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Cited by 52

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Molecular aging of tau: disulfide‐independent aggregation and non‐enzymatic degradation in vitro and in vivo

Watanabe, Atsushi, Hong, Won‐Kyoung, Dohmae, Naoshi, Takio, Koji, Morishima‐Kawashima, Maho, Ihara, Yasuo·2004·Journal of Neurochemistry
DOI 10.1111/j.1471-4159.2004.02611.x
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Abstract

Smearing from high‐molecular‐mass regions to low‐molecular‐mass regions on western blot is the most striking observation of the tau making up paired helical filaments in brain tissues affected by Alzheimer's disease. Because our previous study showed site‐specific deamidation/isomerization in the smeared tau in vivo, a feature of protein aging, recombinant tau was subjected to prolonged (up to 90 days) in vitro incubation. Carboxymethylated tau at ∼50 kDa gradually disappeared and was converted to dimers and to high‐ and low‐molecular‐mass smearing. In addition, the same site‐specific deamidation/isomerization as previously identified in the smeared tau in vivo emerged. Most importantly, tau was spontaneously degraded, generating fragments that start from bulky residues next to asparaginyl residues. This spontaneous degradation of tau probably represents non‐enzymatic cleavage through the formation of succinimide intermediates. Similar degradation products starting from the bulky residues next to asparaginyl residues were found in the smeared tau in vivo partially purified from the homogenates from Alzheimer's disease brains.

Overview

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Crossref · 10.1111/j.1471-4159.2004.02611.x

Cites

7 of 7 references verified0 citation errors · 0 not checkable

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Citations

Cites

Show all 7 references

Research works printed but not linked: 23

  1. 10.1002/ana.410380414 · DOI
  2. Aswad D. W., 1995, Deamidation and Isoaspartate Formation in Peptides and Proteins, 1
  3. 10.1016/0076-6879(77)47016-2 · DOI
  4. 10.1021/bi980537d · DOI · Paper page
  5. 10.1016/S0021-9258(19)75855-4 · DOI
  6. 10.1016/0896-6273(89)90210-9 · DOI · Paper page
  7. 10.1073/pnas.87.15.5827 · DOI
  8. 10.1016/S0014-5793(98)01217-4 · DOI
  9. 10.1038/304727a0 · DOI
  10. 10.1016/S0304-3940(99)00476-0 · DOI
  11. 10.1002/j.1460-2075.1991.tb07820.x · DOI
  12. 10.1016/S0014-5793(96)01386-5 · DOI · Paper page
  13. 10.1016/0896-6273(88)90129-8 · DOI
  14. 10.1093/jnen/60.9.872 · DOI
  15. 10.1016/0304-3940(95)11291-4 · DOI
  16. 10.1074/jbc.270.2.823 · DOI · Paper page
  17. 10.1046/j.1471-4159.1996.67031183.x · DOI · Paper page
  18. 10.1073/pnas.92.18.8463 · DOI · Paper page
  19. 10.1016/S0021-9258(18)37383-6 · DOI
  20. 10.1074/jbc.274.11.7368 · DOI
  21. 10.1083/jcb.118.3.573 · DOI · Paper page
  22. 10.1074/jbc.270.41.24306 · DOI
  23. 10.1073/pnas.85.12.4506 · DOI · Paper page

Cited by

Metadata

Authors
Watanabe, A., Hong, W., Dohmae, N., Takio, K., Morishima‐Kawashima, M., & Ihara, Y.
Venue
Journal of Neurochemistry
Publisher
Wiley
Published
2004-08-16
Volume
90
Issue
6
Pages
1302-1311
ISSN
  • 0022-3042
  • 1471-4159
DOI
10.1111/j.1471-4159.2004.02611.x
Cited by
52
References
7
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.