View All Publications
Molecular structure and peptidoglycan recognition of Mycobacterium tuberculosis ArfA (Rv0899).
Yao Y, Barghava N, Kim J, Niederweis M, Marassi FM
J Mol Biol. 2012 Feb 17;416(2):208-20
AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.
Tian Y, Schwieters CD, Opella SJ, Marassi FM
J Magn Reson. 2012 Jan;214(1):42-50
Mycobacterium tuberculosis Rv0899 defines a family of membrane proteins widespread in nitrogen-fixing bacteria.
Proteins. 2011 Oct;79(10):2946-55
Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL.
Yao Y, Bobkov AA, Plesniak LA, Marassi FM
Biochemistry. 2009 Sep 15;48(36):8704-11
Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.
Mahalakshmi R, Marassi FM
Biochemistry. 2008 Jun 24;47(25):6531-8
Structural similarity of a membrane protein in micelles and membranes.
Franzin CM, Teriete P, Marassi FM
J Am Chem Soc. 2007 Jul 4;129(26):8078-9
The anti-angiogenic peptide anginex disrupts the cell membrane.
Pilch J, Franzin CM, Knowles LM, Ferrer FJ, Marassi FM, Ruoslahti E
J Mol Biol. 2006 Mar 3;356(4):876-85
Correlation of gene and protein structures in the FXYD family proteins.
Franzin CM, Yu J, Thai K, Choi J, Marassi FM
J Mol Biol. 2005 Dec 9;354(4):743-50
Conformation of membrane-associated proapoptotic tBid.
Gong XM, Choi J, Franzin CM, Zhai D, Reed JC, Marassi FM
J Biol Chem. 2004 Jul 9;279(28):28954-60
Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints.
Marassi FM, Opella SJ
Protein Sci. 2003 Mar;12(3):403-11
Francesca Marassi's Research Focus
Cancer, Heart Disease, Infectious Diseases
Dr. Marassi's research focuses on the structure determination of proteins embedded in cellular membranes. These proteins play important roles in regulating cell life and death, in the transport of nutrients across the cell membranes, and in the transmission of biological signals. Their functions are associated with major human diseases, including cancer, infection, and heart disease. Thus, it is not surprising that membrane proteins are the targets of more than 60% of all drugs on the market today. The three-dimensional structure of a protein is essential for understanding its mechanisms of action, for medicinal chemistry efforts, and for the development of therapies. Dr. Marassi’s primary research tool is NMR spectroscopy, a powerful technique that utilizes strong magnetic fields to extract structural information from biological molecules and characterize their interactions with their cellular partners. The Marassi laboratory uses complementary approaches of solution and solid-state NMR spectroscopy for proteins that are either dissolved in micelle solutions or embedded in lipid bilayers. These methods provide direct information about the three-dimensional structures and orientations of membrane proteins, which are essential for understanding their biological functions.
About Francesca Marassi
Francesca M. Marassi obtained her Ph.D. in Chemistry from the University of Toronto in 1993. Dr. Marassi received her postdoctoral training at the University of Pennsylvania where she held Postdoctoral Fellowships from the Natural Sciences & Engineering Research Council of Canada (1993-1995) and from the Medical Research Council of Canada (1995-1998). In 1998, Dr. Marassi joined the Division of Structural Biology at the Wistar Institute in Philadelphia, as Assistant Professor and, in 1999, she was appointed Wistar Professor of Pharmacology at the University of Pennsylvania. In December 2000, Dr. Marassi joined the Sanford-Burnham Medical Research Institute as Assistant Professor. She is currently Associate Professor in the Apoptosis and Cell Death Research program.