Year |
Citation |
Score |
2023 |
Kemeh MM, Lazo ND. Highly toxic Aβ begets more Aβ. Neural Regeneration Research. 19: 1871-1872. PMID 38227503 DOI: 10.4103/1673-5374.390983 |
0.334 |
|
2020 |
Zheng Q, Carty SN, Lazo ND. Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 32628488 DOI: 10.1021/acs.langmuir.0c00723 |
0.532 |
|
2019 |
Zheng Q, Kebede MT, Kemeh MM, Islam S, Lee B, Bleck SD, Wurfl LA, Lazo ND. Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies. Molecules (Basel, Switzerland). 24. PMID 31234523 DOI: 10.3390/molecules24122316 |
0.535 |
|
2018 |
Krasinski CA, Zheng Q, Ivancic VA, Spratt DE, Lazo ND. The Longest Amyloid-β Precursor Protein Intracellular Domain Produced with Aβ42 Forms β-sheet-containing Monomers that Self-assemble and are Proteolyzed by Insulin-degrading Enzyme. Acs Chemical Neuroscience. PMID 30067897 DOI: 10.1021/acschemneuro.8b00305 |
0.461 |
|
2018 |
Zheng Q, Lazo ND. Mechanistic Studies of the Inhibition of Insulin Fibril Formation by Rosmarinic Acid. The Journal of Physical Chemistry. B. PMID 29401384 DOI: 10.1021/acs.jpcb.8b00689 |
0.34 |
|
2017 |
Fontaine DFA, Ivancic VA, Reardon MB, Lazo ND, Jakobsche CE. A versatile platform for adding functional properties to amyloid fibrils. Organic & Biomolecular Chemistry. PMID 28930349 DOI: 10.1039/C7Ob02042B |
0.339 |
|
2016 |
Ivancic V, Ekanayake O, Lazo N. Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils by NMR. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27165642 DOI: 10.1002/cphc.201600246 |
0.435 |
|
2015 |
Selmani V, Robbins KJ, Ivancic VA, Lazo ND. K114 (trans, trans)-bromo-2,5-bis(4-hydroxystyryl)benzene is an efficient detector of cationic amyloid fibrils. Protein Science : a Publication of the Protein Society. 24: 420-5. PMID 25524064 DOI: 10.1002/Pro.2620 |
0.721 |
|
2012 |
Liu G, Gaines JC, Robbins KJ, Lazo ND. Kinetic profile of amyloid formation in the presence of an aromatic inhibitor by nuclear magnetic resonance. Acs Medicinal Chemistry Letters. 3: 856-9. PMID 24900390 DOI: 10.1021/Ml300147M |
0.756 |
|
2012 |
Robbins KJ, Liu G, Selmani V, Lazo ND. Conformational analysis of thioflavin T bound to the surface of amyloid fibrils. Langmuir : the Acs Journal of Surfaces and Colloids. 28: 16490-5. PMID 23151310 DOI: 10.1021/La303677T |
0.745 |
|
2012 |
Sparks S, Liu G, Robbins KJ, Lazo ND. Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix. Biochemical and Biophysical Research Communications. 422: 551-5. PMID 22579683 DOI: 10.1016/J.Bbrc.2012.05.013 |
0.77 |
|
2012 |
Liu G, Robbins KJ, Sparks S, Selmani V, Bilides KM, Gomes EE, Lazo ND. Helix-dipole effects in peptide self-assembly to amyloid. Biochemistry. 51: 4167-74. PMID 22559877 DOI: 10.1021/Bi3001616 |
0.762 |
|
2011 |
Robbins KJ, Liu G, Lin G, Lazo ND. Detection of strongly bound thioflavin T species in amyloid fibrils by ligand-detected 1H NMR Journal of Physical Chemistry Letters. 2: 735-740. DOI: 10.1021/Jz200066B |
0.739 |
|
2010 |
Liu G, Prabhakar A, Aucoin D, Simon M, Sparks S, Robbins KJ, Sheen A, Petty SA, Lazo ND. Mechanistic studies of peptide self-assembly: transient α-helices to stable β-sheets. Journal of the American Chemical Society. 132: 18223-32. PMID 21138275 DOI: 10.1021/Ja1069882 |
0.757 |
|
2009 |
Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB, Shea JE, Ruotolo BT, Robinson CV, Bowers MT. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chemistry. 1: 326-31. PMID 20703363 DOI: 10.1038/Nchem.247 |
0.405 |
|
2008 |
Krone MG, Baumketner A, Bernstein SL, Wyttenbach T, Lazo ND, Teplow DB, Bowers MT, Shea JE. Effects of familial Alzheimer's disease mutations on the folding nucleation of the amyloid beta-protein. Journal of Molecular Biology. 381: 221-8. PMID 18597778 DOI: 10.1016/J.Jmb.2008.05.069 |
0.346 |
|
2008 |
Lazo ND, Maji SK, Fradinger EA, Bitan G, Teplow DB. The Amyloid β Protein Amyloid Proteins: the Beta Sheet Conformation and Disease. 2: 384-491. DOI: 10.1002/9783527619344.ch17 |
0.315 |
|
2007 |
Grant MA, Lazo ND, Lomakin A, Condron MM, Arai H, Yamin G, Rigby AC, Teplow DB. Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus. Proceedings of the National Academy of Sciences of the United States of America. 104: 16522-7. PMID 17940047 DOI: 10.1073/Pnas.0705197104 |
0.393 |
|
2006 |
Teplow DB, Lazo ND, Bitan G, Bernstein S, Wyttenbach T, Bowers MT, Baumketner A, Shea JE, Urbanc B, Cruz L, Borreguero J, Stanley HE. Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach. Accounts of Chemical Research. 39: 635-45. PMID 16981680 DOI: 10.1021/Ar050063S |
0.346 |
|
2006 |
Baumketner A, Bernstein SL, Wyttenbach T, Lazo ND, Teplow DB, Bowers MT, Shea JE. Structure of the 21-30 fragment of amyloid beta-protein. Protein Science : a Publication of the Protein Society. 15: 1239-47. PMID 16731963 DOI: 10.1110/Ps.062076806 |
0.407 |
|
2005 |
Cruz L, Urbanc B, Borreguero JM, Lazo ND, Teplow DB, Stanley HE. Solvent and mutation effects on the nucleation of amyloid beta-protein folding. Proceedings of the National Academy of Sciences of the United States of America. 102: 18258-63. PMID 16339896 DOI: 10.1073/Pnas.0509276102 |
0.397 |
|
2005 |
Lazo ND, Grant MA, Condron MC, Rigby AC, Teplow DB. On the nucleation of amyloid beta-protein monomer folding. Protein Science : a Publication of the Protein Society. 14: 1581-96. PMID 15930005 DOI: 10.1110/Ps.041292205 |
0.428 |
|
2005 |
Borreguero JM, Urbanc B, Lazo ND, Buldyrev SV, Teplow DB, Stanley HE. Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico. Proceedings of the National Academy of Sciences of the United States of America. 102: 6015-20. PMID 15837927 DOI: 10.1073/Pnas.0502006102 |
0.423 |
|
2004 |
Lazo N, Condron MM, Grant MA, Rigby AC, Teplow DB. P1-187 Probing nucleation of Abeta monomer folding Neurobiology of Aging. 25: S149. DOI: 10.1016/S0197-4580(04)80500-1 |
0.358 |
|
2001 |
Lazo ND, Downing DT. Effects of Na2SO4 on hydrophobic and electrostatic interactions between amphipathic α-helices Journal of Peptide Research. 58: 457-463. PMID 12005416 DOI: 10.1034/j.1399-3011.2001.10927.x |
0.316 |
|
1999 |
Lazo ND, Downing DT. A mixture of α-helical and 310-helical conformations for involucrin in the human epidermal corneocyte envelope provides a scaffold for the attachment of both lipids and proteins Journal of Biological Chemistry. 274: 37340-37344. PMID 10601302 DOI: 10.1074/jbc.274.52.37340 |
0.326 |
|
1999 |
Downing DT, Lazo ND. Molecular modelling indicates that the pathological conformations of prion proteins might be β-helical Biochemical Journal. 343: 453-460. PMID 10510313 DOI: 10.1042/0264-6021:3430453 |
0.339 |
|
1999 |
Lazo ND, Downing DT. Fibril formation by amyloid-β proteins may involve β-helical protofibrils Journal of Peptide Research. 53: 633-640. PMID 10408337 DOI: 10.1034/j.1399-3011.1999.00057.x |
0.445 |
|
1998 |
Lazo ND, Downing DT. Amyloid fibrils may be assembled from β-helical protofibrils Biochemistry. 37: 1731-1735. PMID 9492738 DOI: 10.1021/bi971016d |
0.517 |
|
1997 |
Lazo ND, Downing DT. β-helical fibrils from a model peptide Biochemical and Biophysical Research Communications. 235: 675-679. PMID 9207218 DOI: 10.1006/bbrc.1997.6863 |
0.423 |
|
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