David Fushman

1121 Biomolecular Sciences Building
(301) 405-3461
Ph.D., Kazan State University (Physics)

David Fushman is a professor in the Department of Chemistry and Biochemistry with a joint appointment in the Center for Biomolecular Structure and Organization.

His primary scientific interest is in understanding the relationship between structure, dynamics, and function in complex molecular systems, like biological macromolecules.

Fushman has written more than 90 research publications in journals and book chapters, primarily on experimental and computational approaches and models and their application to determine the 3-D structure and dynamics of proteins and protein-protein complexes at atomic-level resolution.

He has served as the program co-chairman for the 10th Chianti Workshop on Magnetic Resonance in 2003 (Italy) and the 12th Chianti/INSTRUCT Workshop on BioNMR in 2012 (Italy), and as a co-organizer of the joint NIH and University of Maryland international practical training course “Structure Determination of Biological Macromolecules by Solution NMR“ in 2008. He was awarded the Alexander von Humboldt Fellowship from 1992 to 1993 and Lady Davis Fellowship from 2008 to 2009.

Fushman was a visiting professor at the University of Florence in 2002, the Technion – Israel Institute of Technology from 2008 to 2009, and the University of Verona, Italy in 2009. Since 2010, he has continuously been a visiting professor at the Technion – Israel Institute of Technology.

He received his doctorate in theoretical and mathematical physics from Kazan State University (now Kazan Federal University) in 1985. Before joining the University of Maryland in 2000, he worked at Kazan Institute of Biology (then the USSR Academy of Sciences), the Institute for Biophysical Chemistry at the University of Frankfurt, Germany, and Rockefeller University.



Rosenzweig R, Bronner V, Zhang D, Fushman D, Glickman MH.  2012.  Rpn1 and Rpn2 coordinate ubiquitin processing factors at the proteasome. Journal of Biological ChemistryJ. Biol. Chem..

Lai M-Y, Zhang D, LaRonde-LeBlanc N, Fushman D.  2012.  Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.



Caceres A, Shang F, Wawrousek E, Liu Q, Avidan O, Cvekl A, Yang Y, Haririnia A, Storaska A, Fushman D et al..  2010.  Perturbing the Ubiquitin Pathway Reveals How Mitosis Is Hijacked to Denucleate and Regulate Cell Proliferation and Differentiation In Vivo. PLoS ONEPLoS ONE. 5(10):e13331-e13331.


Zhang D, Chen T, Ziv I, Rosenzweig R, Matiuhin Y, Bronner V, Glickman MH, Fushman D.  2009.  Together, Rpn10 and Dsk2 Can Serve as a Polyubiquitin Chain-Length Sensor. Molecular Cell. 36(6):1018-1033.

Sims JJ, Haririnia A, Dickinson BC, Fushman D, Cohen RE.  2009.  Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains. Nature Structural & Molecular Biology. 16(8):883-889.

Wang T, Yin L, Cooper EM, Lai M-Y, Dickey S, Pickart CM, Fushman D, Wilkinson KD, Cohen RE, Wolberger C.  2009.  Evidence for Bidentate Substrate Binding as the Basis for the K48 Linkage Specificity of Otubain 1. Journal of Molecular Biology. 386(4):1011-1023.

Zhang N, Wang Q, Ehlinger A, Randles L, Lary JW, Kang Y, Haririnia A, Storaska AJ, Cole JL, Fushman D et al..  2009.  Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13. Molecular Cell. 35(3):280-290.


Haririnia A, Verma R, Purohit N, Twarog MZ, Deshaies RJ, Bolon D, Fushman D.  2008.  Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins. Journal of Molecular Biology. 375(4):979-996.


Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C.  2007.  Crystal Structure and Solution NMR Studies of Lys48-linked Tetraubiquitin at Neutral pH. Journal of Molecular Biology. 367(1):204-211.


Ryabov Y, Fushman D.  2006.  Interdomain mobility in di-ubiquitin revealed by NMR. Proteins: Structure, Function, and Bioinformatics. 63(4):787-796.


Varadan R, Assfalg M, Fushman D.  2005.  Using NMR Spectroscopy to Monitor Ubiquitin Chain Conformation and Interactions with Ubiquitin‐Binding Domains. Ubiquitin and Protein Degradation, Part B. Volume 399:177-192.

Raasi S, Varadan R, Fushman D, Pickart CM.  2005.  Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nature Structural & Molecular Biology. 12(8):708-714.


Pickart CM, Fushman D.  2004.  Polyubiquitin chains: polymeric protein signals. Current Opinion in Chemical Biology. 8(6):610-616.

Verma R, Peters NR, D'Onofrio M, Tochtrop GP, Sakamoto KM, Varadan R, Zhang M, Coffino P, Fushman D, Deshaies RJ et al..  2004.  Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain. Science. 306(5693):117-120.

Varadan R, Assfalg M, Haririnia A, Raasi S, Pickart C, Fushman D.  2004.  Solution Conformation of Lys63-linked Di-ubiquitin Chain Provides Clues to Functional Diversity of Polyubiquitin Signaling. Journal of Biological ChemistryJ. Biol. Chem.. 279(8):7055-7063.


Varadan R, Walker O, Pickart C, Fushman D.  2002.  Structural Properties of Polyubiquitin Chains in Solution. Journal of Molecular Biology. 324(4):637-647.


Camarero JA, Fushman D, Sato S, Giriat I, Cowburn D, Raleigh DP, Muir TW.  2001.  Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308(5):1045-1062.


Pfeiffer S, Fushman D, Cowburn D.  1999.  Impact of Cl− and Na+ ions on simulated structure and dynamics of βARK1 PH domain. Proteins: Structure, Function, and Bioinformatics. 35(2):206-217.


McDonnell JM, Fushman D, Cahill SM, Zhou W, Wolven A, Wilson CB, Nelle TD, Resh MD, Wills J, Cowburn D.  1998.  Solution structure and dynamics of the bioactive retroviral M domain from rous sarcoma virus. Journal of Molecular Biology. 279(4):921-928.



Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D.  1996.  Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity. Journal of Molecular Biology. 255(1):14-21.