Cited by 377Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein

Open access
Goedert, M, Jakes, R, Crowther, R A, Cohen, P, Vanmechelen, E, Vandermeeren, M, Cras, P·1994·Biochemical Journal

Abstract

Tau is a neuronal phosphoprotein the expression of which is developmentally regulated. A single tau isoform is expressed in fetal human brain but six isoforms are expressed in adult human brain, with the fetal isoform corresponding to the shortest adult isoform. Phosphorylation is also developmentally regulated, as fetal tau is phosphorylated at more sites than adult tau. In Alzheimer's disease, the six adult tau isoforms become hyperphosphorylated and form the paired helical filament (PHF), the major fibrous component of the neurofibrillary lesions. One way to identify phosphorylated sites in tau is to use antibodies that recognize phosphorylated residues within a specific amino acid sequence. We here characterize the two novel phosphorylation-dependent anti-tau antibodies AT270 and AT180 and identify their epitopes as containing phosphorylated Thr-181 and Thr-231 respectively. With these antibodies we show that these two threonine residues are partially phosphorylated in fetal and adult tau and almost fully phosphorylated in PHF tau. This result contrasts with previous studies of Ser-202 and Ser-396 which are partially phosphorylated in fetal tau, unphosphorylated in adult tau but almost fully phosphorylated in PHF tau.

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 · 10.1042/bj3010871

Cites

51 of 51 references verified0 citation errors · 0 not checkable

Statistics

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?

  • No significant differences in phospho-tau levels relative to controls were observed for 12E8 and AT270 with modifiers from the EY screen.

    “No significant differences in phospho-tau levels relative to controls were observed (Supplementary Material, Fig. S4).”

    From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [86]

    The indexed Abstract characterizes AT270 and reports phosphorylation in fetal, adult, and paired-helical-filament tau. It does not address an EY screen, 12E8, or statistical comparisons of phospho-tau levels with controls; searches for those terms found no relevant passage. The cited paper therefore cannot verify the reported lack of a significant difference. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

Self-check

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

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

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P.
Affiliations
  • MRC Laboratory of Molecular Biology (GB)
  • University of Dundee (GB)
  • Fujirebio (Belgium) (BE)
  • University of Antwerp (BE)
Corresponding author
  • Goedert, M
  • Jakes, R
Venue
Biochemical Journal
Published
1994-08-01
Volume
301
Issue
3
Pages
871-877
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1958842451
Cited by
375
References
51
Citations by year
2026: 4 · 2025: 10 · 2024: 4 · 2023: 5 · 2022: 12 · 2021: 10 · 2020: 8 · 2019: 9 · 2018: 7 · 2017: 10 · 2016: 7 · 2015: 8 · 2014: 8 · 2013: 9 · 2012: 13
FWCI
9.97
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Discovery Research Portal (University of Dundee) (submittedVersion)
Topics
  • Health Sciences › Medicine › Physiology › 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, paired helical filaments, Alzheimer's disease, epitope mapping, phosphorylation sites, neurofibrillary tangles, tau hyperphosphorylation
MeSH terms
Alzheimer Disease, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antibody Specificity, Epitopes, Binding Sites, Brain, Brain Chemistry, Cerebral Cortex, Humans, Molecular Sequence Data, Phosphorylation, Phosphothreonine, Recombinant Proteins, Structure-Activity Relationship, Microscopy, Immunoelectron, Neurofibrillary Tangles, tau Proteins, Rats

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