Robbyn L. Tuinstra

TL;DR: Results indicate that the increase in mitochondrial reactive oxygen species can result in biochemical aberrations with features reminiscent of mitochondrial myopathy, Friedreich ataxia, and 3-hydroxy-3-methylglutaryl-CoA lyase deficiency.

TL;DR: The results demonstrate that the functional repertoire and regulation of a single naturally occurring amino acid sequence can be expanded by access to a set of highly dissimilar native-state structures.

TL;DR: NMR data support the conclusion that the chemokine fold of Ltn10 is responsible for receptor activation, and the role of amino- and carboxyl-terminal residues in Ltn-mediated receptor activation is examined.

TL;DR: Conformational variants like CC5 are valuable tools for elucidating the biological relevance of the XCL1 native-state interconversion and will assist in future antiviral and functional studies.

TL;DR: A human mutation that substitutes lysine for glutamate 279 produces a protein that is sufficiently stable for isolation and retains substantial catalytic activity, however, thermal inactivation experiments demonstrate that E279A is much less stable than wild-type enzyme.