Author

F. M. Marassi

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

Y. Yao· 3 shared A. A. Bobkov· 2 shared J. E. Kent· 2 shared W. Im· 2 shared A. E. Aleshin· 1 shared A. Iftikar· 1 shared B. E. Ackerman· 1 shared C. Dong· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

Y. Yao

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Author profile →

4 papers

Recent·Most cited

Dynamic nuclear polarization illuminates key protein-lipid interactions in the native bacterial cell envelope

J. E. Kent, B. E. Ackerman, G. T. Debelouchina, F. M. Marassi

This study uses dynamic nuclear polarization to enhance NMR spectroscopy and reveals key protein-lipid interactions in the bacterial cell envelope of Yersinia pestis.

bioRxiv · May 18, 2023Biochemistry

Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids

A. E. Aleshin, Y. Yao, A. Iftikar, A. A. Bobkov, J. Yu, G. Cadwell, M. Klein, C. Dong, L. A. Bankston, R. C. Liddington, W. Im, G. Powis, F. M. Marassi

This study determines the atomic structure of PLEKHA7's PH domain and reveals its multivalent interaction mechanism with membrane-bound PIPs, providing insights for inhibitor design.

bioRxiv · Nov 25, 2020Biochemistry

Correlating the structure and activity of Y. pestis Ail in a bacterial cell envelope

J. E. Kent, L. M. Fujimoto, K. Shn, C. Singh, Y. Yao, S. Park, S. J. Opella, G. V. Plano, F. M. Marassi

This study uses an E. coli model system to investigate the structure and function of Y. pestis Ail in a bacterial cell envelope, revealing its role in virulence and interactions with human serum components.

bioRxiv · Sep 23, 2020Biochemistry

Conformational states of the cytoprotective protein Bcl-xL

P. Ryzhov, Y. Tian, Y. Yao, A. A. Bobkov, W. Im, F. M. Marassi

This study investigates the conformational states of full-length Bcl-xL in soluble and membrane-anchored forms using NMR, MD simulations, and ITC to understand its structure and ligand binding.

bioRxiv · Mar 25, 2020Biophysics