| Year |
Citation |
Score |
| 2024 |
de Boni L, Wallis A, Hays Watson A, Ruiz-Riquelme A, Leyland LA, Bourinaris T, Hannaway N, Wüllner U, Peters O, Priller J, Falkenburger BH, Wiltfang J, Bähr M, Zerr I, Bürger K, ... ... Bartels T, et al. Aggregation-resistant alpha-synuclein tetramers are reduced in the blood of Parkinson's patients. Embo Molecular Medicine. PMID 38839930 DOI: 10.1038/s44321-024-00083-5 |
0.419 |
|
| 2023 |
Fazzari M, Di Biase E, Zaccagnini L, Henriques A, Callizot N, Ciampa MG, Mauri L, Carsana EV, Loberto N, Aureli M, Mari L, Civera M, Vasile F, Sonnino S, Bartels T, et al. GM1 oligosaccharide efficacy against α-synuclein aggregation and toxicity in vitro. Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids. 159350. PMID 37330108 DOI: 10.1016/j.bbalip.2023.159350 |
0.46 |
|
| 2023 |
Ramalingam N, Jin SX, Moors TE, Fonseca-Ornelas L, Shimanaka K, Lei S, Cam HP, Watson AH, Brontesi L, Ding L, Hacibaloglu DY, Jiang H, Choi SJ, Kanter E, Liu L, ... Bartels T, et al. Dynamic physiological α-synuclein S129 phosphorylation is driven by neuronal activity. Npj Parkinson's Disease. 9: 4. PMID 36646701 DOI: 10.1038/s41531-023-00444-w |
0.724 |
|
| 2022 |
de Boni L, Watson AH, Zaccagnini L, Wallis A, Zhelcheska K, Kim N, Sanderson J, Jiang H, Martin E, Cantlon A, Rovere M, Liu L, Sylvester M, Lashley T, Dettmer U, ... ... Bartels T, et al. Brain region-specific susceptibility of Lewy body pathology in synucleinopathies is governed by α-synuclein conformations. Acta Neuropathologica. PMID 35141810 DOI: 10.1007/s00401-022-02406-7 |
0.749 |
|
| 2021 |
Román-Vendrell C, Medeiros AT, Sanderson JB, Jiang H, Bartels T, Morgan JR. Effects of Excess Brain-Derived Human α-Synuclein on Synaptic Vesicle Trafficking. Frontiers in Neuroscience. 15: 639414. PMID 33613189 DOI: 10.3389/fnins.2021.639414 |
0.394 |
|
| 2020 |
Bartels T, De Schepper S, Hong S. Microglia modulate neurodegeneration in Alzheimer's and Parkinson's diseases. Science (New York, N.Y.). 370: 66-69. PMID 33004513 DOI: 10.1126/science.abb8587 |
0.56 |
|
| 2020 |
Sanderson JB, De S, Jiang H, Rovere M, Jin M, Zaccagnini L, Hays Watson A, De Boni L, Lagomarsino VN, Young-Pearse TL, Liu X, Pochapsky TC, Hyman BT, Dickson DW, Klenerman D, ... ... Bartels T, et al. Analysis of α-synuclein species enriched from cerebral cortex of humans with sporadic dementia with Lewy bodies. Brain Communications. 2: fcaa010. PMID 32280944 DOI: 10.1093/braincomms/fcaa010 |
0.722 |
|
| 2019 |
Rovere M, Powers AE, Jiang H, Pitino JC, Fonseca-Ornelas L, Patel DS, Achille A, Langen R, Varkey J, Bartels T. E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity. The Journal of Biological Chemistry. PMID 31048377 DOI: 10.1074/Jbc.Ra118.006551 |
0.411 |
|
| 2018 |
Rovere M, Sanderson JB, Fonseca-Ornelas L, Patel DS, Bartels T. Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces. Febs Letters. PMID 29633780 DOI: 10.1002/1873-3468.13047 |
0.35 |
|
| 2017 |
Schapansky J, Khasnavis S, DeAndrade MP, Nardozzi JD, Falkson SR, Boyd JD, Sanderson JB, Bartels T, Melrose HL, LaVoie MJ. Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons. Neurobiology of Disease. PMID 29246723 DOI: 10.1016/J.Nbd.2017.12.005 |
0.715 |
|
| 2017 |
Dettmer U, Ramalingam N, von Saucken VE, Kim TE, Newman AJ, Terry-Kantor E, Nuber S, Ericsson M, Fanning S, Bartels T, Lindquist S, Levy OA, Selkoe D. Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells. Human Molecular Genetics. 26: 3466-3481. PMID 28911198 DOI: 10.1093/hmg/ddx227 |
0.722 |
|
| 2017 |
Mittal S, Bjørnevik K, Im DS, Flierl A, Dong X, Locascio JJ, Abo KM, Long E, Jin M, Xu B, Xiang YK, Rochet JC, Engeland A, Rizzu P, Heutink P, ... Bartels T, et al. β2-Adrenoreceptor is a regulator of the α-synuclein gene driving risk of Parkinson's disease. Science (New York, N.Y.). 357: 891-898. PMID 28860381 DOI: 10.1126/Science.Aaf3934 |
0.53 |
|
| 2016 |
Bartels T. Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease. Jama Neurology. PMID 27918751 DOI: 10.1001/jamaneurol.2016.4813 |
0.357 |
|
| 2015 |
Dettmer U, Selkoe D, Bartels T. New insights into cellular α-synuclein homeostasis in health and disease. Current Opinion in Neurobiology. 36: 15-22. PMID 26282834 DOI: 10.1016/j.conb.2015.07.007 |
0.739 |
|
| 2015 |
Dettmer U, Newman AJ, Soldner F, Luth ES, Kim NC, von Saucken VE, Sanderson JB, Jaenisch R, Bartels T, Selkoe D. Corrigendum: Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation. Nature Communications. 6: 8008. PMID 26224447 DOI: 10.1038/ncomms9008 |
0.724 |
|
| 2015 |
Dettmer U, Newman AJ, von Saucken VE, Bartels T, Selkoe D. KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity. Proceedings of the National Academy of Sciences of the United States of America. 112: 9596-601. PMID 26153422 DOI: 10.1073/pnas.1505953112 |
0.758 |
|
| 2015 |
Dettmer U, Newman AJ, Soldner F, Luth ES, Kim NC, von Saucken VE, Sanderson JB, Jaenisch R, Bartels T, Selkoe D. Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation. Nature Communications. 6: 7314. PMID 26076669 DOI: 10.1038/Ncomms8314 |
0.733 |
|
| 2015 |
Dettmer U, Bartels T. ExPLAining early synucleinopathies. Brain : a Journal of Neurology. 138: 1449-51. PMID 26013805 DOI: 10.1093/brain/awv099 |
0.577 |
|
| 2015 |
Luth ES, Bartels T, Dettmer U, Kim NC, Selkoe DJ. Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity. Biochemistry. 54: 279-92. PMID 25490121 DOI: 10.1021/bi501188a |
0.661 |
|
| 2014 |
Bartels T, Kim NC, Luth ES, Selkoe DJ. N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation. Plos One. 9: e103727. PMID 25075858 DOI: 10.1371/journal.pone.0103727 |
0.506 |
|
| 2014 |
Luth ES, Stavrovskaya IG, Bartels T, Kristal BS, Selkoe DJ. Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction. The Journal of Biological Chemistry. 289: 21490-507. PMID 24942732 DOI: 10.1074/jbc.M113.545749 |
0.425 |
|
| 2014 |
Hong S, Ostaszewski BL, Yang T, O'Malley TT, Jin M, Yanagisawa K, Li S, Bartels T, Selkoe DJ. Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes. Neuron. 82: 308-19. PMID 24685176 DOI: 10.1016/J.Neuron.2014.02.027 |
0.614 |
|
| 2014 |
Selkoe D, Dettmer U, Luth E, Kim N, Newman A, Bartels T. Defining the native state of α-synuclein Neurodegenerative Diseases. 13: 114-117. PMID 24192542 DOI: 10.1159/000355516 |
0.738 |
|
| 2013 |
Dettmer U, Newman AJ, Luth ES, 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: 6371-85. PMID 23319586 DOI: 10.1074/jbc.M112.403311 |
0.708 |
|
| 2011 |
Bartels T, Choi JG, Selkoe DJ. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature. 477: 107-10. PMID 21841800 DOI: 10.1038/nature10324 |
0.598 |
|
| 2010 |
Bartels T, Ahlstrom LS, Leftin A, Kamp F, Haass C, Brown MF, Beyer K. The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding. Biophysical Journal. 99: 2116-24. PMID 20923645 DOI: 10.1016/J.Bpj.2010.06.035 |
0.497 |
|
| 2010 |
Kamp F, Exner N, Lutz AK, Wender N, Hegermann J, Brunner B, Nuscher B, Bartels T, Giese A, Beyer K, Eimer S, Winklhofer KF, Haass C. Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1. The Embo Journal. 29: 3571-89. PMID 20842103 DOI: 10.1038/Emboj.2010.223 |
0.48 |
|
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