[4][5] In her post-doctoral research, Partch focused on the interaction of the aryl hydrocarbon receptor nuclear translocator with its heterodimeric binding partner, the transcription factor HIF-2α, under Kevin Gardner at University of Texas Southwestern Medical Center.
[3] Partch’s early research at Oregon Health Sciences University has a broad biochemical scope, her first publication focusing on the regulation of IL-15-stimulated TNF-alpha production, a study applicable to patients with rheumatoid arthritis.
Following Partch's earliest research at OHSU, she began to home in on cryptochrome proteins and their signal transduction mechanisms, the focus of her PhD thesis.
Notably, the lab recently published work in the journal Science, elucidating the role of the protein SasA in the cooperative binding of KaiB to the KaiC hexamer in the cyanobacterial circadian clock.
[13] Previously, many models of cyanobacterial time keeping were based solely on the continuous phosphorylation of the Kai proteins (KaiA, KaiB, and KaiC) with SasA and CikA providing only input-output signaling.
These earlier dependent models relied solely on KaiC acting as the main component of the circadian oscillator with KaiA being used to phosphorylase Threonine and Serine and KaiB being used for their subsequent dephosphorylation.
It was found that SasA uses structural mimicry to help fold-switched KaiB bind to the KaiC hexamer so that the nighttime repressive complex can be formed.
[15] This maintains the rhythmicity of the circadian oscillator during limiting concentrations of KaiB by allowing both of the hexamers to auto phosphorylate and dephosphorylate threonine and serine.
Her research showed that mutations in period-altering kinases differentially regulate the activation loop switch to produce expected variations in PER2 stability, laying the groundwork for comprehending and controlling CK1's impact on circadian rhythms.