Matthew Witkin, Md Email & Phone Number

Miami, Florida, United States

Cleveland, Oh

New York, Ny

New York, Ny

In the Armstrong lab, we are exploring how epigenetics impacts the progression of leukemia. At the beginning of my time in the lab, I was responsible for processing and banking human blood samples for a clinical trial for a drug designed to inhibit the DOT1L methyltransferase in patients with MLL. I also worked on an in vivo experiment testing the effects of inhibiting HDACs which helped lead to a publication "Selective Inhibition of HDAC1 and HDAC2 as a Potential Therapeutic Option for B-ALL." Currently, I am working on optimizing a Hi-C technique which will allow us to gain a greater understanding of the conformation of chromatin within our cells. We are also thinking about ways in which we can utilize chromatin readers to improve laboratory methods.***Scott has now moved to Dana Farber, and I am continuing my work in Ross Levine's lab.

Atlanta, Ga

In the McCarty, we studied the mechanisms of cystic fibrosis. Although this is mainly an electrophysical lab, I helped with an in vivo experiement which involved bone marrow transplants in mice. We used a pHrodo assay to determine whether or not bone transplants would help macrophages perform better in CF mice receiving WT bone marrow.

Bronx, Ny

For this Summer Undergraduate Research Program I worked with Mary Short in Dr. E. Richard Stanley's laboratory in the Department of Developmental and Molecular Biology at the Albert Einstein College of Medicine. My project utilized a yeast two/three hybrid system in order to identify what proteins interact with an actin bundling protein called Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2) otherwise known as Macrophage Actin-Associated Tyrosine Phosphorylated Protein (MAYP). We also attempted to map the binding site with these interactions by using different deletion mutants. Additionally, we tried to identify which tyrosine residues were essential for the regulation of PSTPIP2 binding by mutating these residues to phenylalanine residues. Overall, we managed to identify about 20 proteins that appear to interact with PSTPIP2. Most proteins seem to bind closer to its carboxy terminal end and tyrosine phosphorylation appears to play a negative regulatory role.

Philadelphia, Pa

Worked in Dr. Wilson's Gene Therapy Program lab for the summer on a project that utilized mutagenesis to attempt to determine the location of the sialic acid linkage binding site on AAV6.

Doctor Of Medicine - Md

Bachelor Of Science (Bs), Biology & Economics

Biology