Francesca Marassi, Ph.D.
Francesca Marassi's Research Focus
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 Sanford Burnham Prebys as Assistant Professor. She is currently Professor and Department Chair, Department of Biophysics at Medical College of Wisconsin.
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 (Reading) 2015 Nov ;161(11):2174-2183
Calcium-induced environmental adaptability of the blood protein vitronectin.
Tian Y, Shin K, Aleshin AE, Im W, Marassi FM
Biophys J 2022 Oct 18 ;121(20):3896-3906
A periplasmic cinched protein is required for siderophore secretion and virulence of Mycobacterium tuberculosis.
Zhang L, Kent JE, Whitaker M, Young DC, Herrmann D, Aleshin AE, Ko YH, Cingolani G, Saad JS, Moody DB, Marassi FM, Ehrt S, Niederweis M
Nat Commun 2022 Apr 26 ;13(1):2255
Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids.
Aleshin AE, Yao Y, Iftikhar A, Bobkov AA, Yu J, Cadwell G, Klein MG, Dong C, Bankston LA, Liddington RC, Im W, Powis G, Marassi FM
Structure 2021 Sep 2 ;29(9):1029-1039.e3
Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope.
Kent JE, Fujimoto LM, Shin K, Singh C, Yao Y, Park SH, Opella SJ, Plano GV, Marassi FM
Biophys J 2021 Feb 2 ;120(3):453-462
Conformational States of the Cytoprotective Protein Bcl-xL.
Ryzhov P, Tian Y, Yao Y, Bobkov AA, Im W, Marassi FM
Biophys J 2020 Oct 6 ;119(7):1324-1334
Calcium and hydroxyapatite binding site of human vitronectin provides insights to abnormal deposit formation.
Shin K, Kent JE, Singh C, Fujimoto LM, Yu J, Tian Y, Im W, Marassi FM
Proc Natl Acad Sci U S A 2020 Aug 4 ;117(31):18504-18510