My current project entitled: "Therapeutic Strategies for Anemia in 3q26 Rearranged Leukemia" received a two-year Ruth L. Kirschstein Predoctoral Individual National Research Service Award (NRSA) (Parent F31) from The National Institutes of Health (NIH) / National Heart, Lung, and Blood Institute (NHLBI). (link)
- Advancing our understanding of the molecular mechanism by which the oncogene EVI1 reprograms hematopoietic differentiation to produce erythroid blockage.
- Uncovering new molecular strategies that reverse anemia-associated leukemia.
- Together, these studies will improve patients’ survival rates, and reduce lethality of leukemia, especially 3q26 rearrangements leukemia.
During my rotation in Smrcka Lab, my project was a part of a larger project aiming to test the inhibitory effect of small molecules (Selenocystamine) on Gβγ signaling after knocking out the expression of Gβ2 and point mutating Gβ1 (C204A). We used CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) to achieve Gβ2 Knockout and Gβ1 Point Mutation (Gβ1 C204A).
- Achieving a cell line containing Gβ2 knock out and Gβ1 point mutation (C204A) will help shed the light on how Selenocystamine modifies Gβγ and inhibits interaction with its effector, blocking the downstream signaling.
During my rotation in Perkins Lab, I had two objectives: First, purifying and crystalizing PRDM3 protein for X-ray crystallography, and second, studying PRDM3 protein binding affinities to DNA and SAM.Significance/Rational
- Understanding the 3D structure of PRDM3 protein will help shed lights on how PRDM3 participates in leukemia carcinogenesis and thus it serves as the first step toward finding a new therapeutic methods and drugs that target PRDM3 overexpression and serves as potential leukemia therapy.
- Studying the function of PRDM3 and its downstream signaling pathway in physiological and pathological conditions is as important as studying its 3D structure. PRDM3 binds to DNA and SAM and the binding is necessary for PRDM3 to function as a lysine methyltransferase.
During my rotation in Yule Lab, I had two objectives: First, understanding Inositol trisphosphate receptor (IP3R) interdomain interaction, and second, generation of human IP3R1 truncation fragments expressed in some Gillespie syndrome patients.
- Understanding IP3R interdomain interactions will help shed lights on how the receptor signals or functions.
- Creating the truncation fragments and expressing them in cells will help us determine if they affect calcium signaling and/or cell behavior.
- Conducted molecular biology experiments in order to study cell fate determination in the root cells of Arabidopsis
- Studied SCRAMBLED (SCM) receptor protein, its features, and its protein-protein interactions
- Prepared registration files of new medical products by collecting information concerning probable dosage forms, active ingredient, excipients and different procedures for analyzing and titration in different production stages
- Assisted in various stages of medicine preparation including weighing and mixing raw materials, granulating, drying, compressing and packaging final products for solid dosage forms
- Executed biological, chemical, and physical in-process quality control tests for intermediate and final products
- Designed appealing final product packaging for marketing purposes