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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