Laboratory of David Cowburn

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Material Transfer Agreement form to be filed with requests for plasmids etc The lab's research interests focus on the structural biology of protein domains in intracellular signal transduction, including SH2, SH3, kinase, phosphatase, PH domains, and many others and how natural ligands interact with them. Signaling disorders related to these domains lead to many disease states. An additional area of interest is the development of NMR and related methods for structural biology. Projects include segmental labeling, other novel isotopic labeling methods, and detection of protein-protein interaction surfaces and dynamics.
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Cornell Biochemistry, including Tri Institutional Structural Biology Series
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Ferrage F., Cowburn D., Ghose R. Accurate Sampling of High-Frequency Motions in Proteins by Steady-State (15)N-{(1)H} Nuclear Overhauser Effect Measurements in the Presence of Cross-Correlated Relaxation. J Am Chem Soc 2009 May 6; 131 (17):6048-9
Xiong X, Cui P, Hossain S, Xu R, Warner B, Guo X, An X, Debnath A, Cowburn D, Kotula L. (2008) . Allosteric Inhibition of the nonMyristoylated c-Abl Tyrosine Kinase by Phosphopeptides Derived from Abi1/Hssh3bp1. BBA Molecular Cell Research, 1783, 737-47.
Bhattacharya S, Dai Z, Li J, Baxter S, Callaway DJ, Cowburn D, Bu Z. A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. J Biol Chem. 2010 ;285(13):9981-94


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David Cowburn, Ph.D., D.Sc., Professor, Depts of Biochemistry, and of Physiology and Biophysics, Albert Einstein College of Medicine of Yeshiva University, Bronx, NY, 10461, US. T +19089130495 cowburn@cowburnlab.org.