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 |
|
Show low-probability matches. |