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Proteolytic cleavage of polymeric tau protein by caspase-3: implications for Alzheimer disease

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023752%3A_____%2F13%3A43914507" target="_blank" >RIV/00023752:_____/13:43914507 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1097/NEN.0000000000000013" target="_blank" >http://dx.doi.org/10.1097/NEN.0000000000000013</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1097/NEN.0000000000000013" target="_blank" >10.1097/NEN.0000000000000013</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Proteolytic cleavage of polymeric tau protein by caspase-3: implications for Alzheimer disease

  • Original language description

    Truncated tau protein at Asp(421) is associated with neurofibrillary pathology in Alzheimer disease (AD); however, little is known about its presence in the form of nonfibrillary aggregates. Here, we report immunohistochemical staining of the Tau-C3 antibody, which recognizes Asp(421)-truncated tau, in a group of AD cases with different extents of cognitive impairment. In the hippocampus, we found distinct nonfibrillary aggregates of Asp(421)-truncated tau. Unlike Asp(421)-composed neurofibrillary tangles, however, these nonfibrillary pathologies did not increase significantly with respect to the Braak staging and, therefore, make no significant contribution to cognitive impairment. On the other hand, despite in vitro evidence that caspase-3 cleaves monomeric tau at Asp(421), to date, this truncation has not been demonstrated to be executed by this protease in polymeric tau entities. We determined that Asp(421) truncation can be produced by caspase-3 in oligomeric and multimeric comple

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    ED - Physiology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GBP304%2F12%2FG069" target="_blank" >GBP304/12/G069: Project of excellence in the field of neuroscience</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Neuropathology and Experimental Neurology

  • ISSN

    0022-3069

  • e-ISSN

  • Volume of the periodical

    72

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    17

  • Pages from-to

    1145-1161

  • UT code for WoS article

    000330433200004

  • EID of the result in the Scopus database