University of Pittsburgh

Jamie Moroco, PhD

Postdoctoral Associate





	
	


			

		Dr. Jamie Moroco	
		

		

	
Contact

    	
		
	
	
	    

    
    
   
    
   
    
        
    
   
   
   
   
   
   
    
    
	
	
	
		
		
	



	
Education
	
	

	
PhD in Molecular Pharmacology, University of Pittsburgh, School of Medicine, 2013
BS in Biological Sciences, Carnegie Mellon University, 2007
        

              
   
  
 
 


  
 
 
 
 
 
 
 
 	
Mentor
	
	

	
Thomas Smithgall, PhD
        

                
        
        
        
        	
Dissertation
	
	

	DIVERSITY IN SRC-FAMILY KINASE ACTIVATION MECHANISMS: IMPLICATIONS FOR SELECTIVE INHIBITOR DISCOVERY	
	


        
        
        
        
 
 
   
   
















        













	
Areas of Interest
	
	

	I am interested in the structural dynamics of the Src family kinases and how a better understanding of their mechanisms of activation can lead to more effective and targeted therapies for HIV and cancer.	
	






	
Why I Chose Pitt
	
	

	
I like the interdisciplinary and collaborative nature of the
university, the diverse research interests of the faculty, and the
translational aspect of the research from bench to bedside at the UPMC
hospitals. And because I love
Pittsburgh!
Following her graduation, Dr. Moroco accepted a position as a Postdoctoral Research Associate in the lab of Dr. John Engen at Northeastern University.
Abstracts
Moroco
JA, Alvarado JJ, Yeh JI, and Smithgall TE. "Diversity in
the Control of individual Src-family kinases by their SH3 domains." April 9-13,
2011. Experimental Biology, Washington, DC. 
	
	




	
Publications
	
	

	
Lee, J; Su, E. W; Zhu, C; Hainline, S; Phuah, J; Moroco, J. A; Smithgall, T. E; Kuchroo, V. K; and Kane, L. P. (2011) Phosphotyrosine-dependent coupling of Tim-3 to TCR signaling pathways. Mol. Cell. Biol. 31: 3963-3974. |  View Abstract
Alvarado J. J; Betts L; Moroco J. A; Smithgall T. E; and Yeh, J. I. (2010) Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory region supports an SH3-dominant activation mechanism. J. Biol. Chem. 285: 35455-35461. |  View Abstract