top of page

Publications

To find publications online, click on the titles. A subscription may be necessary.

For my Google Scholar Profile, click HERE.

Journal Articles

  1. Skeens A., Markle J.M., Pettipas G.,  Frey S., and Legleiter J. Divalent cations promote huntingtin fibril formation on endoplasmic reticulum membranes. BBA-Biomembranes (2024) 1866:184339.

  2. Skeens A., Siriwardhana C., Massinople S.E., Wunder M.M., Keith K.M., Girman T., Ellis Z.L., Frey S.L. and Legleiter J. The polyglutamine domain is the primary driver of seeding in Huntingtin aggregation. PLoS One (2024) 19: e0298323.

  3. Stonebraker A.R., Hankin R., Kapp K.L., Li P., Valentine S.J., and Legleiter J. Charge within Nt17 peptides modulates huntingtin aggregation and initial lipid binding events. Biophysical Chemistry (2023) 303:107123.

  4. Stonebraker A.R., Beasley M., Massinople S., Wunder M., Li P., Valentine S.J., and Legleiter J. Cholesterol impacts the formation of huntingtin/lipid complexes and subsequent aggregation. Protein Science (2023) 32:e4642.

  5. Beasley M., Frazee N., Groover S., Valentine S.J., Mertz B., and Legleiter J. Physicochemical Properties Altered by the Tail Group of Lipid Membranes Influence Huntingtin Aggregation and Lipid Binding. Journal of Physical Chemistry B (2022) 126:3067-3081.

  6. Legleiter J., Thakkar R., Velasquez-Silva A., Miranda-Carvajal I., Whitaker S., Tomich J., and Comer J. Design of Peptides that Fold and Self-Assemble on Graphite. Journal of Chemical Information and Modeling (2022) 62:4066-4082.

  7. Adegbuyiro A., Stonebraker A.R., Sedighi F., Fan C.K., Hodges B., Li P., Valentine S.J., and Legleiter J. Oxidation Promotes Distinct Huntingtin Aggregates in the Presence and Absence of Membranes. Biochemistry (2022) 61:1517-1530.

  8. Adegbuyiro A., Sedighi F., Jain P., Pinti M.V., Siriwardhana C., Hollander J.M., and Legleiter J. Mitochondrial membranes modify mutant huntingtin aggregation. BBA-Biomembranes (2021) 1863:186363.

  9. Groover S.E., Legleiter J., and Battin E.E. Huntingtin Protein Purification and Experimentation: An Innovative Undergraduate Research-Based Biochemistry Experiment. Journal of Chemical Education (2021) 90:3011-3018.

  10. Groover S.E., Adegbuyiro A., Fan C.K., Hodges, B.L., Beasley M., Taylor K., Stonebraker A.R., Siriwardhana C., and Legleiter J. Macromolecular crowding in solution alters huntingtin interaction and aggregation at interfaces. Colloids and Surfaces B: Biointerfaces (2021) 206:111969.

  11. Beasley M., Groover S.E., Valentine S., and Legleiter J. Lipid headgroups alter huntingtin aggregation on membranes. BBA-Biomembranes (2021) 1863:183497.

  12. Groover S.E., Beasley M., Ramamurthy V., and Legleiter J., Phosphomimetic mutations impact huntingtin aggregation in the presence of a variety of lipid systems. Biochemistry (2020) 59:4681-4693.

  13. Beasley M., Stonebraker A.R., and Legleiter J. Normalizing Polydiacetylene Colorimetric Assays of Vesicle Binding Across Lipid Systems. Analytical Biochemistry (2020) 609:113864.

  14. Sedighi F., Adegibuyiro A., and Legleiter J.  SUMOylation of huntingtin prevents fibrillization and localization onto lipid membranes. ACS Chemical Neuroscience (2020) 11:328−343.

  15. Arndt J.R., Chaibva M., Kondalaji S.G., Khakinejad M., Sarver O., Legleiter J., and Valentine S.J. Nucleation inhibition of Huntingtin protein (htt) by polyproline PPII helices: a potential interaction with the N-terminal α-helical region of htt. Biochemistry (2020) 59:436-449.

  16. Pilkington A.W. IV, Nyman M., Valentine S.J., and Legleiter J. Acetylation of Aβ40 alters aggregation in the presence and absence of lipid membranes. ACS Chemical Neuroscience (2020) 11:146-161.

  17. Karanji A.K., Beasley M., Sharif D., Ranjbaran A., Legleiter J., and Valentine S.J. Investigating the interactions of the first 17 amino acid residues of Huntingtin with lipid vesicles using mass spectrometry and molecular dynamics. J. Mass Spectrom. (2019) 1-13.

  18. Beasley M., Stonebraker A.R., Hasan I., Kapp K.L., Liang B.J., Agarwal G., Groover S., Sedighi F., and Legleiter J. Lipid Membranes Influence the Ability of Small Molecules To Inhibit Huntingtin Fibrillization. Biochemistry (2019) 58:4361-4373.

  19. Pilkington A.W. IV, Donohoe G.C., Akhmedov N.G>, Ferrebee T., Valentine S.J. and Legleiter J. Hydrogen Peroxide Modifies Aβ–Membrane Interactions with Implications for Aβ40 Aggregation. Biochemistry (2019) 58:2893-2905.

  20. Pilkington A.W. IV and Legleiter J. Challenges in understanding the structure/activity relationship of Aβ oligomers. AIMS Biophysics (2019) 6:1-22.

  21. Chaibva M., Gao X., Jain P., Campbell IV W.A., Frey S.L., and Legleiter J. Sphingomyelin and GM1 Influence Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes. ACS Omega (2018) 3:273-285.

  22. Kumar B., Miller K., Charon N.W., and Legleiter J. Periplasmic flagella in Borrelia burgdoferi function to maintain cellular integrity upon external stress. PLoS ONE (2017) 12:e0184648.

  23. Adegbuyiro A., Sedighi F., Pilkington IV A.W., Groover S., and Legleiter J. Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease. Biochemistry (2017) 56:1199-1217.

  24. Chaibva M., Jawahery S., Pilkington IV A.W., Arndt J.R., Sarver O., Valentine S., Matysiak S., and Legleiter J. Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding. Biophysical Journal (2016) 111:349-362.

  25. Shamitko-Klingensmith N., Boyd, J.W., and Legleiter J. Microtubule modification influences cellular response to amyloid-β exposure. AIMS Biophysics (2016) 3: 261-285.

  26. Gao X., Campbell IV W.A., Chaibva M., Jain P., Frey S.L., and Legleiter J.Cholesterol modifies huntingtin binding to, disruption of, and aggregation on lipid membranes. Biochemistry (2016) 55:92-102.

  27. Berger T.R., Montie H.L., Jain P., Legleiter J., Merry D.E. Identification of novel polyglutamine-expanded aggregation species in spinal and bulbar muscular atrophy. Brain Research (2015) 1628, Part B:254-264

  28. Arndt, J.R., Kondalaji, S.G., Maurer, M.M., Parker, A., Legleiter, J., and Valentine, S.J. Huntingtin N-terminal monomeric and multimeric structures destabilized by covalent modification of heteroatomic residues. Biochemistry (2015) 54:4285-4296.

  29. Arndt J.R., Chaibva M., and Legleiter J. The emerging role of the first 17 amino acids of huntingtin in Huntington’s disease. Biomolecular Concepts (2015) 6:33-46.

  30. Arndt J.R., Brown R.J., Burke K.A., Legleiter J., and Valentine S.J. Lysine Residues in the N-Terminal Huntingtin Amphipathic α-Helix Play a Key Role in Peptide Aggregation. Journal of Mass Spectrometry (2015) 50:117-126.

  31. Shakitko-Klingensmith N. and Legleiter J. Investigation of temperature induced mechanical changes in supported bilayers by variants of tapping mode atomic force microscopy. Scanning (2015) 37:23-35.

  32. Yates E.A. and Legleiter, J.Preparation protocols of Aβ(1-40) promote the formation of polymorphic aggregates and altered interactions with lipid bilayers. Biochemistry (2014) 53:7038-7050.

  33. Chaibva M., Burke K.A., and Legleiter J. Curvature Enhances Binding and Aggregation of Huntingtin at Lipid Membranes. Biochemistry (2014) 53:2355-2365.

  34. Burke K.A., Hensal K.M., Umbaugh C.S., Chaibva M., and Legleiter J., Huntingtin disrupts lipid bilayers in a polyQ-length dependent manner. Biochimica et Biophysica Acta (BBA) – Biomembranes. (2013) 1828:1953-1961..

  35. Burke K.A., Kauffman K.J., Umbaugh C.S., Frey S.L., and Legleiter J. The Interaction of Polyglutamine Peptides With Lipid Membranes is Regulated by Flanking Sequences Associated with Huntingtin. Journal of Biological Chemistry. (2013) 288:14993-15005.

  36. Yates E.A., Owens S.L., Lynch M.F., Cucco E.M., Umbaugh C.S., and Legleiter J.Specific domains of Aβ facilitate aggregation on and association with lipid bilayers.Journal of Molecular Biology. (2013) 425:1915-1933.

  37. Lotz, G.P. and Legleiter, J. The role of amyloidogenic protein oligomerization in neurodegenerative disease. Journal of Molecular Medicine (2013) 1-12.

  38. Burke, K.A., Yate, and Legleiter, J. Amyloid-forming proteins Alter the Local Mechanical Properties of Lipid Bilayers. Biochemistry (2013) 52:808-817.

  39. Burke, K.A., Yate, and Legleiter, J. Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration. Frontiers in Neurology (2013) 4:17.

  40. Shamitko-Klingensmith, N., Wambaugh, K. M., Burke, K. A., Magnone, G. J., and Legleiter, J.  Correlation of atomic force microscopy tapping forces to mechanical properties of lipid membranes, ASME Conference Proceedings (2012) DETC2012-70233.

  41. Shamitko-Klingensmith, N., Molchanoff, K. M., Burke, K. A., Magnone, G. J., and Legleiter, J.  Mapping the Mechanical Properties of Cholesterol-Containing Supported Lipid Bilayers with Nanoscale Spatial Resolution, Langmuir (2012) 28:13411-13422.

  42. Nucifora, L. G., Burke, K. A., Feng, X., Arbez, N., Zhu, S., Miller, J., Yang, G., Ratovitski, T., Delannoy, M., Muchowski, P. J., Finkbeiner, S., Legleiter, J., Ross, C. A., and Poirier, M. A. Identification of Novel Potentially Toxic Oligomers Formed in Vitro from Mammalian-derived Expanded huntingtin Exon-1 Protein, Journal of Biological Chemistry (2012) 287:16017-16028.

  43. Legleiter, J., Burke, K. A., and Yates, E. A.  Investigation of protein/lipid interactions via scanning probe acceleration microscopy: theory and experiment,ASME Conference Proceedings (2012) DETC2012-70228.

  44. Yates, E. A., Cucco, E. M., and Legleiter, J.  Point Mutations in Aβ Induce Polymorphic Aggregates at Liquid/Solid Interfaces, ACS Chemical Neuroscience (2011) 2:294-307.

  45. Pifer, P. M., Yates, E. A., and Legleiter, J.  Point Mutations in Aβ Result in the Formation of Distinct Polymorphic Aggregates in the Presence of Lipid Bilayers, PLoS One (2011) 6:e16248.

  46. Miller, J., Arrasate, M., Brooks, E., Libeu, C. P., Legleiter, J., Hatters, D., Curtis, J., Cheung, K., Krishnan, P., Mitra, S., Widjaja, K., Shaby, B. A., Lotz, G. P., Newhouse, Y., Mitchell, E. J., Osmand, A., Gray, M., Thulasiramin, V., Saudou, F., Segal, M., Yang, X. W., Masliah, E., Thompson, L. M., Muchowski, P. J., Weisgraber, K. H., and Finkbeiner, S. Identifying polyglutamine protein species in situ that best predict neurodegeneration, Nature Chemical Biology (2011) 7:925-934.

  47. Legleiter, J., Fryer, J. D., Holtzman, D. M., and Kowalewski, T. The Modulating Effect of Mechanical Changes in Lipid Bilayers Caused by ApoE-Containing Lipoproteins on Aβ Induced Membrane Disruption, ACS Chemical Neuroscience (2011) 2:588-599.

  48. Burke, K. A., Godbey, J., and Legleiter, J. Assessing mutant huntingtin fragment and polyglutamine aggregation by atomic force microscopy, Methods (2011) 53:275-284.

  49. Sathasivam, K., Lane, A., Legleiter, J., Warley, A., Woodman, B., Finkbeiner, S., Paganetti, P., Muchowski, P. J., Wilson, S., and Bates, G. P.  Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington’s disease, Human Molecular Genetics (2010) 19:65-78.

  50. Lotz, G. P., Legleiter, J., Aron, R., Mitchell, E. J., Huang, S.-Y., Ng, C., Glabe, C., Thompson, L. M., and Muchowski, P. J.  Hsp70 and Hsp40 Functionally Interact with Soluble Mutant Huntingtin Oligomers in a Classic ATP-dependent Reaction Cycle, Journal of Biological Chemistry (2010) 285:38183-38193.

  51. Legleiter, J., Mitchell, E., Lotz, G. P., Sapp, E., Ng, C., DiFiglia, M., Thompson, L. M., and Muchowski, P. J. Mutant Huntingtin Fragments Form Oligomers in a Polyglutamine Length-dependent Manner in Vitro and in Vivo, Journal of Biological Chemistry (2010) 285:14777-14790.

  52. Kumar, B., Pifer, P. M., Giovengo, A., and Legleiter, J. The effect of set point ratio and surface Young’s modulus on maximum tapping forces in fluid tapping mode atomic force microscopy, Journal of Applied Physics (2010) 107:044508.

  53. Abraham, A., Mihaliuk, E., Kumar, B., Legleiter, J., and Gullion, T.  Solid-State NMR Study of Cysteine on Gold Nanoparticles, Journal of Physical ChemistryC (2010) 114:18109-18114.

  54. Legleiter, J., Lotz, G. P., Miller, J., Ko, J., Ng, C., Williams, G. L., Finkbeiner, S., Patterson, P. H., and Muchowski, P. J.  Monoclonal Antibodies Recognize Distinct Conformational Epitopes Formed by Polyglutamine in a Mutant Huntingtin Fragment, Journal of Biological Chemistry (2009) 284:21647-21658.

  55. Legleiter, J. The effect of drive frequency and set point amplitude on tapping forces in atomic force microscopy: simulation and experiment, Nanotechnology (2009) 20:245703.

  56. Cheng, J. S., Dubal, D. B., Kim, D. H., Legleiter, J., Cheng, I. H., Yu, G.-Q., Tesseur, I., Wyss-Coray, T., Bonaldo, P., and Mucke, L. Collagen VI protects neurons against Aβ toxicity, Nature Neuroscience (2009) 12:119-121.

  57. Cheng, I. H., Scearce-Levie, K., Legleiter, J., Palop, J. J., Gerstein, H., Bien-Ly, N., Puolivali, J., Lesne, S., Ashe, K. H., Muchowski, P. J., and Mucke, L. Accelerating amyloid-β fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models, Journal of Biological Chemistry (2007) 282:23818-23828.

  58. Legleiter, J., Park, M., Cusick, B., and Kowalewski, T.  Scanning probe acceleration microscopy (SPAM) in fluids: Mapping mechanical properties of surfaces at the nanoscale, Proceedings of the National Academy of Sciences of the United States of America (2006) 103:4813-4818.

  59. Kowalewski, T., and Legleiter, J.  Imaging stability and average tip-sample force in tapping mode atomic force microscopy, Journal of Applied Physics (2006) 99:064903.

  60. Ehrnhoefer, D. E., Duennwald, M., Markovic, P., Wacker, J. L., Engemann, S., Roark, M., Legleiter, J., Marsh, J. L., Thompson, L. M., Lindquist, S., Muchowski, P. J., and Wanker, E. E.  Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington’s disease models, Human Molecular Genetics (2006)15:2743-2751.

  61. Legleiter, J., and Kowalewski, T. Insights into fluid tapping-mode atomic force microscopy provided by numerical simulations, Applied Physics Letters (2005) 87:163120-163123.

  62. Wahrle, S. E., Jiang, H., Parsadanian, M., Legleiter, J., Han, X. L., Fryer, J. D., Kowalewski, T., and Holtzman, D. M. ABCA1 is required for normal central nervous system ApoE levels and for lipidation of astrocyte-secreted apoE, Journal of Biological Chemistry (2004) 279:40987-40993.

  63. Legleiter, J., and Kowalewski, T. Tapping, pulling, probing: atomic force microscopy in drug discovery, Drug Discovery Today: Technologies (2004) 1:163-169.

  64. Legleiter, J., DeMattos, R. B., Holtzman, D. M., and Kowalewski, T.  In situAFM studies of astrocyte-secreted apolipoprotein E- and J-containing lipoproteins, Journal of Colloid and Interface Science (2004) 278:96-106.

  65. Legleiter, J., Czilli, D. L., Gitter, B., DeMattos, R. B., Holtzman, D. M., and Kowalewski, T.  Effect of different anti-Aβ antibodies on Aβ fibrillogenesis as assessed by atomic force microscopy, Journal of Molecular Biology (2004) 335:997-1006.

  66. Kowalewski, T., and Legleiter, J.  Improvement of Tapping Mode AFMImaging Stability by Operation Far Below Resonance Frequency of a Cantilever,ASME Conference Proceedings (2003) 595-597.

  67. Tristram-Nagle, S., Liu, Y. F., Legleiter, J., and Nagle, J. F.  Structure of gel phase DMPC determined by X-ray diffraction, Biophysical Journal (2002) 83:3324-3335.

 

Pre-Prints​

  1. Sedighi F., Skeens A., Adegbuyiro A., Bard J.*, Siriwardhana C., Donley E.*, Geldenhuys W.J., and Legleiter J. Oligomerization enhances huntingtin membrane activity but is suppressed by covalent crosslinking. bioRxiv (2023) 2023.03.01.530665.

  2. Siriwardhana C., Adegbuyiro A., Sedighi F., Stonebraker A.R., Groover S., Beasley M., Skeens A., Mertz B., Geldenhuys W., and Legleiter J. Blocking the ability of huntingtin to bind membranes: a therapeutic strategy for Huntington’s disease. bioRxiv (2024) 2024.07.17.603089.

​

Book Chapters

  1. Chaibva, M., Shamitko-Klingensmith, N., and Legleiter, J. “Recovering Time-Resolved Imaging Forces in solution by Scanning Probe Acceleration Microscopy: Theory and Application.” In Surface Science Characterization Techniques for Nanomaterials. Kumar, C., Ed. (2015) 69-89.

  2. Burke, K.A. and Legleiter, J. Atomic force microscopy assays for evaluating polyglutamine aggregation in solution and on surfaces. Methods in Molecular Biology (2013) 1017:21-40.

  3. Legleiter, J.  Assessing Aβ Aggregation State by Atomic Force Microscopy, In Alzheimer’s Disease and Frontotemporal Dementia: Methods and Protocols (Roberson, E. D., Ed.), (2011) pp 57-70.

  4. Legleiter, J. and T., K. (2006) Atomic Force Microscopy, In Part A: Protein Misfolding, Aggregation and Conformational Diseases (Uversky, V. N., and Fink, A. L., Eds.), pp 315-334, Kluwer Academic / Plenum Publishers, New York.

  5. Legleiter, J. and Kowalewski, T. (2004) Atomic force microscopy of β-amyloid: static and dynamic studies of nanostructure and its formation, Methods in molecular biology (Clifton, N.J.) 242, 349-364.

bottom of page