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Wei Qiang, Ph.D. - Publications

Affiliations: 
2005-2009 Michigan State University, East Lansing, MI 
 2014- Chemistry State University of New York, Binghamton, Vestal, NY, United States 
Area:
Physical Chemistry, Biochemistry, NMR
Website:
https://wqiang.wixsite.com/mysite
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54 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
2024 Vugmeyster L, Au DF, Frazier B, Qiang W, Ostrovsky D. Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles. Physical Chemistry Chemical Physics : Pccp. 26: 5466-5478. PMID 38277177 DOI: 10.1039/d3cp04824a  0.343
2023 Qiang W, Kengwerere MK, Zhao W, Scott FJ, Wutoh-Hughes X, Wang T, Mentink-Vigier F. Heterotypic Interactions between the 40- and 42-Residue Isoforms of β-Amyloid Peptides on Lipid Bilayer Surfaces. Acs Chemical Neuroscience. 14: 4153-4162. PMID 37991929 DOI: 10.1021/acschemneuro.3c00523  0.361
2023 Kenyaga JM, Oteino SA, Sun Y, Qiang W. In-cell P solid-state NMR measurements of the lipid dynamics and influence of exogeneous β-amyloid peptides on live neuroblastoma neuro-2a cells. Biophysical Chemistry. 297: 107008. PMID 36989875 DOI: 10.1016/j.bpc.2023.107008  0.375
2022 Kenyaga JM, Cheng Q, Qiang W. Early stage β-amyloid-membrane interactions modulate lipid dynamics and influence structural interfaces and fibrillation. The Journal of Biological Chemistry. 298: 102491. PMID 36115457 DOI: 10.1016/j.jbc.2022.102491  0.399
2021 Otieno SA, Qiang W. Roles of key residues and lipid dynamics reveal pHLIP-membrane interactions at intermediate pH. Biophysical Journal. PMID 34624273 DOI: 10.1016/j.bpj.2021.10.001  0.449
2021 Deo T, Cheng Q, Paul S, Qiang W, Potapov A. Application of DNP-enhanced solid-state NMR to studies of amyloid-β peptide interaction with lipid membranes. Chemistry and Physics of Lipids. 105071. PMID 33716023 DOI: 10.1016/j.chemphyslip.2021.105071  0.394
2020 Qiang W, Doherty KE, Klees LM, Tobin-Miyaji Y. Time-Dependent Lipid Dynamics, Organization and Peptide-Lipid Interaction in Phospholipid Bilayers with Incorporated β-Amyloid Oligomers. The Journal of Physical Chemistry Letters. 8329-8336. PMID 32931283 DOI: 10.1021/Acs.Jpclett.0C01967  0.79
2020 Hu ZW, Au DF, Cruceta L, Vugmeyster L, Qiang W. The N-terminal modified Aβ variants enable modulations to the structures and cytotoxicity levels of wild-type Aβ fibrils through cross-seeding. Acs Chemical Neuroscience. PMID 32603584 DOI: 10.1021/Acschemneuro.0C00316  0.358
2020 Cheng Q, Hu ZW, Tobin-Miyaji Y, Perkins AE, Deak T, Qiang W. Fibrillization of 40-Residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms. Biomolecules. 10. PMID 32521743 DOI: 10.3390/biom10060881  0.372
2019 Ding X, Sun F, Chen J, Chen L, Tobin-Miyaji Y, Xue S, Qiang W, Shi-Zhong L. Amyloid-Forming Segment Induces Aggregation of FUS-LC Domain from Phase Separation Modulated by Site-Specific Phosphorylation. Journal of Molecular Biology. PMID 31805282 DOI: 10.1016/J.Jmb.2019.11.017  0.322
2019 Vugmeyster L, Au DF, Ostrovsky D, Kierl B, Fu R, Hu ZW, Qiang W. Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N-Terminus. Biophysical Journal. PMID 31570231 DOI: 10.1016/J.Bpj.2019.09.004  0.356
2019 Hu ZW, Vugmeyster L, Au DF, Ostrovsky D, Sun Y, Qiang W. Molecular structure of an N-terminal phosphorylated β-amyloid fibril. Proceedings of the National Academy of Sciences of the United States of America. PMID 31097588 DOI: 10.1073/Pnas.1818530116  0.337
2019 Otieno SA, Klees LM, Zhang A, Giza HM, Hanz SZ, Chakravorty B, Yao L, An M, Qiang W. The pH-Specific Thermodynamic Intermediates of Phlip Membrane Insertion Biophysical Journal. 116: 513a. DOI: 10.1016/J.Bpj.2018.11.2766  0.773
2018 Otieno SA, Hanz SZ, Chakravorty B, Zhang A, Klees LM, An M, Qiang W. pH-dependent thermodynamic intermediates of pHLIP membrane insertion determined by solid-state NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 30442664 DOI: 10.1073/Pnas.1809190115  0.778
2018 Xu D, Chen W, Tobin-Miyaji YJ, Sturge CR, Yang S, Elmore B, Singh A, Pybus C, Greenberg D, Sellati TJ, Qiang W, Dong H. Fabrication and Microscopic and Spectroscopic Characterization of Cytocompatible Self-Assembling Antimicrobial Nanofibers. Acs Infectious Diseases. PMID 29949345 DOI: 10.1021/Acsinfecdis.8B00069  0.31
2018 Qiang W, Doherty KE. Model Phospholipid Liposomes to Study the β-Amyloid-Peptide-Induced Membrane Disruption. Methods in Molecular Biology (Clifton, N.J.). 1777: 355-367. PMID 29744848 DOI: 10.1007/978-1-4939-7811-3_23  0.512
2018 Cheng Q, Hu ZW, Doherty KE, Tobin-Miyaji YJ, Qiang W. 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. Biochimica Et Biophysica Acta. PMID 29548698 DOI: 10.1016/J.Bbamem.2018.03.008  0.543
2017 Vugmeyster L, Ostrovsky D, Hoatson GL, Qiang W, Falconer IB. Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation. The Journal of Physical Chemistry. B. PMID 28699757 DOI: 10.1021/Acs.Jpcb.7B04726  0.31
2017 Hu ZW, Ma MR, Chen YX, Zhao YF, Qiang W, Li YM. Phosphorylation at Ser(8) as an intrinsic regulatory switch to regulate the morphologies and structures of Alzheimer's 40-residue β-amyloid (Aβ40) fibrils. The Journal of Biological Chemistry. 292: 8846. PMID 28550132 DOI: 10.1074/Jbc.A116.757179  0.33
2017 Cheng Q, Qiang W. 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. The Journal of Physical Chemistry. B. PMID 28535056 DOI: 10.1021/Acs.Jpcb.7B02953  0.384
2017 Qiang W, Yau WM, Lu JX, Collinge J, Tycko R. Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes. Nature. PMID 28052060 DOI: 10.1038/Nature20814  0.552
2016 Vugmeyster L, Ostrovsky D, Clark MA, Falconer IB, Hoatson GL, Qiang W. Fast Motions of Key Methyl Groups in Amyloid-β Fibrils. Biophysical Journal. 111: 2135-2148. PMID 27851938 DOI: 10.1016/J.Bpj.2016.10.001  0.332
2016 Hanz SZ, Shu NS, Qian J, Christman N, Kranz P, An M, Grewer C, Qiang W. Protonation-Driven Membrane Insertion of a pH-Low Insertion Peptide. Angewandte Chemie (International Ed. in English). PMID 27578553 DOI: 10.1002/Anie.201605203  0.685
2016 Vugmeyster L, Clark MA, Falconer IB, Ostrovsky D, Gantz D, Qiang W, Hoatson GL. Flexibility and Solvation of Amyloid-β Hydrophobic Core. The Journal of Biological Chemistry. PMID 27402826 DOI: 10.1074/Jbc.M116.740530  0.331
2016 Delgado DA, Doherty K, Cheng Q, Kim H, Xu D, Dong H, Grewer C, Qiang W. Distinct membrane disruption pathways induced by the 40-resdiue β-amyloid peptides. The Journal of Biological Chemistry. PMID 27056326 DOI: 10.1074/Jbc.M116.720656  0.509
2016 An M, Klees L, Zhang A, Onyango JO, Gordon EA, Eng C, Winge-Barnes S, Lichter E, Nazarenko V, Bell MM, Bandler IG, Awad AK, Shu NS, Qiang W, Yao L. What is the Fate-Determining Step in pHLIP-Mediated Cargo Delivery? Biophysical Journal. 110: 80a. DOI: 10.1016/J.Bpj.2015.11.493  0.763
2015 Shu NS, Chung MS, Yao L, An M, Qiang W. Residue-specific structures and membrane locations of pH-low insertion peptide by solid-state nuclear magnetic resonance. Nature Communications. 6: 7787. PMID 26195283 DOI: 10.1038/Ncomms8787  0.718
2015 Liu P, Reed MN, Kotilinek LA, Grant MK, Forster CL, Qiang W, Shapiro SL, Reichl JH, Chiang AC, Jankowsky JL, Wilmot CM, Cleary JP, Zahs KR, Ashe KH. Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration. Cell Reports. 11: 1760-71. PMID 26051935 DOI: 10.1016/J.Celrep.2015.05.021  0.317
2015 Akinlolu RD, Nam M, Qiang W. Competition between Fibrillation and Induction of Vesicle Fusion for the Membrane-Associated 40-Residue β-Amyloid Peptides Biochemistry. 54: 3416-3419. PMID 25988500 DOI: 10.1021/Acs.Biochem.5B00321  0.482
2015 Sgourakis NG, Yau WM, Qiang W. Modeling an in-register, parallel "iowa" aβ fibril structure using solid-state NMR data from labeled samples with rosetta. Structure (London, England : 1993). 23: 216-27. PMID 25543257 DOI: 10.1016/J.Str.2014.10.022  0.387
2015 Qiang W, Yau WM, Schulte J. Fibrillation of β amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption. Biochimica Et Biophysica Acta. 1848: 266-76. PMID 24769158 DOI: 10.1016/J.Bbamem.2014.04.011  0.48
2014 Qiang W, Akinlolu RD, Nam M, Shu N. 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. Biochemistry. 53: 7503-14. PMID 25397729 DOI: 10.1021/Bi501003N  0.533
2013 Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R. Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell. 154: 1257-68. PMID 24034249 DOI: 10.1016/J.Cell.2013.08.035  0.559
2013 Qiang W, Kelley K, Tycko R. Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth. Journal of the American Chemical Society. 135: 6860-71. PMID 23627695 DOI: 10.1021/Ja311963F  0.566
2013 Gabrys CM, Qiang W, Sun Y, Xie L, Schmick SD, Weliky DP. Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures. The Journal of Physical Chemistry. A. 117: 9848-59. PMID 23418890 DOI: 10.1021/Jp312845W  0.79
2013 Lu J, Qiang W, Yau W, Schwieters CD, Meredith SC, Tycko R. Molecular Structure of beta-Amyloid Fibrils in Alzheimer's Disease Brain Tissue. Cell. 154: 1257-1268. DOI: 10.2210/Pdb2M4J/Pdb  0.556
2013 Lu J, Qiang W, Meredith S, Yau W, Schweiters C, Tycko R. 40-residue beta-amyloid fibril derived from Alzheimer's disease brain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19009  0.524
2012 Qiang W, Tycko R. Zero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance. The Journal of Chemical Physics. 137: 104201. PMID 22979851 DOI: 10.1063/1.4749258  0.519
2012 Hu KN, Qiang W, Bermejo GA, Schwieters CD, Tycko R. Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 218: 115-27. PMID 22449573 DOI: 10.1016/J.Jmr.2012.03.001  0.546
2012 Qiang W, Yau WM, Luo Y, Mattson MP, Tycko R. Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America. 109: 4443-8. PMID 22403062 DOI: 10.1073/Pnas.1111305109  0.579
2012 Qiang W, Yau W, Luo Y, Mattson M, Tycko R. 40-residue D23N beta amyloid fibril Journal of Back and Musculoskeletal Rehabilitation. 109: 4443-4448. DOI: 10.2210/Pdb2Lnq/Pdb  0.528
2012 Qiang W, Yau W, Luo Y, Mattson M, Tycko R. Antiparallel beta-sheet structural model for Iowa-mutant beta-amyloid fibrils Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17774  0.521
2011 Hu KN, Qiang W, Tycko R. A general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers. Journal of Biomolecular Nmr. 50: 267-76. PMID 21710190 DOI: 10.1007/S10858-011-9517-1  0.528
2011 Qiang W, Yau WM, Tycko R. Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth. Journal of the American Chemical Society. 133: 4018-29. PMID 21355554 DOI: 10.1021/Ja109679Q  0.58
2010 Tristram-Nagle S, Chan R, Kooijman E, Uppamoochikkal P, Qiang W, Weliky DP, Nagle JF. HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics. Journal of Molecular Biology. 402: 139-53. PMID 20655315 DOI: 10.1016/J.Bpj.2010.12.1234  0.707
2010 Gabrys CM, Yang R, Wasniewski CM, Yang J, Canlas CG, Qiang W, Sun Y, Weliky DP. Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide. Biochimica Et Biophysica Acta. 1798: 194-201. PMID 19616505 DOI: 10.1016/J.Bbamem.2009.07.007  0.722
2010 Diaz-Martinez M, Chakraborty H, Qiang W, Weliky D, Lentz BR. Effect of HIV Gp41 Fusion Peptide and its Cross-Linked Oligomers in Membrane Fusion Biophysical Journal. 98: 674a. DOI: 10.1016/J.Bpj.2009.12.3703  0.715
2009 Qiang W, Sun Y, Weliky DP. A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide. Proceedings of the National Academy of Sciences of the United States of America. 106: 15314-9. PMID 19706388 DOI: 10.1073/Pnas.0907360106  0.744
2009 Qiang W, Weliky DP. HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of beta strand conformation with membrane cholesterol, and proximity to lipid headgroups. Biochemistry. 48: 289-301. PMID 19093835 DOI: 10.1021/Bi8015668  0.739
2009 Sackett K, Qiang W, Sun Y, Nethercott MJ, Shai Y, Weliky DP. Functional and Structural Measurements of HIV gp41 Fusion Protein Constructs Biophysical Journal. 96: 358a. DOI: 10.1016/J.Bpj.2008.12.1807  0.789
2008 Qiang W, Bodner ML, Weliky DP. Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries. Journal of the American Chemical Society. 130: 5459-71. PMID 18370385 DOI: 10.1021/Ja077302M  0.778
2007 Zheng Z, Qiang W, Weliky DP. Investigation of finite-pulse radiofrequency-driven recoupling methods for measurement of intercarbonyl distances in polycrystalline and membrane-associated HIV fusion peptide samples. Magnetic Resonance in Chemistry : Mrc. 45: S247-60. PMID 18157840 DOI: 10.1002/Mrc.2160  0.705
2007 Qiang W, Yang J, Weliky DP. Solid-state nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups. Biochemistry. 46: 4997-5008. PMID 17417873 DOI: 10.1021/Bi6024808  0.728
2005 Du JT, Li YM, Ma QF, Qiang W, Zhao YF, Abe H, Kanazawa K, Qin XR, Aoyagi R, Ishizuka Y, Nemoto T, Nakanishi H. Synthesis and conformational properties of phosphopeptides related to the human tau protein. Regulatory Peptides. 130: 48-56. PMID 15869817 DOI: 10.1016/J.Regpep.2005.03.003  0.33
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