Cited by 488Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404

Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., Lee, V. M‐Y.·1994·Journal of Neuroscience Research

DOI 10.1002/jnr.490390607

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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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“[91] Otvos L, Feiner L, Lang E, Szendrei GI, Goedert M, Lee VM.”
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“…a single CHI was assessed using the pTau antibodies S214, PHF1 and AT8, which recognize unique tau phosphorylation sites (Goedert et al., 1995; Otvos et al., 1994; Yu et al., 2009) S214+, PHF1+ and AT8+ cell density was assessed in ipsilesional and contralesional cortex, corpus callosum and…”
Method
Nanoskalauntersuchungen vom zellulären Metabolismus mittels Sekundärionen-Massenspektrometrie
Karsten, L. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9484
Tau load in select brainstem neurons predicts the severity and nature of balance deficits in the absence of cell deathPreprint
Zhu, Y., Gelnaw, H., Leary, P., Raghuraman, R., Kamath, N., Kraja, A., Liu, J., Bai, Q., Higashijima, S., Burton, E. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.14.618073
Differential Effects on In Vitro Tau Aggregation Due to 7, 11, and 14 Pseudophosphorylated Sites
Prasad, V., & Gamblin, T. C. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00358
Brain large artery dilatation increases the risk for Alzheimer’s disease pathologyPreprint
Simpson, D., Morrone, C. D., Wear, D., Khani, A., Liu, F., Gutierrez, J., & Yu, W. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.29.672901
“Finally, we saw no increase in the hyperphosphorylation of tau after elastase injection using the PHF1 antibody that recognizes tau protein phosphorylation at Ser396 and Ser404 residues (Otvos et al., 1994).”
Additional file 1 of Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology
Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Figshare · doi:10.6084/m9.figshare.20176025
Additional file 1 of Downstream effects of polypathology on neurodegeneration of medial temporal lobe subregions
Wisse, L. E. M., Ravikumar, S., Ittyerah, R., Lim, S., Lane, J., Bedard, M. L., Xie, L., Das, S. R., Schuck, T., Grossman, M., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15033187
PICALM Genetic Variant Alters mRNA Expression Without Affecting Protein Levels or Tau Spreading in Alzheimer’s Disease
Ando, K., Lopez‐Gutierrez, L., Mansour, S., Yilmaz, Z., Dauphinot, L., Verheijen, J., Fontaine, G., Quintanilla‐Sánchez, C., Aydin, E., Doeraene, E., et al. (2026) · Cells · doi:10.3390/cells15030235
“Mouse monoclonal PHF1 antibody was provided by Dr. Peter Davies and recognizes pSer396/404 of tau [67].”
Timing matters: early administration of a high-affinity antibody targeting the tau repeat domain prevents aggregation in a mouse tauopathy model
Penny, L. K., Arastoo, M., Lofthouse, R. A., Abdallah, A., Imoesi, P. I., Schwab, K., Shiells, H., Melis, V., Riedel, G., Harrington, C. R., et al. (2026) · Alzheimer s Research & Therapy · doi:10.1186/s13195-026-01985-x
“Two well established examples being p396 [38] and p202/205 [39] which are archetypal of disease-relevant tau.”
Neurovascular large artery dilatation increases the risk for Alzheimer's disease pathology
Simpson, D., Morrone, C. D., Wear, D., Khani, A., Liu, F., Gutierrez, J., & Yu, W. H. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107368
Expanding landscape of tau pathology in neurological disorders: A narrative review guiding diagnostic development and targeted therapeutics
Yakubu, A. O., Atafo, G. I., Nwaze, C. E., Bakare, T. Y., Adeniyi, T. O., Alare, K., Oladele, A. B., & Solagbade, O. S. (2026) · NeuroMarkers. · doi:10.1016/j.neumar.2026.100167 · Cited by 1
Identification et caractérisation fonctionnelle de nouveaux sites de clivage de la protéine Tau
Derisbourg, M. J. (2015) · theses.fr (ABES) · doi:10.70675/ef5f45b0zf4e8z433fz9beaz8d2cc6de65bc
Propagation axonale des pathologies Tau et Aβ dans la maladie d'Alzheimer : à la recherche de propagons dans le circuit subiculo-fornico-mamillaire
Thierry, M. (2020) · theses.fr (ABES) · doi:10.70675/d2f36d94zaa16z4617z94c6zabb1ad26f3fb
Phosphorylation of S396 and S400 Promotes Tau Self-Assembly and Favors the Chronic Traumatic Encephalopathy (CTE) Protofilament FoldPreprint
Powell, W. C., Yan, N., Tse, E., Melo, A. A., Sin, N., Southworth, D. R., & Gestwicki, J. E. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.19.726321
Stable neuronal representations underlie cognitive resilience to Alzheimer's disease pathology
Chen, K.-Y., Pineau, E., Koletar, M., Trevisiol, A., He, J. S., Hill, M. E., Goubran, M., Sled, J. G., Mclaurin, J., & Stefanovic, B. (2026) · Alzheimer's & Dementia · doi:10.1002/alz.71570 · Cited by 2
Robust tauopathy and memory deficits in a mouse model constitutively overexpressing human P301L MAPT
Hamm, M. J., McNaught, K., Janus, C., Gazarov, E. A., Strickland, Z., Shubin, J., Reinhardt, J., Park, J., Rayaprolu, S., Antropov, W. V., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107496
Investigating the role of EFhd2 protein in modulating tau pathology in a tauopathy mouse model
Soliman, A. S., Umstead, A., & Vega, I. E. (2026) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2026.1833887
“…2% goat serum/0.1% Triton-X/TBS: pSer422 (1:2K; Abcam cat. no. ab79415, RRID:AB_1603345), Alz50 (1:2K, RRID:AB_2313937), and PHF1(1:500, RRID:AB_2315150) (Wolozin et al., 1986; Ksiezak-Reding et al., 1988, 1995; Goedert et al., 1991; Greenberg et al., 1992; Otvos et al., 1994; Carmel et al., 1996).”
Influential
The truncated Tau fragment 315–441 produced by Caspase-2 translocates to the nucleus and alters the proteome of neuroblastoma cells
López-Aviña, Y. I., Ríos‐Castro, E., Rodríguez‐Cruz, F., Mendoza-Franco, G., Vega, B. C., Boucard, A. A., Luna‐Arias, J. P., Basurto‐Islas, G., & García‐Sierra, F. (2026) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2026.151567
Effect of tau silencing on tau pathology propagation, a treatment efficient at the earliest stages of the disease?
Kosa, A., Lopez‐Gutierrez, L., Ando, K., Doeraene, E., Aydin, E., Lasri, H., Wathelet‐Depauw, A., Pieters, K., Morckhoven, D. V., Dubois, C., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107598
Safe and efficient intracellular delivery of functional antibodies into cultured neural cells shows a role for Alzheimer’s-relevant tau phosphorylation in cell integrity
Viola, K. L., Chromy, B. A., Nowar, R., Lambert, M. P., & Klein William, L. (2026) · Frontiers in Dementia · doi:10.3389/frdem.2026.1737082
“Phosphorylation of tau at Ser396 and Ser404 is a prominent feature of paired helical filaments and neurofibrillary tangles and is commonly regarded as a marker of pathological tau accumulation (Greenberg, 1990; Otvos Jr et al., 1994; Hefti et al., 2019).”
Untitled work
Duong (2000) · doi:10.1002/1097-0169(200011)47:3

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: Otvos, L.
Goedert, M.
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
DOI: 10.1002/jnr.490390607
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 3588 d)
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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Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404

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