David Fushman
Professor
1121 Biomolecular Sciences Building
(301) 405-3461
Education:
Ph.D., Kazan State University (Physics)
Biography:
David Fushman is a professor of chemistry and biochemistry with an affiliate appointment in the University of Maryland Institute for Advanced Computer Studies.
His research explores the structure, dynamics, stability and function of biological macromolecules, with a focus on intracellular signaling and ubiquitin-mediated pathways. Fushman develops and applies advanced theoretical and experimental methods to understand multidomain proteins and their roles in protein stability and function.
Publications
2012
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
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
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.
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.
2009
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.
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.
2008
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
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.
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.
2006
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
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.
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.
2004
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.
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.
2002
2002. Structural Properties of Polyubiquitin Chains in Solution. Journal of Molecular Biology. 324(4):637-647.
2001
2001. Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308(5):1045-1062.
1999
1999. Solution Structure of the Proapoptotic Molecule BID: A Structural Basis for Apoptotic Agonists and Antagonists. Cell. 96(5):625-634.
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.
1998
1998. Solution structure and dynamics of the bioactive retroviral M domain from rous sarcoma virus. Journal of Molecular Biology. 279(4):921-928.
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.
1997
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
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.