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  • 1
    Electronic Resource
    Electronic Resource
    Modeling of a periodic instability in paired helical filaments reveals an axial repeat (2000)
    Springer
    Acta neuropathologica 99 (2000), S. 534-538 
    Details
    ISSN: 1432-0533
    Keywords: Key words Paired helical filaments ; Electron ¶microscopy ; Tau ; Neurofibrillary tangles ; Mathematical modeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Ultrastructural studies of paired helical filaments (PHF) have been facilitated by the ability to isolate enriched fractions of detergent-insoluble forms of PHF. These fractions are composed of a relatively homogeneous population of short (usually 〈 400 nm) highly fragmented PHF. A small proportion of isolated PHF have highly stereotyped angled profiles that represent deformations due to structural instability. These distorted PHF can be characterized quantitatively using a simple numerical procedure that reveals that the axial instabilities occur with predictable regularity over the length of the PHF. Using a structural model of PHF, it is shown that the periodicity of the axial instability can be correlated to an axially repeated subunit of uniform size. The upper limit for the axial extent of the repeated segment was calculated to be 80 nm, similar to the size of a single one-half twist in the PHF ribbon. It is proposed that this segment may represent one type of particle in the hierarchy of structural subunits in the PHF ribbon, or an oligomeric intermediate species in PHF assembly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010051157
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  • 2
    Electronic Resource
    Electronic Resource
    Absence of protease-resistant prion protein in dementia characterized by neuronal loss and status spongiosus (1993)
    Springer
    Acta neuropathologica 86 (1993), S. 515-517 
    Details
    ISSN: 1432-0533
    Keywords: Dementia ; Prion ; Pick's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Dementia characterized by neuronal loss and status spongiosus (DNLS) is a non-Alzheimer degenerative process which is characterized by Pick-like lobar atrophy with neuronal depletion and gliosis of the cerebral cortex, corpus striatum, medial thalamus, and substantia nigra and the absence of neuronal inclusions. To further investigate the cause and pathogenesis of DNLS, we probed cerebral homogenates from three cases of DNLS for protease-resistant prion protein to determine if DNLS could be a variant of a human prion disease. Limited proteolysis of prion proteins and guanidine thiocyanate treatment of cortical homogenates was used to enrich potential abnormal prion protein immunoreactivity. Although protease-resistant prion protein was detected in a case of sporadic Creutzfeldt-Jakob disease no abnormal prion protein was found in the cases of DNLS. We conclude that DNLS is not a human prion disease and remains an important dementia of uncertain eitology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00228588
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a shared epitope in cortical Lewy body fibrils and Alzheimer paired helical filaments (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 1-6 
    Details
    ISSN: 1432-0533
    Keywords: Lewy body ; Neurofilament ; Alzheimer's disease ; Paired helical filaments ; Diffuse Lewy body disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The straight fibrils of the Lewy body contain an epitope related to phosphorylation of the KSPV motif common to the C termini of the 200- and 170-kDa neurofilament subunits and τ. To further characterize this phosphorylated neurofilament/τ epitope in Lewy bodies and to analyze the constituents of isolated Lewy bodies we used a combined biochemical and immunochemical approach. In formalin-fixed paraffin-embedded tissue cortical Lewy bodies were labelled by monoclonal antibodies directed to phosphorylation-dependent KSPV epitopes in the sequences of neurofilament and phosphorylation-independent epitopes. Immunoblotting of solubilized Lewy body fibrils with the same antibodies which stained Lewy bodies in tissue sections revealed that the immunoreactive Lewy body proteins were phosphorylated neurofilament subunits. An antibody to the 68-kDa neurofilament subunit labelled Lewy bodies and Lewy body protein at 50–68 kDa. We conclude that the shared phosphorylated epitope in Lewy body fibrils and paired helical filaments is related to the common KSPV sequence in neurofilament and τ, and that all three neurofilament subunits are present in the Lewy body. This result indicates that although Lewy bodies and neurofibrillary tangles share epitopes they are comprised of distinct structural subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294352
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    Paper (German National Licenses)
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  • 4
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    Unknown
    On Balzer's small set solutin to Russell's Paradox (1993)
    The Hague : Periodicals Archive Online (PAO)
    The Journal of Value Inquiry. 27:3/4 (1993) 541 
    Details
    ISSN: 0022-5363
    Topics: Philosophy
    Notes: Forum
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:n252-1993-027-03-000025
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  • 5
    Electronic Resource
    Electronic Resource
    Alzheimer paired helical filaments: a comparison with the twisted ribbon model (1995)
    Springer
    Acta neuropathologica 90 (1995), S. 194-197 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Paired helical filaments ; Electron microscopy ; Tau
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To investigate if Alzheimer paired helical filaments (PHF) closely resemble twisted ribbons, as indicated by recent high-resolution ultrastructural studies, we compared physical models of twisted ribbons with electron microscopic images of PHF. Uranyl-acetate-stained, isolated PHF with one or two helical turns were compared with scale models of twisted ribbons with one and two helical turns rotated at different angles. The various rotations of the twisted ribbon model corresponded well with the different orientations of randomly dispersed PHF. The electron-dense regions of individual PHF turns previously thought to represent a cross-over site of paired filaments corresponded to the edge of the twisted ribbon when the ribbon was oriented perpendicular to the filament axis. These data indicate that the overall configuration of PHF is a twisted ribbon but does not exclude possible configuration restrictions due to an ordered arrangement of subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294320
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Alzheimer paired helical filaments: a comparison with the twisted ribbon model (1995)
    Springer
    Acta neuropathologica 90 (1995), S. 194-197 
    Details
    ISSN: 1432-0533
    Keywords: Key words Alzheimer's disease ; Paired helical ; filaments ; Electron microscopy ; Tau
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To investigate if Alzheimer paired helical filaments (PHF) closely resemble twisted ribbons, as indicated by recent high-resolution ultrastructural studies, we compared physical models of twisted ribbons with electron microscopic images of PHF. Uranyl-acetate-stained, isolated PHF with one or two helical turns were compared with scale models of twisted ribbons with one and two helical turns rotated at different angles. The various rotations of the twisted ribbon model corresponded well with the different orientations of randomly dispersed PHF. The electron-dense regions of individual PHF turns previously thought to represent a cross-over site of paired filaments corresponded to the edge of the twisted ribbon when the ribbon was oriented perpendicular to the filament axis. These data indicate that the overall configuration of PHF is a twisted ribbon but does not exclude possible configuration restrictions due to an ordered arrangement of subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050318
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    Paper (German National Licenses)
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