Two‐Dimensional Characterization of Paired Helical Filament‐Tau from Alzheimer's Disease: Demonstration of an Additional 74‐kDa Component and Age‐Related Biochemical Modifications
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Summary
The results show that the severity of neurofibrillary degeneration of AD is modulated by age, with a lower degree of phosphorylation in the youngest and most severely affected patients.
- Type
- dissertation
- Published
- 1997-08-01
- Cited by
- 81
- References
- 62
- Access
- Open access
- OpenAlex
- https://openalex.org/W9231745
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:16774739
Keywords
beta-Carotene, Oxidative phosphorylation, Degradation (telecommunications), BETA (programming language), Chemistry
References
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- Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain.
- Analysis of microtubule-associated protein tau glycation in paired helical filaments.
- Two dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines.
- Neurofibrillary degeneration in amyotrophic lateral sclerosis/parkinsonism-dementia complex of Guam. Immunochemical characterization of tau proteins.
- High resolution two-dimensional electrophoresis of proteins.
- Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases
- Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation.
- A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities.
- Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease.
- Specific Pathological Tau Protein Variants Characterize Pick's Disease
- Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding.
- Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease
- Characterization of mAb AP422, a novel phosphorylation‐dependent monoclonal antibody against tau protein
- Proline-directed and Non-proline-directed Phosphorylation of PHF-tau (*)
- AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease.
Cited by
- Atypical Progressive Supranuclear Palsy With Corticospinal Tract Degeneration
- Cortical Alzheimer type pathology does not influence tau pathology in progressive supranuclear palsy.
- Neurofibrillary pathology of Alzheimer's disease and other tauopathies.
- Genetic Characterisation of Neurodegenerative disorders
- 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
- Tau, a biological marker of neurodegenerative diseases.
- Implication de la protéine tau dans la dégénérescence neuronale in vitro
- Genetika neurodegenerativnih bolesti
- Argyrophilic Grain Disease Is a Sporadic 4‐Repeat Tauopathy
- Neurofibrillary Degeneration in Progressive Supranuclear Palsy and Corticobasal Degeneration
- Tau protein isoforms, phosphorylation and role in neurodegenerative disorders.
- Tau Protein in Normal and Alzheimer's Disease Brain: An Update
- [Tauopathy and Alzheimer disease: a full degenerating process].
- Exon 3 insert of tau protein in neurodegenerative diseases
- Rapid Tau Protein Dephosphorylation and Differential Rephosphorylation during Cardiac Arrest-Induced Cerebral Ischemia and Reperfusion
- The complex p25/Cdk5 kinase in neurofibrillary degeneration and neuronal death: The missing link to cell cycle
- Alzheimer-specific epitope of AT100 in transfected cell lines with tau: toward an efficient cell model of tau abnormal phosphorylation.
- Phosphorylated Protein Kinases Associated with Neuronal and Glial Tau Deposits in Argyrophilic Grain Disease
- New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry
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