The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry
Abstract
Abstract: Paired helical filaments (PHFs) are the structural constituents of neurofibrillary tangles in Alzheimer's disease and are composed of hyperphosphorylated forms of the microtubule‐associated protein tau (PHF‐tau). Pathological hyperphosphorylation of tau is believed to be an important contributor to the destabilisation of microtubules and their subsequent disappearance from tangle‐bearing neurons in Alzheimer's disease, making elucidation of the mechanisms that regulate tau phosphorylation an important research goal. Thus, it is essential to identify, preferably by direct sequencing, all of the sites in PHF‐tau that are phosphorylated, a task that is incomplete because of the difficulty to date of purifying insoluble PHF‐tau to homogeneity and in sufficient quantities for structural analysis. Here we describe the solubilisation of PHF‐tau followed by its purification by Mono Q chromatography and reversed‐phase HPLC. Phosphopeptides from proteolytically digested PHF‐tau were sequenced by nanoelectrospray mass spectrometry. We identified 22 phosphorylation sites in PHF‐tau, including five sites not previously identified. The combination of our new data with previous reports shows that PHF‐tau can be phosphorylated on at least 25 different sites.
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Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965
Self-citationJin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., & Selkoe, D. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017033108 · Cited by 876
Tau and neurodegenerative disease: the story so far
Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806
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Metadata
- Authors
- Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1998-12
- Volume
- 71
- Issue
- 6
- Pages
- 2465-2476
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2006520473
- Cited by
- 377
- References
- 63
- FWCI
- 7.63
- Type
- journal article
- Language
- en
- Open access
- closed
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- The paper
- Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H. (1998). New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.1998.71062465.x
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