Specific Pathological Tau Protein Variants Characterize Pick's Disease
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Summary
The 55 and 64 kDa Tau doublet appears to be specific to PiD, less acidic than AD Tau proteins, and well correlated with the presence of PB.
- Type
- article
- Published
- 1996-02-01
- Cited by
- 229
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1967000235
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:36815305
Keywords
Pathological, Tau protein, Disease, Computational biology, Biology
References
No references recorded for this paper.
Cited by
- Two‐Dimensional Characterization of Paired Helical Filament‐Tau from Alzheimer's Disease: Demonstration of an Additional 74‐kDa Component and Age‐Related Biochemical Modifications
- Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies
- Therapeutic and functional studies in animal models of Alzheimer's disease
- Tau gene mutations and tau pathology in frontotemporal dementia and parkinsonism linked to chromosome 17.
- Neurofibrillary pathology of Alzheimer's disease and other tauopathies.
- Differential Incorporation of Tau Isoforms in Alzheimer's Disease
- Etude du mécanisme d’agrégation de la protéine Tau et son inhibition par des composés polyphénoliques
- Anti-tau phospho-specific Ser262 antibody recognizes a variety of abnormal hyper-phosphorylated tau deposits in tauopathies including Pick bodies and argyrophilic grains
- Argyrophilic grain disease and Alzheimer's disease are distinguished by their different distribution of tau protein isoforms
- Tau nucléaire : un acteur clé dans le stress neuronal
- Repetitive head trauma, chronic traumatic encephalopathy and tau: Challenges in translating from mice to men.
- Fatal Attractions: Protein Aggregates in Neurodegenerative Disorders
- Neuropathology of Pick body disease.
- Tau, a biological marker of neurodegenerative diseases.
- Implication de la protéine tau dans la dégénérescence neuronale in vitro
- Juvenile Frontotemporal Dementia with Parkinsonism Associated with Tau Mutation G389R
- Molekulare Neuropathologie der Nicht-Alzheimer-Demenzen
- Invited review: Prion‐like transmission and spreading of tau pathology
- Normal and pathological Tau proteins as factors for microtubule assembly.
- Expanding morphological dimensions in neuropathology, from sequence biology to pathological sequences and clinical consequences
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