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Jeffrey L. Price

Jeffrey Price
Born 1958
New York City, New York
Residence United States
Fields Chronobiology, Neurology, Cognitive Neuroscience
Institutions University of Missouri-Kansas City
Member of Society for Research on Biological Rhythms
Alma mater Undergraduate: College of William and Mary
Ph.D.: Johns Hopkins University
Known for Circadian rhythms research
Website
sbs.umkc.edu

Jeffrey L. Price (born 1958) is an American researcher and author in the fields of circadian rhythms and molecular biology. His chronobiology work with Drosophila melanogaster has led to the discoveries of the circadian genes timeless (tim) and doubletime (dbt), and the doubletime regulators spaghetti (SPAG) and bride of doubletime (BDBT).

Price was born in New York City and raised in New Jersey and Virginia. He graduated from the College of William and Mary with a Bachelor of Science degree in Biology, and later received his Ph.D. in Biology from Johns Hopkins University. He completed his postdoctoral training in Taiwan, Republic of China, and in the lab of Michael Young at Rockefeller University through the Howard Hughes Medical Institute. Price is currently an associate professor in the School of Biological Sciences at University of Missouri-Kansas City, and an associate professor in the department of Neurology and Cognitive Neuroscience at the University of Missouri-Kansas City School of Medicine.

Price's research centers around the molecular mechanisms of circadian rhythms, using Drosophila melanogaster as model organisms. He is specifically interested in the role of protein kinases in clock function, and using forward genetics screens Price has contributed to the identification and characterization of many critical elements of the Drosophila circadian clock.

The molecular circadian clock of D. melanogaster can be described as a feedback loop of transcription and translation, in which the proteins CLOCK and CYCLE act as transcriptional activators of the period and timeless genes. Their protein products, PER and TIM, respectively, dimerize and translocate to the nucleus after phosphorylation by DBT. In the nucleus, PER/TIM heterodimers bind to and suppress CLK/CYC heterodimers to inhibit the transcription of period and timeless, resulting in daily oscillations of PER and TIM. DBT is itself regulated by BDBT and SPAG, which stimulate its kinase activity toward PER and increase the cytoplasmic stability of DBT, respectively.


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