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|Associate Professor, Neurology|
|Member, Biochemistry, Biophysics & Structural Biology GPB Home Area, Brain Research Institute, Neuroscience GPB Home Area|
Zhefeng Guo is a structural biologist and biochemist who joined the UCLA School of Medicine faculty in 2008. Dr. Guo earned his B.S. in Microbiology (1995) at Shandong University and M.S. in Biochemistry (1998) at Peking University in China. Then Dr. Guo came to the United States for graduate studies and received his Ph.D. in Biochemistry (2003) at UCLA, where he was focused on developing electron paramagnetic resonance (EPR) methods to study protein structure, dynamics, and folding in Wayne Hubbell's laboratory. In 2004, Dr. Guo joined David Eisenberg's research group for postdoc training, working on the structural characterization of amyloid fibrils using the approaches of protein engineering and X-ray crystallography. His laboratory is currently investigating the structure and fibrillization mechanism of amyloid fibrils related to a wide range of human disorders such as Alzheimer's, Parkinson's and prion diseases, with the goal of developing molecular diagnostics and therapeutics for amyloid diseases
Gu Lei, Tran Joyce, Jiang Lin, Guo Zhefeng A new structural model of Alzheimer's AÎ²42 fibrils based on electron paramagnetic resonance data and Rosetta modeling. Journal of structural biology. 2016; 194(1): 61-7.
Gu Lei, Liu Cong, Stroud James C, Ngo Sam, Jiang Lin & Guo Zhefeng Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers. Journal of Biological Chemistry. 2014; 10.1074/jbc.M114.569004.
Gu, Lei; Liu, Cong & Guo, Zhefeng Structural insights into Aβ42 oligomers using site-directed spin labeling. Journal of Biological Chemistry. 2013; 288: 18673-18683. Selected as JBC "Paper of the Week".
Gu, Lei & Guo, Zhefeng Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils. Journal of Neurochemistry. 2013; 126: 305-311.
Agopian, Audrey & Guo, Zhefeng Structural origin of polymorphism of Alzheimer's amyloid β-fibrils. Biochemical Journal. 2012; 447: 43-50.
Ngo, Sam; Chiang, Vicky & Guo, Zhefeng Quantitative analysis of spin exchange interactions to identify β strand and turn regions in Ure2 prion domain fibrils with site-directed spin labeling. Journal of Structural Biology. 2012; 180: 374-381.
Ngo, Sam; Chiang, Vicky; Ho, Elaine; Le, Linh & Guo, Zhefeng Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study. PLoS ONE 2012; 7: e47248.
Gu, Lei; Ngo, Sam & Guo, Zhefeng Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments. Journal of Biological Chemistry. 2012; 287: 9081-9.
Ngo, Sam & Guo, Zhefeng Key residues for the oligomerization of Aβ42 protein in Alzheimer's disease. Biochemical and Biophysical Research Communications. 2011; 414: 512-6.
Ngo, Sam; Gu, Lei & Guo, Zhefeng Hierarchical organization in the amyloid core of yeast prion protein Ure2. Journal of Biological Chemistry. 2011; 286: 29691-29699.
Lopez, Carlos J; Fleissner, Mark R; Guo, Zhefeng; Kusnetzow, Ana K & Hubbell, Wayne L Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Science. 2009; 18: 1637-52.
Guo, Zhefeng; Cascio, Dulio; Hideg, Kalman & Hubbell, Wayne L. Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme. Protein Science. 2008; 17: 228-239.
Guo, Zhefeng & Eisenberg, David The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold. Protein Science. 2008; 17: 1617-1623.
Guo, Zhefeng & Eisenberg, David The mechanism of the amyloidogenic conversion of T7 endonuclease I. Journal of Biological Chemistry. 2007; 282: 14968-74.
Guo, Zhefeng; Cascio, Dulio; Hideg, Kalman; Kalai, Tamas & Hubbell, Wayne L. Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme. Protein Science. 2007; 16: 1069-1086.
Guo, Zhefeng & Eisenberg, David Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proceedings of the National Academy of Sciences of USA. 2006; 103: 8042-7.