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Zhefeng Guo, Ph.D. - Publications

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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30 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Jang C, Portugal Barron D, Duo L, Ma C, Seabaugh H, Guo Z. EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet Structure. Acs Chemical Neuroscience. PMID 38109787 DOI: 10.1021/acschemneuro.3c00364  0.357
2023 Zhang A, Portugal Barron D, Chen EW, Guo Z. A protein aggregation platform that distinguishes oligomers from amyloid fibrils. The Analyst. 148: 2283-2294. PMID 37129054 DOI: 10.1039/d3an00487b  0.302
2022 Xiao H, Duo L, Zhen J, Wang H, Guo Z. Static and dynamic disorder in Aβ40 fibrils. Biochemical and Biophysical Research Communications. 610: 107-112. PMID 35461071 DOI: 10.1016/j.bbrc.2022.04.036  0.304
2021 Liu EN, Park G, Nohara J, Guo Z. Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2. Royal Society Open Science. 8: 201747. PMID 33959337 DOI: 10.1098/rsos.201747  0.358
2021 Yoon A, Zhen J, Guo Z. Segmental structural dynamics in Aβ42 globulomers. Biochemical and Biophysical Research Communications. 545: 119-124. PMID 33548624 DOI: 10.1016/j.bbrc.2021.01.081  0.361
2020 Wang H, Duo L, Hsu F, Xue C, Lee YK, Guo Z. 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. PMID 32235842 DOI: 10.1038/S41598-020-62181-X  0.392
2020 Wang J, Park G, Lee YK, Nguyen M, San Fung T, Lin TY, Hsu F, Guo Z. Spin Label Scanning Reveals Likely Locations of β-Strands in the Amyloid Fibrils of the Ure2 Prion Domain. Acs Omega. 5: 5984-5993. PMID 32226879 DOI: 10.1021/acsomega.9b04358  0.316
2019 Xue C, Tran J, Wang H, Park G, Hsu F, Guo Z. Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism. Royal Society Open Science. 6: 190179. PMID 31417723 DOI: 10.1098/Rsos.190179  0.34
2018 Wang H, Lee YK, Xue C, Guo Z. Site-specific structural order in Alzheimer's Aβ42 fibrils. Royal Society Open Science. 5: 180166. PMID 30109072 DOI: 10.1098/Rsos.180166  0.459
2018 Hsu F, Park G, Guo Z. Key Residues for the Formation of Aβ42 Amyloid Fibrils. Acs Omega. 3: 8401-8407. PMID 30087945 DOI: 10.1021/acsomega.8b00887  0.311
2017 Xue C, Lee YK, Tran J, Chang D, Guo Z. A mix-and-click method to measure amyloid-β concentration with sub-micromolar sensitivity. Royal Society Open Science. 4: 170325. PMID 28878984 DOI: 10.1098/Rsos.170325  0.348
2017 Xue C, Lin TY, Chang D, Guo Z. Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation. Royal Society Open Science. 4: 160696. PMID 28280572 DOI: 10.1098/Rsos.160696  0.34
2016 Tran J, Chang D, Hsu F, Wang H, Guo Z. Cross-seeding between Aβ40 and Aβ42 in Alzheimer's disease. Febs Letters. PMID 27981583 DOI: 10.1002/1873-3468.12526  0.316
2016 Gu L, Tran J, Jiang L, Guo Z. A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling. Journal of Structural Biology. PMID 26827680 DOI: 10.1016/J.Jsb.2016.01.013  0.357
2015 Guo ZN, Xu L, Hu Q, Matei N, Yang P, Tong LS, He Y, Guo Z, Tang J, Yang Y, Zhang JH. Hyperbaric Oxygen Preconditioning Attenuates Hemorrhagic Transformation Through Reactive Oxygen Species/Thioredoxin-Interacting Protein/Nod-Like Receptor Protein 3 Pathway in Hyperglycemic Middle Cerebral Artery Occlusion Rats. Critical Care Medicine. PMID 26646457 DOI: 10.1097/CCM.0000000000001468  0.336
2014 Gu L, Liu C, Stroud JC, Ngo S, Jiang L, Guo Z. Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers. The Journal of Biological Chemistry. 289: 27300-13. PMID 25118290 DOI: 10.1074/Jbc.M114.569004  0.391
2013 Gu L, Liu C, Guo Z. Structural insights into Aβ42 oligomers using site-directed spin labeling. The Journal of Biological Chemistry. 288: 18673-83. PMID 23687299 DOI: 10.1074/Jbc.M113.457739  0.435
2013 Gu L, Guo Z. Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils. Journal of Neurochemistry. 126: 305-11. PMID 23406382 DOI: 10.1111/Jnc.12202  0.327
2012 Ngo S, Chiang V, Ho E, Le L, Guo Z. Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study. Plos One. 7: e47248. PMID 23077577 DOI: 10.1371/Journal.Pone.0047248  0.404
2012 Ngo S, Chiang V, Guo Z. 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. 180: 374-81. PMID 22967940 DOI: 10.1016/J.Jsb.2012.08.008  0.444
2012 Agopian A, Guo Z. Structural origin of polymorphism of Alzheimer's amyloid β-fibrils. The Biochemical Journal. 447: 43-50. PMID 22823461 DOI: 10.1042/Bj20120034  0.437
2012 Gu L, Ngo S, Guo Z. Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments. The Journal of Biological Chemistry. 287: 9081-9. PMID 22277652 DOI: 10.1074/Jbc.M111.292086  0.396
2011 Ngo S, Guo Z. Key residues for the oligomerization of Aβ42 protein in Alzheimer's disease. Biochemical and Biophysical Research Communications. 414: 512-6. PMID 21986527 DOI: 10.1016/J.Bbrc.2011.09.097  0.443
2011 Ngo S, Gu L, Guo Z. Hierarchical organization in the amyloid core of yeast prion protein Ure2. The Journal of Biological Chemistry. 286: 29691-9. PMID 21730048 DOI: 10.1074/Jbc.M111.269092  0.435
2009 López CJ, Fleissner MR, Guo Z, Kusnetzow AK, Hubbell WL. Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Science : a Publication of the Protein Society. 18: 1637-52. PMID 19585559 DOI: 10.1002/Pro.180  0.585
2008 Guo Z, Eisenberg D. The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold. Protein Science : a Publication of the Protein Society. 17: 1617-23. PMID 18552127 DOI: 10.1110/Ps.036368.108  0.39
2008 Guo Z, Cascio D, Hideg K, Hubbell WL. Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 lysozyme. Protein Science : a Publication of the Protein Society. 17: 228-39. PMID 18096642 DOI: 10.1110/Ps.073174008  0.584
2007 Guo Z, Cascio D, Hideg K, Kálái T, Hubbell WL. Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme. Protein Science : a Publication of the Protein Society. 16: 1069-86. PMID 17473014 DOI: 10.1110/Ps.062739107  0.565
2007 Guo Z, Eisenberg D. The mechanism of the amyloidogenic conversion of T7 endonuclease I. The Journal of Biological Chemistry. 282: 14968-74. PMID 17360710 DOI: 10.1074/Jbc.M609514200  0.325
2006 Guo Z, Eisenberg D. Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proceedings of the National Academy of Sciences of the United States of America. 103: 8042-7. PMID 16698921 DOI: 10.1073/Pnas.0602607103  0.34
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