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  • Articles: DFG German National Licenses  (3)
  • 1995-1999  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Two-Dimensional Characterization of Paired Helical Filament-Tau from Alzheimer's Disease: Demonstration of an Additional 74-kDa Component and Age-Related Biochemical Modifications (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: PHF-tau proteins are the major components of the paired helical filament (PHF) from Alzheimer's disease (AD) neurofibrillary lesions. They differ both qualitatively and quantitatively in their degree of phosphorylation when compared with native tau proteins. However, little is known about the extent and heterogeneity of phosphorylated sites or the isoform composition and the isoelectric variants of PHF-tau. Therefore, we have characterized PHF-tau proteins from cortical brain tissue homogenates of 13 AD patients using two-dimensional gel electrophoresis. Whatever the topographical origin of brain tissue homogenates, PHF-tau proteins shared the same two-dimensional gel electrophoresis profile made of a tau triplet of 55, 64, and 69 kDa. A 74-kDa hyperphosphorylated tau component was detected particularly in the youngest and most severely affected AD patients. This additional component of hyperphosphorylated tau was shown to correspond to the longest brain tau isoform. Furthermore, the isoelectric points of PHF-tau from older AD patients were significantly more basic, indicating a lower degree of phosphorylation. These results show that the severity of neurofibrillary degeneration of AD is modulated by age.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69020834.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Hyperphosphorylated tau proteins differentiate corticobasal degeneration and Pick’s disease (1996)
    Springer
    Acta neuropathologica 91 (1996), S. 351-359 
    Details
    ISSN: 1432-0533
    Keywords: Key words Cytoskeleton ; Microtubule-associated ; proteins ; Neurodegenerative disorders ; Protein ; phosphorylation ; Western blotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In neurodegenerative disorders, hyperphosphorylated tau proteins aggregate into abnormal filaments. In the present study, tau protein alterations were studied in one corticobasal degeneration and seven Pick’s disease cases using specific immunological probes. The typical lesions of corticobasal degeneration and Pick’s disease were revealed by immunohistochemistry, including the presence of Pick bodies and achromatic swollen neurons, neuritic alterations, and neurofibrillary tangles. Tau-immunoreactive glial tangles were also observed. By immunoblotting, the case of corticobasal degeneration was characterized by the tau profile previously reported to occur in progressive supranuclear palsy with an intense labeling of the two tau 64 and 69 bands, while tau 55 was not visualized. In Pick’s disease cases with Pick bodies and neurofibrillary tangles, a tau triplet similar to that encountered in Alzheimer’s disease (tau 55, 64 and 69) was detected. Furthermore, a particular tau profile was found in four Pick’s disease cases showing only Pick bodies and no neurofibrillary tangles. In these cases, tau 55 and 64 were strongly immunoreactive, whereas tau 69 was almost unlabeled. These differences are likely to be related to particular pools of tau isoforms present within the degenerating neurons. Since there is a great diversity of neurodegenerative disorders with substantial clinical and neuropathological overlap, the electrophoretic profile of tau proteins could represent a useful marker for the type of neurodegeneration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050436
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    One-and-a-half syndrome in pontine infarcts: MRI correlates (1999)
    Springer
    Neuroradiology 41 (1999), S. 666-669 
    Details
    ISSN: 1432-1920
    Keywords: Key words One-and-a-half syndrome ; Infarcts pontine ; Magnetic resonance imaging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The one-and-a-half syndrome is characterised by a lateral gaze palsy in one direction and internuclear ophthalmoplegia in the other. It is due to a unilateral lesion of the dorsal pontine tegmentum, involving the ipsilateral paramedian pontine reticular formation, internuclear fibres of the ipsilateral medical longitudinal fasciculus and, usually, the abducens nucleus. The main causes of this rare syndrome are stroke and multiple sclerosis. Few cases have been reported since the introduction of MRI. Our aim was to examine clinicoradiological correlations in six patients with a one-and-a-half syndrome due to a stroke. Ophthalmological symptoms were diplopia, oscillopsia or blurred vision. Four patients had an associated facial nerve palsy, three a hemiparesis and one a unilateral hemihypoaesthesia. MRI revealed an infarct in the pons in all patients. The cause of the infarct was a basilar artery dissection in one patient, bilateral vertebral artery dissection in a second and unknown in the other four. All patients recovered within 2 days to 8 weeks. This study showed a good correlation between the site of the lesion (superior, inferior or extensive pontine ischaemia) and clinical deficits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002340050821
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    Paper (German National Licenses)
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