Zhefeng Guo, Ph.D.

Affiliations: 
2003 University of California, Los Angeles, Los Angeles, CA 
Area:
proteins involved in visual signal transduction (rhodopsin, the G-protein transducin and arrestin) and soluble ligand-binding proteins
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"Zhefeng Guo"
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SNBCP

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Wayne Lester Hubbell grad student 2003 UCLA
 (Correlation of spin label side-chain dynamics with protein structure: Studies of T4 lysozyme with site-directed mutagenesis and x-ray crystallography.)
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Publications

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Jang C, Portugal Barron D, Duo L, et al. (2023) EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet Structure. Acs Chemical Neuroscience
Zhang A, Portugal Barron D, Chen EW, et al. (2023) A protein aggregation platform that distinguishes oligomers from amyloid fibrils. The Analyst. 148: 2283-2294
Xiao H, Duo L, Zhen J, et al. (2022) Static and dynamic disorder in Aβ40 fibrils. Biochemical and Biophysical Research Communications. 610: 107-112
Liu EN, Park G, Nohara J, et al. (2021) Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2. Royal Society Open Science. 8: 201747
Yoon A, Zhen J, Guo Z. (2021) Segmental structural dynamics in Aβ42 globulomers. Biochemical and Biophysical Research Communications. 545: 119-124
Wang H, Duo L, Hsu F, et al. (2020) Polymorphic Aβ42 fibrils adopt similar secondary structure but differ in cross-strand side chain stacking interactions within the same β-sheet. Scientific Reports. 10: 5720
Wang J, Park G, Lee YK, et al. (2020) Spin Label Scanning Reveals Likely Locations of β-Strands in the Amyloid Fibrils of the Ure2 Prion Domain. Acs Omega. 5: 5984-5993
Xue C, Tran J, Wang H, et al. (2019) Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism. Royal Society Open Science. 6: 190179
Wang H, Lee YK, Xue C, et al. (2018) Site-specific structural order in Alzheimer's Aβ42 fibrils. Royal Society Open Science. 5: 180166
Hsu F, Park G, Guo Z. (2018) Key Residues for the Formation of Aβ42 Amyloid Fibrils. Acs Omega. 3: 8401-8407
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