The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
Abstract
The microtubule‐associated protein τ is hyperphosphorylated in the paired helical filaments (PHFs) of Alzheimer's disease. Immunological and direct chemical studies have identified Ser 396 and Ser 404 as two of the phosphorylated sites. Previously, we have demonstrated, using synthetic τ peptides containing phosphorylated Ser 396 , that this site is recognized by the monoclonal antibody PHF‐1. The present sudy extends this observation by showing that PHF‐1 recognizes τ peptides containing either individually phosphorylated Ser 396 or Ser 404 , but that there is a >10‐fold increase in the sensitivity of detection of τ peptides by PHF‐1 when both serines are phosphorylated. The recognition of singly or doubly phosphorylated Ser 396 and Ser 404 in τ by PHF‐1 can also be demonstrated in Chinese hamster ovary cells transfected with full‐length wild‐type τ constructs or mutant constructs with Ala substituted for Ser 396 or Ser 404 . We conclude that the PHF‐1 epitope contains both phosphorylated Ser 396 and Ser 404 . © 1994 Wiley‐Liss, Inc.
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“…la Recherche Médicale U422, Lille, France) and PHF1 (a kind gift from Dr. P. Davies) recognize human and murine tau phosphorylated at S396 and S404 (Otvos et al., 1994; Buée-Scherrer et al., 1996); PG5 (a kind gift from Dr. P. Davies) recognizes human and murine tau phosphorylated at S409…”
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Metadata
- Authors
- Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., & Lee, V. M.
- Affiliations
- The Wistar Institute (US)
- University of Pennsylvania (US)
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Otvos, L.
- ORCID
- Venue
- Journal of Neuroscience Research
- Publisher
- Wiley
- Published
- 1994-12-15
- Volume
- 39
- Issue
- 6
- Pages
- 669-673
- ISSN
- 0360-4012 (ISSN-L)
- 1097-4547
- OpenAlex
- W1984482388
- Semantic Scholar
- 4518f282e57a4d29fb281b9a658ed49720534f5d
- Cited by
- 488
- References
- 21
- Citations by year
- 2026: 14 · 2025: 27 · 2024: 14 · 2023: 11 · 2022: 13 · 2021: 11 · 2020: 13 · 2019: 13 · 2018: 6 · 2017: 13 · 2016: 16 · 2015: 12 · 2014: 7 · 2013: 24 · 2012: 23
- FWCI
- 7.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neuroscience Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag010670-02, 5p01ag009215-20)
- National Institute on Aging (AG09215, AG 10670)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tau hyperphosphorylation, paired helical filaments, Alzheimer's disease, epitope mapping, CHO cells
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Epitopes, Enzyme-Linked Immunosorbent Assay, Cricetinae, Humans, Molecular Sequence Data, Peptides, Phosphorylation, Serine, Blotting, Western, CHO Cells, tau Proteins, DNA, Complementary
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