Structure of the chemokine receptor CXCR1 in phospholipid bilayers.
Park SH, Das BB, Casagrande F, Tian Y, Nothnagel HJ, Chu M, Kiefer H, Maier K, De Angelis AA, Marassi FM, Opella SJ
Nature. 2012 Nov 29;491(7426):779-83
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
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Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes.
Cheng X, Jo S, Qi Y, Marassi FM, Im W
Biophys J. 2015 Apr 21;108(8):1954-62
Conformation of BCL-XL upon Membrane Integration.
Yao Y, Fujimoto LM, Hirshman N, Bobkov AA, Antignani A, Youle RJ, Marassi FM
J Mol Biol. 2015 Feb 27;
Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.
Ding Y, Fujimoto LM, Yao Y, Marassi FM
J Biomol NMR. 2015 Apr;61(3-4):275-86
Influence of the lipid membrane environment on structure and activity of the outer membrane protein Ail from Yersinia pestis.
Ding Y, Fujimoto LM, Yao Y, Plano GV, Marassi FM
Biochim Biophys Acta. 2015 Feb;1848(2):712-20
Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints.
Tian Y, Lu GJ, Marassi FM, Opella SJ
J Biomol NMR. 2014 Sep;60(1):67-71
Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines.
Gong XM, Ding Y, Yu J, Yao Y, Marassi FM
Biochim Biophys Acta. 2015 Jan;1848(1 Pt B):299-306
A practical implicit solvent potential for NMR structure calculation.
Tian Y, Schwieters CD, Opella SJ, Marassi FM
J Magn Reson. 2014 Jun;243:54-64
The rheostat in the membrane: BCL-2 family proteins and apoptosis.
Volkmann N, Marassi FM, Newmeyer DD, Hanein D
Cell Death Differ. 2014 Feb;21(2):206-15
Membrane protein structure determination in membrana.
Ding Y, Yao Y, Marassi FM
Acc Chem Res. 2013 Sep 17;46(9):2182-90
Membrane protein structure determination: back to the membrane.
Yao Y, Ding Y, Tian Y, Opella SJ, Marassi FM
Methods Mol Biol. 2013;1063:145-58
Francesca Marassi's Research Focus
Cancer, Infectious Diseases, Computational Biology
Dr. Marassi's research focuses on understanding the structures and functions of proteins embedded in cellular membranes. Membrane proteins mediate all interactions of a cell or organism with the outside world and, as such, are responsible for the basic human experiences (taste, smell, touch, sight, thought, etc.) that constitute life. They are encoded by at least 30% of all genes and perform essential biological functions that include cellular transport, signaling, and programmed cell death. Dysfunctions of human membrane proteins are linked with devastating diseases and the membrane proteins encoded by viruses and bacteria play major roles in infection, virulence, and antibiotic resistance. It is, therefore, not surprising that membrane proteins are the principal targets of most drugs on the market today and that understanding their biological functions is a major goal of biomedical research.
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. Her laboratory uses complementary approaches of solution NMR and solid-state NMR for proteins that are embedded in lipid bilayers to obtain direct information about three-dimensional structure and membrane orientation.
About Francesca Marassi
Dr. Marassi earned her Ph.D. in Chemistry from the University of Toronto in 1993. She received postdoctoral training at the University of Pennsylvania, where she held fellowships from the Natural Sciences and 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 Professor in the NCI-Designated Cancer Center.