of very long chain and branched chain fatty acids, metabolism of reactive oxygen and nitrogen species, and reduction of hydrogen peroxide among others. These organelles are known to host numerous proteins and enzymes depending on the cellular environment. All of the proteins needed in the peroxisomes are encoded in the nucleus and synthesized in the cytosol which are then transported to the peroxisomes with the help of a sophisticated protein-transport machinery. Pex5 is one of …