Tobias S. Ulmer
Dept. of Biochemistry & Molecular Biology
Zilkha Neurogenetic Institute
Keck School of Medicine
- Signal Transduction
- Aging and Associated Diseases
- Membrane Proteins
- Structural Biology
Research OverviewMy research program centers on elucidating the molecular mechanism underlying physiological function and pathological dysfunction, respectively, of biological processes at atomic resolution. Specifically, the three-dimensional structure of proteins, their dynamics as well as protein-protein and protein-lipid interactions are determined. As a principal research tool, high-resolution, multidimensional solution-state nuclear magnetic resonance (NMR) spectroscopy is employed. My overarching interest is devoted to the structural biology of proteins that are either membrane embedded or membrane surface-bound.
Specifically, my laboratory focuses on understanding
(1) the structural basis of transmembrane signaling in cell surface receptors,
(2) the mechanism of misfolding of the protein alpha-synuclein, underlying the pathogenesis of Parkinson's disease, and
(3) proteins involved in disulfide bond catalysis in the Chlamydia family of human pathogens.
Rao JN, Jao CC, Hedge BG, Langen R, and Ulmer TS
A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins.
J Am Chem Soc, 132, 8657-8668, 2010
Suk JE, Lokappa SB, and Ulmer TS
The clustering and spatial arrangement of b-sheet sequence, but not order, govern a-synuclein fibrillogenesis.
Biochemistry, 49, 1533-1540, 2010
Rao JN, Kim YE, Park LS, and Ulmer TS
Effect of pseudorepeat rearrangement on a-synuclein misfolding, vesicle binding, and micelle binding.
J Mol Biol, 390, 516-529, 2009
Lau TL, Kim C, Ginsberg MH, and Ulmer TS
The structure of the integrin aIIbb3 transmembrane complex explains integrin transmembrane signalling.
EMBO J, 28, 1351-1361, 2009
Lau TL, Dua V, and Ulmer TS
Structure of the integrin aIIb transmembrane segment.
J Biol Chem, 283, 16162-16168, 2008
Rao JN, Dua V, and Ulmer TS
Characterization of a-synuclein interactions with selected aggregation-inhibiting small molecules.
Biochemistry, 47, 4651-4647, 2008
Lau TL, Partridge AW, Ginsberg MH, and Ulmer TS
Structure of the integrin b3 transmembrane segment in phospholipid bicelles and detergent micelles.
Biochemistry, 47, 4008-4016, 2008
Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, and Ulmer TS
Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase.
J Biol Chem, 283, 824-832, 2008