CoChat
Sign Up
Cited by 765

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding

Danzer, Karin M., Haasen, Dorothea, Karow, Anne R., Moussaud, Simon, Habeck, Matthias, Giese, Armin, Kretzschmar, Hans, Hengerer, Bastian, Kostka, Marcus·2007·The Journal of Neuroscience
DOI 10.1523/jneurosci.2617-07.2007
Open this paper in CoChat — free account

Abstract

Aggregation of α-synuclein (α-syn) has been linked to the pathogenesis of Parkinson's disease (PD) and other neurodegenerative diseases. Increasing evidence suggests that prefibrillar oligomers and protofibrils, rather than mature fibrils of α-syn, are the pathogenic species in PD. Despite extensive effort on studying oligomerization of α-syn, no studies have compared different oligomer species directly on a single-particle level and investigated their biological effects on cells. In this study, we applied a novel highly sensitive single molecule detection system that allowed a direct comparison of different oligomer types. Furthermore, we studied biological effects of different oligomer types on cells. For this purpose, we developed new oligomerization protocols, that enabled the use of these different oligomers in cell culture. We found that all of our three aggregation protocols resulted in heterogeneous populations of oligomers. Some types of oligomers induced cell death via disruption of cellular ion homeostasis by a presumably pore-forming mechanism. Other oligomer types could directly enter the cell resulting in increased α-syn aggregation. Based on our results, we propose that under various physiological conditions, heterogeneous populations of oligomeric forms will coexist in an equilibrium. These different oligomer types lead directly or indirectly to cell damage. Our data indicate that inhibition of early α-syn aggregation events would consequently prevent all α-syn oligomer related toxicities. This has important implications for the development of disease-modifying drugs for the treatment of PD and other synucleinopathies.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1523/jneurosci.2617-07.2007

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Oligomeric α-Syn species appear prone to uptake and spread from cell-to-cell in a prion-like manner, leading to templated misfolding of native α-Syn and formation of aggregates throughout the brain.

    “Particularly, the oligomeric α-Syn species appear to be prone to uptake and spread from cell-to-cell in a prion-like manner, leading to the templated misfolding of the native forms of α-Syn and formation of α-Syn aggregates throughout the brain, which are the defining pathological features of Parkinson’s disease (PD) and dementia with Lewy body (DLB) [12–19].”

    From LRP1 is a neuronal receptor for α-synuclein uptake and spread (2022) · cites this paper as [15]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 55

  1. 10.1097/WNR.0b013e3280115185 · DOI
  2. 10.1111/j.1471-4159.2006.03731.x · DOI · Paper page
  3. 10.1016/j.jmb.2005.10.071 · DOI
  4. 10.1007/s00232-003-0638-7 · DOI
  5. Avdulov, 1997, Lipid binding to amyloid β-peptide aggregates: preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids, J Neurochem, 69, 1746, 10.1046/j.1471-4159.1997.69041746.x · DOI
  6. 10.1073/pnas.0511256103 · DOI
  7. 10.1016/S0197-4580(02)00065-9 · DOI · Paper page
  8. 10.1074/jbc.M400348200 · DOI
  9. 10.1016/S0140-6736(04)17103-1 · DOI · Paper page
  10. 10.1073/pnas.97.2.571 · DOI
  11. 10.1016/S0896-6273(03)00568-3 · DOI · Paper page
  12. 10.1074/jbc.M500997200 · DOI
  13. 10.1096/fj.03-1449com · DOI · Paper page
  14. 10.1111/j.1471-4159.2006.03803.x · DOI
  15. 10.1038/35081564 · DOI
  16. 10.1038/35017124 · DOI
  17. 10.1074/jbc.M208194200 · DOI
  18. 10.1016/j.jmb.2004.07.052 · DOI
  19. 10.2174/138620706775213921 · DOI
  20. 10.1016/S0022-2836(02)00775-1 · DOI
  21. 10.1016/j.jmb.2004.04.051 · DOI
  22. 10.1074/jbc.M000099200 · DOI
  23. 10.1073/pnas.96.24.13756 · DOI
  24. Kask, 2000, Two-dimensional fluorescence intensity distribution analysis: theory and applications, Biophys J, 78, 1703, 10.1016/S0006-3495(00)76722-1 · DOI
  25. 10.1074/jbc.275.19.14077 · DOI
  26. 10.1016/S0076-6879(06)13017-7 · DOI
  27. 10.1074/jbc.C400260200 · DOI
  28. 10.1038/ng0298-106 · DOI · Paper page
  29. Lashuel, 2005, In vitro preparation of prefibrillar intermediates of amyloid-β and α-synuclein, Methods Mol Biol, 299, 19
  30. 10.1017/S0033583506004422 · DOI
  31. Lashuel, 2002, Neurodegenerative disease: amyloid pores from pathogenic mutations, Nature, 418, 291, 10.1038/418291a · DOI
  32. 10.1016/S0022-2836(02)00735-0 · DOI
  33. 10.1074/jbc.M107045200 · DOI
  34. 10.1523/JNEUROSCI.0692-05.2005 · DOI
  35. 10.1016/j.bbrc.2005.02.094 · DOI
  36. 10.1126/science.287.5456.1265 · DOI
  37. 10.1111/j.1749-6632.1996.tb34447.x · DOI
  38. 10.1385/JMN:17:2:205 · DOI
  39. 10.1016/0006-8993(94)01463-R · DOI
  40. 10.1074/jbc.M401076200 · DOI
  41. 10.1038/71247 · DOI
  42. 10.1021/bi020604a · DOI
  43. Pountney, 2005, Annular α-synuclein oligomers are potentially toxic agents in α-synucleinopathy Hypothesis, Neurotox Res, 7, 59, 10.1007/BF03033776 · DOI
  44. 10.1021/bi001315u · DOI
  45. 10.1126/science.1090278 · DOI · Paper page
  46. 10.1111/j.1742-4658.2007.05733.x · DOI
  47. 10.1074/jbc.M105343200 · DOI · Paper page
  48. 10.1021/bi971075r · DOI
  49. 10.1021/bi0121353 · DOI
  50. 10.1021/bi0102398 · DOI
  51. 10.1016/S0092-8674(00)81564-0 · DOI
  52. 10.2174/138620706777452447 · DOI
  53. 10.1074/jbc.274.28.19509 · DOI
  54. 10.1002/ana.10795 · DOI · Paper page
  55. 10.1021/bi035901+ · DOI

Cited by

Sorted by citations

Metadata

Authors
Danzer, K. M., Haasen, D., Karow, A. R., Moussaud, S., Habeck, M., Giese, A., Kretzschmar, H., Hengerer, B., & Kostka, M.
Venue
The Journal of Neuroscience
Publisher
Society for Neuroscience
Published
2007-08-22
Volume
27
Issue
34
Pages
9220-9232
ISSN
  • 0270-6474
  • 1529-2401
DOI
10.1523/jneurosci.2617-07.2007
Cited by
765
References
4
Language
en
Licence
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 184 d)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review