top of page

37. Extraction of in-cell beta-amyloid fibrillar aggregates for studying molecular-level structural propagations using solid-state NMR spectroscopy (2024) J.M. Kenyaga, W. Qiang. Biochemistry, in press. 

36. Modulation of lipid dynamics in the beta-amyloid aggregates induced membrane fragmentation (2024) W. Qiang, M.K. Kengwerere, J.M. Kenyaga. J. Phys. Chem. B, 128, 23, 5667-5675.

 

35. Neutron spin echo shows pHLIP is capale of retarding membrane thickness fluctuations (2024) H.L. Scott, V. Burns-Casamayor, A.C. Dixson, R.F. Standaert, C.B. Stanley, L. Stingaciu, J.Y. Carrillo, B.G. Sumpter, J. Katsaras, W. Qiang, F.A. Heberle, B. Mertz, R. Ashkar, F.N. Barrera. BBA-Biomembranes, 1866, 7, 184349.

34. Rigidifying of the internal dynamic of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles (2024) L. Vugmeyster, D.F. Au, B. Frazier, W. Qiang, D. Ostrovsky. Phys. Chem. Chem. Phys., 26, 5466-5478.

33. Heterotypic Interactions Between the 40- and 42-Residue Isoforms of Beta-Amyloid Peptides on Lipid Bilayer Surfaces (2023) W. Qiang, M.K. Kengwerere. W. Zhao, F.J. Scotts, X. Wutoh-Hughes, T. Wang, F. Mentink-Vigier. ACS Chem. Neurosci., 14, 23, 4153-4162.

32. Modulation of Aggregation and Structural Polymorphisms of b-Amyloid Fibrils in Cellular Environments by Pyroglutamate-3 Variants Cross-Seeding (2023) L. Cruceta, Y. Sun, J.M. Kenyaga, D. Ostrovsky, A. Rodgers, L. Vugmeyster, L. Yao, W. Qiang. J. Biol. Chem., 299, 10, 105196.

31. In-Cell 31P Solid-State NMR Measurements of the Lipid Dynamics and Influence of Exogenous Beta-Amyloid Peptides on Live Neuroblastoma Neuro-2a Cells. (2023) J. Kenyaga, S.A. Otieno, W. Qiang. Biophys. Chem., 297, 107008.

30. Early Stage b-Amyloid-Membrane Interactions Modulate Lipid Dynamics and Influence Structural Interface and Fibrillation. (2022) J. Kenyaga, Q. Cheng, W. Qiang,
J. Biol. Chem. 298, 10, 102491.

 

29. Roles of Key Residues and Lipid Dynamics Reveal pHLIP-membrane Interactions at Intermediate pH. (2021) S.A. Otieno, W. Qiang. Biophys. J., 120, 1-14.

28. Cross-seeded Fibrillation Induced by Pyroglutamate-3 and Truncated Aβ40 Variants Leads to Aβ40 Structural Polymorphism Modulation and Elevated Toxicity. (2021) Z.W. Hu, L. Cruceta, S. Zhang, Y. Sun, W. Qiang. ACS Chem. Neurosci., 12, 3625-3637.

27. Application of DNP-enhanced solid-state NMR to studies of amyloid-beta peptide interaction with lipid membranes. (2021) T. Deo, Q. Cheng, S. Paul, W. Qiang, A. Potapov. Chem. Phys. Lipid, 236, 105071.

26. Probing amyloid beta interactions with synthetic heparan sulfate oilgosaccharides. (2021) P. Wang, J. Zhao, S. H. Nasr, S.A. Otieno, F. Zhang, W. Qiang, R.J. Linhardt, X. Huang. ACS Chem. Biol., online ahead of print.

25. Time-dependent lipid dynamics, organization and peptide-lipid interaction in phospholipid bilayers with incorporated beta-amyloid oligomers. (2020) W. Qiang, K.E. Doherty, L.M. Klees, Y. Tobin-Miyaji. J. Phys. Chem. Lett., 11, 8329-8336.

24. The N-terminal modified Aβ variants enable modulations to the structures and cytotoxicity levels of wild-type Aβ fibrils through cross-seeding. (2020) Z.W. Hu, D.F. Au, L. Cruceta, L. Vugmeyster, W. Qiang. ACS Chemical Neuroscience, 11(14), 2058-2065.

23. Fibrillization of 40-Residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms. (2020) Q. Cheng, Z.W. Hu, Y. Tobin-Miyaji, A.E. Perkins, T. Deak, W. Qiang. Biomolecules, 10 (6), 881.

22. Amyloid-forming segment induces aggregation of FUS-LC domain from phase separation modulated by site-specific phosphorylation. (2020) X. Ding, F. Sun, J. Chen, L. Chen, Y. Tobin-Miyaji, S. Xue, W. Qiang. S.Z. Luo, J. Mol. Biol. 432 (2), 467-483.

21. Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus. (2019) L Vugmeyster, D.F. Au, D. Ostrovsky, B. Kierl, R. Fu, Z.W. Hu, W. Qiang, Biophys. J. 117(8), 1524-1535.

20. Molecular structure of an N-terminal phosphorylated β-amyloid fibril. (2019) Z.W. Hu, L.Vugmeyster, D.F. Au, D. Ostrovsky, Y. Sun, W. Qiang, PNAS 116 (23), 11253-11258.

19. pH-dependent thermodynamic intermediates of pHLIP membrane insertion determined by solid-state NMR spectroscopy. (2018) S.A. Otieno, S.Z. Hanz, B. Chakravorty, A. Zhang, L.M. Klees, M. An, W. Qiang, PNAS 115(48), 12194-12199.

18. The on-fibrillation-pathway membrane content leakage and off-fibrillation-pathway lipid mixing induced by 40-residue β-amyloid peptides in biologically relevant model liposomes. (2018) Q. Cheng, Z.W. Hu, K.E. Doherty, Y.J. Tobin-Miyaji, W. Qiang, BBA-Biomembranes 1780 (9), 1670-1680.

17. Fabrication and Microscopic and Spectroscopic Characterization of Cytocompatible Self-Assembling Antimicrobial Nanofibers. (2018) D. Xu, W. Chen, Y.J. Tobin-Miyaji, C.R. Sturge, S. Yang, B. Elmore, A. Singh, C. Pybus, D.E. Greenberg, T.J. Sellati, W. Qiang, H. Dong, ACS Infectious Diseases 4 (9), 1327-1335.

16. Model Phospholipid Liposomes to Study the β-Amyloid-Peptide-Induced Membrane Disruption. W. Qiang, K.E. Doherty, In: Nilsson B., Doran T. (eds) Peptide Self-Assembly. (2018) Methods in Molecular Biology, vol 1777. Humana Press, New York, NY

15. Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by 2H NMR Relaxation. (2017) L. Vugmeyster, D. Ostrovsky, G.L. Hoatson, W. Qiang, I.B. Falconer,  J. Phys. Chem. B 121(30), 7267-7275.

14. Solid-state-nmr-structure-based inhibitor design to achieve selective inhibition of the parallel-in-register β-sheet versus antiparallel Iowa mutant β-amyloid fibrils. (2017) Q. Cheng, W. Qiang, J. Phys. Chem. B 121 (22), 5544-5552.

13. Phosphorylation at Ser8 as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) Fibrils. (2017) Z.W. Hu, M.R. Ma, Y.X. Chen, Y.F. Zhao, W. Qiang, Y.M. Li, J. Biol. Chem. 292 (7), 2611-2623.

12. Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes. (2017) W. Qiang, W.M. Yau, J.X. Lu, J. Collinge, R. Tycko. Nature 541 (7636), 217-221.

11. Fast motions of key methyl groups in Amyloid-β fibrils. (2016) L. Vugmeyster, D. Ostrovsky, M.A. Clark, I.B. Falconer, G.L. Hoatson, W. Qiang,  Biophys. J. 111(10), 2135-2148.

10. Protonation‐Driven Membrane Insertion of a pH‐Low Insertion Peptide. (2016) S.Z. Hanz, N.S. Shu, J. Qian, N. Christman, P. Kranz, M. An, C. Grewer, W. Qiang, Angew. Chem. Int. Ed. 128 (40), 12564-12569.

9. Flexibility and solvation of amyloid-β hydrophobic core. (2016) L. Vugmeyster, M.A. Clark, I.B. Falconer, D. Ostrovsky, D. Gantz, W. Qiang, G.L. Hoatson, J. Biol. Chem. 291 (35), 18484-18495.

8. Distinct membrane disruption pathways are induced by 40-residue β-amyloid peptides. (2016) D.A. Delgado, K. Doherty, Q. Cheng, H. Kim, D. Xu, H. Dong, C. Grewer, W. Qiang, J. Biol. Chem. 291 (33), 12233-12241.

7. Membrane activity of a supramolecular peptide-based chemotherapeutic enhancer. (2016) D. Xu, L. JiangL. DeRidderB. ElmoreM. Bukhari, W. QiangD.S.K. Samways, H. Dong, Molecular Biosystems 12(9), 2695-2699.

6. Residue-specific structures and membrane locations of pH-low insertion peptide by solid-state nuclear magnetic resonance. (2015) N.S. Shu, M.S. Chung, L. Yao, M. An, W. Qiang  Nat. Commun. 6(1), 1-10.

5. Quaternary structure defines a large class of amyloid-β oligomers neutralized by sequestration. (2015) P. Liu, M.N. Reed, L.A. Kotilinek, M.K.O. Grant, C.L. Forster, W. Qiang, S.L. Shapiro, J.H. Reichl, A.C.A. Chiang, J.L. Jankowsky, C.M. Wilmot, J.P. Cleary, K.R. Zahs, K.H. Ashe, Cell Rep. 11 (11), 1760-1771.

4. Competition between fibrillation and induction of vesicle fusion for the membrane-associated 40-residue β-amyloid peptides. (2015) R.D. Akinlolu, M. Nam, W. Qiang, Biochemistry 54 (22), 3416-3419.

3. Modeling an in-register, parallel “iowa” aβ fibril structure using solid-state NMR data from labeled samples with rosetta. (2015) N.G. Sgourakis, W.M. Yau, W. Qiang, Structure 23 (1), 216-227.

2. Fibrillation of β amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption. (2015) W. Qiang, W.M. Yau, J. Schulte, BBA-Biomembranes 1848(1), 266-276.

1. Structural Evolution and Membrane Interaction of the 40-Residue β Amyloid Peptides: Differences in the Initial Proximity between Peptides and the Membrane Bilayer Studied by Solid-State Nuclear Magnetic Resonance Spectroscopy. (2014) W. Qiang, R.D. Akinlolu, M. Nam, N. Shu, Biochemistry 53(48), 7503-7514.

bottom of page