Publications

  1. Rovere, M., Powers, A. E., Patel, D. S., & Bartels, T. pTSara-NatB, an improved N-terminal acetylation system for recombinant protein expression in E. coli. PloS One, 13(7), e0198715. (2018).
  2. Rovere, M., Sanderson, J. B., Fonseca-Ornelas, L., Patel, D. S., & Bartels, T. Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces. FEBS Letters, 592(9), 1464–1472. (2018)
  3. Schapansky, J., Khasnavis, S., DeAndrade, M. P., Nardozzi, J. D., Falkson, S. R., Boyd, J. D., Sanderson, J., Bartels, T., Melrose, H., LaVoie, M. Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons. Neurobiol Dis, 111, 26–35. (2018)
  4. Dettmer, U., Ramalingam, N., von Saucken, V., Kim, T., Newman, A., Terry-Kantor, E., Nuber, S., Ericsson, M., Fanning, S., Bartels, T., Lindquist, S., Levy, O., Selkoe, D. Loss of native a-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells. HMG, 26, 3466–3481 (2017).
  5. Mittal, S., Bjornevik, K., Im, D., Flierl, A., Dong, X., Locascio, J., About, K., Long, E., Jin, M., Bing, X., Xiang, Y., Rochet, J., England, A., Rizzu, P., Heutnink, H., Bartels, T., Selkoe, D., Calderone, B., Glicksman, M., Khurana, V., Schüle, B., Park, D., Riise, T., Scherzer, C. b2-Adrenoreceptor is a regulator of the a-synuclein gene driving risk of Parkinson’s disease. Science 357, 891–898 (2017).
  6. Bartels, T. Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease. JAMA Neurol., (2016).
  7. Dettmer, U., Selkoe, D. & Bartels, T. New insights into cellular α-synuclein homeostasis in health and disease. Curr. Opin. Neurobiol. 36, 15–22 (2015).
  8. Bartels, T. Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease. JAMA Neurol., (2016).
  9. Dettmer, U., Selkoe, D. & Bartels, T. New insights into cellular α-synuclein homeostasis in health and disease. Curr. Opin. Neurobiol. 36, 15–22 (2015).
  10. Dettmer, U., Newman, A. J., Saucken, von, V. E., Bartels, T. & Selkoe, D. KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity. PNAS 112, 9596–9601 (2015).
  11. Luth, E. S., Bartels, T., Dettmer, U., Kim, N. C. & Selkoe, D. J. Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity. Biochemistry 54, 279–292 (2015).
  12. Dettmer, U. , Newman, A. J., Soldner, F. Luth, E., Kim, N. Saucken, von, V. E., Sanderson, J., Jaenisch, R., Bartels, T. & Selkoe, D. Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation. Nat Commun 6, 7314 (2015).
  13. Luth, E. S., Stavrovskaya, I. G., Bartels, T., Kristal, B. S. & Selkoe, D. J. Soluble, Prefibrillar α-Synuclein Oligomers Promote Complex I-dependent, Ca2+-induced Mitochondrial Dysfunction. The Journal of biological chemistry 289, 21490–21507 (2014).
  14. Hong, S., Ostaszewski, B., Yang, T. O’Malley, T., Jin, M., Yanagisawa, K., Li, S., Bartels, T. & Selkoe, D. Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes. Neuron 82, 308–319 (2014).
  15. Bartels, T., Kim, N. C., Luth, E. S. & Selkoe, D. J. N-Alpha-Acetylation of α-Synuclein Increases Its Helical Folding Propensity, GM1 Binding Specificity and Resistance to Aggregation. PLoS ONE 9, e103727 (2014).
  16. Selkoe, D. Dettmer, U., Luth, E., Kim, N., Newman, A., Bartels, T. Defining the native state of α-synuclein. Neurodegener Dis 13, 114–117 (2014).
  17. Dettmer, U., Newman, A. J., Luth, E. S., Bartels, T. & Selkoe, D. In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells. The Journal of biological chemistry 288, 6371–6385 (2013).
  18. Bartels, T., Choi, J. G. & Selkoe, D. J. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477, 107–110 (2011).
  19. Kamp, F., Exner, N., Lutz, A., Wender, N., Degerman, J., Brunner, B.,Nuscher, B., Bartels, T., Giese, A., Beyer, K., Eimer, S., Winklhofer, K., Haass, C. Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1. EMBO J. 29, 3571–3589 (2010).
  20. Bartels, T. et al. The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding. Biophysical journal 99, 2116–2124 (2010).
  21. Bartels, T., Lankalapalli, R. S., Bittman, R., Beyer, K. & Brown, M. F. Raftlike mixtures of sphingomyelin and cholesterol investigated by solid-state 2H NMR spectroscopy. Journal of the American Chemical Society 130, 14521–14532 (2008).
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