53. Zheng Q, Lee B, Kebede MT, Ivancic VA, Kemeh MM, Lemos Brito H, Spratt DE and Lazo ND. Exchange Broadening Underlies the Enhancement of IDE-Dependent Degradation of Insulin by Anionic Membranes. ACS Omega 2022, 7, 24757-24765. This work was supported by a grant from the National Institute on Aging (R15AG055043).
52. Zheng Q, Kebede MT, Lee B, Krasinski CA, Islam S, Wurfl LA, Kemeh MM, Ivancic VA, Jakobsche CE, Spratt DE and Lazo ND. Differential Effects of Polyphenols on Insulin Proteolysis by the Insulin-degrading Enzyme. Antioxidants 2021, 10(1342), 1-11. This work was supported by a grant from the National Institute on Aging (R15AG055043).
51. Bocach DB, Jones KL, Bell JM, Zheng Q, Lazo ND, Smith-Carpenter JE, Alper BJ. Ghrelin Proteolysis by Insulin-degrading Enzyme. bioRxiv
50. Zheng Q, Carty SN and Lazo ND. Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides. Langmuir 2020, 86, 8389-8397. This work was supported by a grant from the National Institute on Aging (R15AG055043) and by the Lise Ann and Leo E. Beavers II endowment to Clark University.
DOI: 10.1021/acs.langmuir.0c00723
49. Zheng Q, Kebede MK, Kemeh MM, Islam S, Lee B, Bleck SD, Wurfl LA and Lazo ND. Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies. Molecules 2019, 24 (2316), 1-20. This work was supported by a grant from the National Institute on Aging (R15AG055043).
DOI: 10.3390/molecules24122316
48. Ivancic VA, Krasinski CA, Zheng Q, Meservier RJ, Spratt DE and Lazo ND. Enzyme kinetics from circular dichroism of insulin reveals mechanistic insights into the regulation of insulin-degrading enzyme. Bioscience Reports 2018, 38(6), 1-10. This work was supported by a grant from the National Institute on Aging (R15AG055043).
PMID: 30305381 PMCID: PMC6239264 DOI: 10.1042/BSR20181416
47. Krasinski CA, Ivancic VA, Zheng Q, Spratt DE and Lazo ND. Resveratrol sustains insulin-degrading enzyme activity towards Aß42. ACS Omega 2018, 3(10), 13275-13282. This work was supported by a grant from the National Institute on Aging (R15AG055043).
PMID: 30411033 PMCID: PMC6210067 DOI: 10.1021/acsomega.8b01913
46. Krasinski CA, Zheng Q, Ivancic VA, Spratt DE and Lazo ND. The longest amyloid-ß precursor protein intracellular domain produced with Aß42 forms ß-sheet-containing monomers that self-assemble and are proteolyzed by insulin-degrading enzyme. ACS Chem. Neurosci. 2018, 9, 2892-2897. This work was supported by a grant from the National Institute on Aging (R15AG055043).
PMID: 30067897 DOI: 10.1021/acschemneuro.8b00305
45. Zheng Q and Lazo ND. Mechanistic studies of the inhibition of insulin fibril formation by rosmarinic acid. J. Phys. Chem B 2018, 122, 2323-2331. This work was supported in part by a grant from the Lise Ann and Leo E. Beavers II endowment to Clark University.
PMID: 29401384 DOI: 10.1021/acs.jpcb.8b00689
44. Fontaine DFA, Ivancic VA, Reardon MB, Lazo ND, Jakobsche CE. A versatile platform for adding functional properties to amyloid fibrils. Org. Biomol. Chem. 2017, 15, 8023-8027.
PMID: 28930349 DOI: 10.1039/c7ob02042b
43. Ivancic VA, Ekayanake O and Lazo ND. Binding mode of thioflavin T on the surface of amyloid fibrils. ChemPhysChem 2016, 17, 2461-2464.
PMID: 27165642 DOI: 10.1002/cphc.201600246
42. Selmani V, Robbins KJ, Ivancic VA and Lazo ND. K114 (trans, trans)-bromo-2,5-bis (4-hydroxystyryl)benzene is an efficient detector of cationic amyloid fibrils. Protein Science 2015, 24, 420-425.
PMID: 25524064 PMCID: PMC4353367 DOI: 10.1002/pro.2620
41. Robbins KJ, Liu G, Selmani V and Lazo ND. Conformational analysis of thioflavin T bound to the surface of amyloid fibrils. Langmuir 2012, 28, 16490-16495.
PMID: 23151310 DOI: 10.1021/la303677t
40. Liu G, Gaines JC, Robbins KJ and Lazo ND. Kinetic profile of amyloid formation in the presence of an aromatic inhibitor by nuclear magnetic resonance. ACS Med. Chem. Lett. 2012, 3, 856-859.
PMID: 24900390 PMCID: PMC4025671 DOI: 10.1021/ml300147m
39. Liu G, Robbins KJ, Sparks S, Selmani V, Bilides K and Lazo ND. Helix dipole effects in peptide self-assembly to amyloid. Biochemistry 2012, 51, 4167-4174.
PMID: 22559877 DOI: 10.1021/bi3001616
38. Sparks S, Liu G, Robbins KJ and Lazo ND. Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix. Biochem. Biophys. Res. Commun. 2012, 422, 551-555.
PMID: 22579683 DOI: 10.1016/j.bbrc.2012.05.013
37. Robbins KJ, Liu G, Lin G and Lazo ND. Detection of strongly bound thioflavin T species in amyloid fibrils by ligand-detected 1H NMR. J. Phys. Chem. Lett. 2011, 2, 735-740.
36. Liu G, Prabhakar A, Aucoin D, Simon M, Sparks S, Robbins KJ, Sheen, Petty SA and Lazo ND. Mechanistic studies of peptide self-assembly: Transient α-helices to stable β-sheets. J. Am. Chem. Soc. 2010, 132, 18223-18232.
PMID: 21138275 DOI: 10.1021/ja1069882
35. Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB, Shea J-E, Ruotolo BT, Robinson CV, Bowers MT. Amyloid-β protein oligomerization: The importance of tetramers and dodecamers in the aetiology of Alzheimer’s disease. Nature Chem. 2009, 1(4):326-331.
34. Murray MM, Krone MG, Bernstein SL, Baumketner A, Condron MM, Lazo ND, Teplow DB, Wyttenbach T, Shea JE, Bowers MT. Amyloid-β protein: Experiment and theory on the 21-30 fragment. J. Phys. Chem. B 2009, 113(17):6041-6046.
33. 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-β protein. J. Mol. Biol. 2008, 381(1): 221-228.
32. 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-β protein monomer folding nucleus. Proc. Natl. Acad. Sci. 2007, 104, 16522-16527.
31. Teplow DB, Lazo ND, Bitan G, Bernstein S, Bowers MT, Baumketner, A, Shea J-E, Urbanc B, Cruz L, Borreguero JM, Stanley HE. Elucidating amyloid-β protein folding and assembly: A multidisciplinary approach. Accts. Chem. Res. 2006, 39, 635-645.
30. Maier M, Seabrook TJ, Lazo ND, Jiang L, Das P, Janus C, Lemere CA. Short A immunogens reduce cerebral Aβ load and learning deficits in an Alzheimer’s disease mouse model in the absence of an Aβ-specific cellular immune response. J. Neurosci. 2006, 26, 4717-4728.
29. Baumketner A, Bernstein SL, Wyttenbach T, Lazo ND, Teplow DB, Bowers MT, Shea J-E. Structure of the 21-30 fragment of Alzheimer’s amyloid-β protein: A molecular dynamics study. Protein Science 2006, 15, 1239-1247.
28. Cruz L, Urbanc B, Borreguero JM, Lazo ND, Teplow DB, Stanley HE. Solvent and mutation effects on the nucleation of amyloid-β protein folding. Proc. Natl. Acad. Sci. 2005, 102, 18258-18263.
27. Lazo ND, Grant MA, Condron MM, Rigby AC, Teplow DB. On the nucleation of amyloid-β protein monomer folding. Protein Science 2005, 14, 1581-1596.
26. Borreguero JM, Urbanc B, Lazo ND, Buldyrev SV, Teplow DB, Stanley HE. Folding events in the 21-30 region of amyloid-β protein (Aβ) studied in silico. Proc. Natl. Acad. Sci. 2005, 102, 6015-6020.
25. Ferraro D, Lazo ND, Robertson AD. EX1 hydrogen exchange and protein folding. Biochemistry 2004, 43, 587-594.
24. Lazo ND, Downing DT. Effects of Na2SO4 on hydrophobic and electrostatic interactions between amphipathic α-helices. J. Peptide Res. 2001, 58, 457-463.
23. Lazo ND, Downing DT. A mixture of α-helical and 310-helical conformations for involucrin in human epidermal corneocyte envelopes provides a scaffold for the attachment of both lipids and proteins. J. Biol. Chem. 1999, 274, 37340-37344.
22. Downing DT, Lazo ND. Molecular modeling indicates that the pathological conformation of prion proteins may be β-helical. Biochemical J. 1999, 343, 453-460.
21. Lazo ND, Downing DT. The crystalline regions of Bombyx mori silk fibroin may exhibit β-turn and β-helix conformations. Macromolecules 1999, 32, 4700-4705.
20. Lazo ND, Downing DT. Fibril formation by amyloid-β(34-42) may involve β-helical protofibrils. J. Peptide Res. 1999, 53, 633-640.
19. Lazo ND, Downing DT. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry 1998, 37, 1731-1735.
18. Lazo ND, Downing DT. Stabilization of amphipathic α-helix and β-sheet conformations in synthetic peptides by side-chain hydrogen bonding in the presence and absence of ionic interactions. J. Peptide Res. 1998, 51, 85-89.
17. Lazo ND, Downing DT. β-helical fibrils from a model peptide. Biochem. Biophys. Res. Commun. 1997, 235, 675-679.
16. Lazo ND, Downing DT. Circular dichroism of model peptides emulating the α-helical regions of intermediate filament proteins. Biochemistry 1997, 36, 2559-2565.
15. Lazo ND, Meine J, Downing DT. Lipids are covalently attached to rigid corneocyte envelopes existing predominantly as β-sheets: a solid-state NMR study. J. Invest. Dermatol. 1995, 105, 296-300.
14. Hu W, Lazo ND, Cross TA. Tryptophan dynamics and structural refinement in a lipid bilayer: solid-state NMR of the gramicidin channel. Biochemistry 1995, 34, 14138-14146.
13. Lazo ND, Hu W, Cross TA. Low-temperature 15N NMR characterization of polypeptide backbone vibrations. J. Magn. Reson. Ser. B 1995, 107, 53-60.
12. Robson KJ, Stewart ME, Lazo ND, Michelsen S, Downing DT. 6-Hydroxy-4-sphingenine in human epidermal ceramides. J. Lipid Res. 1994, 35, 2060-2068.
11. Lazo ND, Hu W, Lee K-C, Cross TA. Rapidly frozen polypeptide samples for characterization of high-definition dynamics by solid-state NMR spectroscopy. Biochem. Biophys. Res. Commun. 1993, 197, 904-909.
10. Cross TA, Ketchem RR, Hu W, Lee-K-C, Lazo ND, North CL. Structure and dynamics of a membrane-bound polypeptide. Bull. Magn. Reson. 1992, 14, 96-101.
9. Lazo ND, Hu W, Cross TA. Probing lipid-protein interactions by solid-state NMR spectroscopy of fast-frozen samples. J. Chem. Soc. Chem. Commun. 1992, 1529-1531.
8. Lazo ND, Murray DK, Kieke ML, Haw JF. In situ 13C solid-state NMR study of the Cu/ZnO/alumina methanol-synthesis catalyst. J. Am. Chem. Soc. 1992, 114, 8552-8559.
7. Munson EJ, Khier AK, Lazo ND, Haw JF. In situ solid-state NMR study of methanol-to-gasoline chemistry in zeolite HZSM-5. J. Phys. Chem. 1992, 96, 7740-7746.
6. Munson EJ, Lazo ND, Moellenhoff ME, Haw JF. CO is neither an intermediate nor a catalyst in MTG chemistry on zeolite HZSM-5. J. Am. Chem. Soc. 1991, 113, 2783-2784.
5. Lazo ND, Richardson BR, Schettler PS, White JL, Munson EJ, Haw JF. In situ variable-temperature solid-state 13C NMR study of the reactions of isobutylene in zeolites HY and HZSM-5. J. Phys. Chem. 1991, 95, 9420-9425.
4. Lazo ND, White JL, Munson EJ, Lambregts M, Haw JF. Structure, dynamics and reactivity of an alkoxy intermediate formed from acetylene on zeolite catalysts: an in situ solid-state NMR study. J. Am. Chem. Soc. 1991, 112, 4050-4052.
3. White JL, Lazo ND, Richardson BR, Haw JF. In situ solid-state NMR investigation of cracking reactions in zeolite HY. J. Catal. 1990, 125, 260-263.
2. Richardson BR, Lazo ND, Schettler PS, White JL, Haw JF. Reactions of butadiene in zeolite catalysts by in situ variable-temperature solid-state nuclear magnetic resonance spectrometry. J. Am. Chem. Soc. 1990, 112, 2886-2891.
1. Haw JF, Richardson BR, Oshiro IS, Lazo ND, Speed JA. Reactions of propene on zeolite HY catalyst studied by in situ variable-temperature solid-state nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 1989, 111, 2052-2058.
Book Chapters
3. Lazo ND, Maji SK, Fradinger EA, Bitan G, Teplow DB. The amyloid-β protein. In Amyloid proteins – the β-sheet conformation and disease (Sipe JD, Editor), Wiley VCH, 2005, Volume 2, 385-491.
2. Fradinger EA, Maji SK, Lazo ND, Teplow DB. Studying amyloid-β protein assembly. In Amyloid Precursor Protein: A Practical Approach (Xia W and Xu H, Editors), CRC Press, 2005, 83-110.
1. Downing DT, Lazo ND. Lipid and protein structures in the permeability barrier. In Dry Skin and Moisturizers: Chemistry and Function (Meibach HI and Loden M, Editors), CRC Press, 2000, 39-44.
