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.
2012. Rpn1 and Rpn2 coordinate ubiquitin processing factors at the proteasome. Journal of Biological ChemistryJ. Biol. Chem..
2012. Determining Protein Dynamics from 15N Relaxation Data by Using DYNAMICS. Protein NMR Techniques. 831:485-511.
2012. Structural and biochemical studies of the open state of Lys48-linked diubiquitin. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.
2011. A Hierarchical Algorithm for Fast Debye Summation with Applications to Small Angle Scattering. Technical Reports from UMIACS.
2011. Structure and recognition of polyubiquitin chains of different lengths and linkage. F1000 Biology ReportsF1000 Biol Rep. 3
2011. Fast approximations of the rotational diffusion tensor and their application to structural assembly of molecular complexes. Proteins: Structure, Function, and Bioinformatics. 79(7):2268-2281.
2010. Structural Assembly of Molecular Complexes Based on Residual Dipolar Couplings. J. Am. Chem. Soc.. 132(26):8961-8972.
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.
2010. Reversible Post-Translational Carboxylation Modulates the Enzymatic Activity of N-Acetyl-l-ornithine Transcarbamylase. Biochemistry. 49(32):6887-6895.
2010. Exploring the Linkage Dependence of Polyubiquitin Conformations Using Molecular Modeling. Journal of Molecular Biology. 395(4):803-814.
2009. Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13. Molecular Cell. 35(3):280-290.
2009. Improvement and analysis of computational methods for prediction of residual dipolar couplings. Journal of Magnetic Resonance. 201(1):25-33.
2009. Together, Rpn10 and Dsk2 Can Serve as a Polyubiquitin Chain-Length Sensor. Molecular Cell. 36(6):1018-1033.
2009. Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains. Nature Structural & Molecular Biology. 16(8):883-889.
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.
2008. Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins. Journal of Molecular Biology. 375(4):979-996.
2008. Affinity Makes the Difference: Nonselective Interaction of the UBA Domain of Ubiquilin-1 with Monomeric Ubiquitin and Polyubiquitin Chains. Journal of Molecular Biology. 377(1):162-180.
2007. Mapping the Interactions between Lys48 and Lys63-Linked Di-ubiquitins and a Ubiquitin-Interacting Motif of S5a. Journal of Molecular Biology. 368(3):753-766.
2007. Crystal Structure and Solution NMR Studies of Lys48-linked Tetraubiquitin at Neutral pH. Journal of Molecular Biology. 367(1):204-211.
2007. Effects of cyclization on conformational dynamics and binding properties of Lys48-linked di-ubiquitin. Protein Science. 16(3):369-378.
2007. Structural Biology: Analysis of 'downhill' protein folding; Analysis of protein-folding cooperativity (Reply). Nature. 445(7129):E17-E18-E17-E18.
2006. Interdomain mobility in di-ubiquitin revealed by NMR. Proteins: Structure, Function, and Bioinformatics. 63(4):787-796.
2006. An Efficient Computational Method for Predicting Rotational Diffusion Tensors of Globular Proteins Using an Ellipsoid Representation. Journal of the American Chemical Society. 128(48):15432-15444.
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.
2005. Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nature Structural & Molecular Biology. 12(8):708-714.
2005. Structural Determinants for Selective Recognition of a Lys48-Linked Polyubiquitin Chain by a UBA Domain. Molecular Cell. 18(6):687-698.
2004. Polyubiquitin chains: polymeric protein signals. Current Opinion in Chemical Biology. 8(6):610-616.
2004. Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain. Science. 306(5693):117-120.
2004. Characterization of the Overall Rotational Diffusion of a Protein From 15N Relaxation Measurements and Hydrodynamic Calculations. Protein NMR Techniques. 278:139-159.
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.
2002. Structural Properties of Polyubiquitin Chains in Solution. Journal of Molecular Biology. 324(4):637-647.
2001. Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308(5):1045-1062.
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.
1999. A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Molecular and Cellular Biochemistry. 192(1):109-121.
1999. Solution Structure of the Proapoptotic Molecule BID: A Structural Basis for Apoptotic Agonists and Antagonists. Cell. 96(5):625-634.
1998. The Solution Structure and Dynamics of the Pleckstrin Homology Domain of G Protein-coupled Receptor Kinase 2 (β-Adrenergic Receptor Kinase 1) A BINDING PARTNER OF Gβγ SUBUNITS. Journal of Biological ChemistryJ. Biol. Chem.. 273(5):2835-2843.
1998. Solution structure and dynamics of the bioactive retroviral M domain from rous sarcoma virus. Journal of Molecular Biology. 279(4):921-928.
1997. The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration. Journal of Molecular Biology. 266(1):173-194.
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.