Publications

Xue, C, Lin, TY, Chang, D, and Guo, Z. Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation. R. Soc. Open Sci., 4: 160696. doi:10.1098/rsos.160696. (2017)

Tran, J, Chang, D, Hsu, F, Wang, H, and Guo, Z. Cross-seeding between Aβ40 and Aβ42 in Alzheimer’s disease. FEBS Lett., doi:10.1002/1873-3468.12526. Pubmed PMID:27981583 (2016)

Gu, L, Tran, J, Jiang, L, and Guo, Z. A new structural model of Alzheimer’s Aβ42 fibrils based on electron paramagnetic resonance data and rosetta modeling. J. Struct. Biol., 194:61-7. doi:10.1016/j.jsb.2016.01.013. PubMed PMID:26827680 PubMed Central PMC4764428 [Available on 2017-04-01] (2016).

Gu, L, Liu, C, Stroud, JC, Ngo, S, Jiang, L, Guo, Z. Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers. J. Biol. Chem. 289.:27300-13. doi: 10.1074/jbc.M114.569004. PubMed PMID:25118290 PubMed Central PMC4175361 (2014).

Gu, L, Liu, C, Guo, Z. Structural insights into Aβ42 oligomers using site-directed spin labeling. J. Biol. Chem. 288.:18673-83. doi: 10.1074/jbc.M113.457739. PubMed PMID:23687299 PubMed Central PMC3696641 (2013).

Gu, L, Guo, Z. Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils. J. Neurochem. 126.:305-11. doi: 10.1111/jnc.12202. PubMed PMID:23406382 PubMed Central PMC3716832 (2013).

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. Epub 2012/10/16. doi: 10.1371/journal.pone.0047248. PubMed PMID:23077577 PubMed Central PMC3473064 (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. J. Struct. Biol. 180.:374-81. doi: 10.1016/j.jsb.2012.08.008. PubMed PMID:22967940 (2012).

Agopian, A, Guo, Z. Structural origin of polymorphism of Alzheimer's amyloid β-fibrils. Biochem. J. 447.:43-50. doi: 10.1042/BJ20120034. PubMed PMID:22823461 (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. J. Biol. Chem. 287.:9081-9. doi: 10.1074/jbc.M111.292086. PubMed PMID:22277652 PubMed Central PMC3308762 (2012).

Ngo, S, Guo, Z. Key residues for the oligomerization of Aβ42 protein in Alzheimer's disease. Biochem. Biophys. Res. Commun. 414.:512-6. doi: 10.1016/j.bbrc.2011.09.097. PubMed PMID:21986527 (2011).

Ngo, S, Gu, L, Guo, Z. Hierarchical organization in the amyloid core of yeast prion protein Ure2. J. Biol. Chem. 286.:29691-9. doi: 10.1074/jbc.M111.269092. PubMed PMID:21730048 PubMed Central PMC3191010 (2011).

López, CJ, Fleissner, MR, Guo, Z, Kusnetzow, AK, Hubbell, WL. Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Sci. 18.:1637-52. doi: 10.1002/pro.180. PubMed PMID:19585559 PubMed Central PMC2776952 (2009).

Guo, Z, Eisenberg, D. The structure of a fibril-forming sequence, NNQQNY, in the context of a globular fold. Protein Sci. 17.:1617-23. doi: 10.1110/ps.036368.108. PubMed PMID:18552127 PubMed Central PMC2525518 (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 Sci. 17.:228-39. doi: 10.1110/ps.073174008. PubMed PMID:18096642 PubMed Central PMC2222722 (2008).

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 Sci. 16.:1069-86. doi: 10.1110/ps.062739107. PubMed PMID:17473014 PubMed Central PMC2206656 (2007).

Guo, Z, Eisenberg, D. The mechanism of the amyloidogenic conversion of T7 endonuclease I. J. Biol. Chem. 282.:14968-74. doi: 10.1074/jbc.M609514200. PubMed PMID:17360710 (2007).

Guo, Z, Eisenberg, D. Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proc. Natl. Acad. Sci. U.S.A. 103.:8042-7. doi: 10.1073/pnas.0602607103. PubMed PMID:16698921 PubMed Central PMC1472426 (2006).

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