Francesca Marassi, Ph.D.

Francesca Marassi headshot

Francesca Marassi, Ph.D.


Fax: (858) 646-3197

Research Assistant Professor(s)

Francesca Marassi's Research Focus

Cancer, Infectious Diseases, Atherosclerosis, Computational Biology, Biochemistry, Structural Biology
Bcl-2 Family, Apoptosis and Cell Death, Biodefense, Host Defense, Host-Pathogen Interactions, Infectious Disease Processes, Ligand-Mediated Protein Conformational Changes, Protein Structure-Function Relationships
Biophysics, Chemistry, Nuclear Magnetic Resonance Spectroscopy (NMR), Phage Display, Protein-Protein Interactions, Protein-Small Molecule Interactions, Solid-State NMR
Computational Modeling

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 percent 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.

Francesca Marassi's Bio

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 SBP as Assistant Professor. She is currently Professor in the NCI-Designated Cancer Center.


CMSN Accessory

Publications

High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes.

Yao Y, Dutta SK, Park SH, Rai R, Fujimoto LM, Bobkov AA, Opella SJ, Marassi FM

J Biomol NMR 2017 Mar ;67(3):179-190

High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.

Tian Y, Schwieters CD, Opella SJ, Marassi FM

J Biomol NMR 2017 Jan ;67(1):35-49

Yersinia pestis uses the Ail outer membrane protein to recruit vitronectin.

Bartra SS, Ding Y, Miya Fujimoto L, Ring JG, Jain V, Ram S, Marassi FM, Plano GV

Microbiology 2015 Nov ;161(11):2174-2183

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Structure of human Vitronectin C-terminal domain and interaction with <i>Yersinia pestis</i> outer membrane protein Ail.

Shin K, Lechtenberg BC, Fujimoto LM, Yao Y, Bartra SS, Plano GV, Marassi FM

Sci Adv 2019 Sep ;5(9):eaax5068

Lipoprotein Particle Formation by Proapoptotic tBid.

Ekanayake V, Nisan D, Ryzhov P, Yao Y, Marassi FM

Biophys J 2018 Aug 7 ;115(3):533-542

Regulation of apoptosis by an intrinsically disordered region of Bcl-xL.

Follis AV, Llambi F, Kalkavan H, Yao Y, Phillips AH, Park CG, Marassi FM, Green DR, Kriwacki RW

Nat Chem Biol 2018 May ;14(5):458-465

Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.

Berkamp S, Park SH, De Angelis AA, Marassi FM, Opella SJ

J Biomol NMR 2017 Nov ;69(3):111-121

Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers.

Dutta SK, Yao Y, Marassi FM

J Phys Chem B 2017 Aug 17 ;121(32):7561-7570

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