Structure and pathology of tau protein in Alzheimer disease
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11120%2F12%3A43906685" target="_blank" >RIV/00216208:11120/12:43906685 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00023752:_____/12:43913799
Výsledek na webu
<a href="http://dx.doi.org/10.1155/2012/731526" target="_blank" >http://dx.doi.org/10.1155/2012/731526</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1155/2012/731526" target="_blank" >10.1155/2012/731526</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Structure and pathology of tau protein in Alzheimer disease
Popis výsledku v původním jazyce
Alzheimer's disease (AD) is the most common type of dementia. In connection with the global trend of prolonging human life and the increasing number of elderly in the population, the AD becomes one of the most serious health and socioeconomic problems ofthe present. Tau protein promotes assembly and stabilizes microtubules, which contributes to the proper function of neuron. Alterations in the amount or the structure of tau protein can affect its role as a stabilizer of microtubules as well as some ofthe processes in which it is implicated. The molecular mechanisms governing tau aggregation are mainly represented by several posttranslational modifications that alter its structure and conformational state. Hence, abnormal phosphorylation and truncation of tau protein have gained attention as key mechanisms that become tau protein in a pathological entity. Evidences about the clinicopathological significance of phosphorylated and truncated tau have been documented during the progressio
Název v anglickém jazyce
Structure and pathology of tau protein in Alzheimer disease
Popis výsledku anglicky
Alzheimer's disease (AD) is the most common type of dementia. In connection with the global trend of prolonging human life and the increasing number of elderly in the population, the AD becomes one of the most serious health and socioeconomic problems ofthe present. Tau protein promotes assembly and stabilizes microtubules, which contributes to the proper function of neuron. Alterations in the amount or the structure of tau protein can affect its role as a stabilizer of microtubules as well as some ofthe processes in which it is implicated. The molecular mechanisms governing tau aggregation are mainly represented by several posttranslational modifications that alter its structure and conformational state. Hence, abnormal phosphorylation and truncation of tau protein have gained attention as key mechanisms that become tau protein in a pathological entity. Evidences about the clinicopathological significance of phosphorylated and truncated tau have been documented during the progressio
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
FH - Neurologie, neurochirurgie, neurovědy
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GBP304%2F12%2FG069" target="_blank" >GBP304/12/G069: Projekt excelence v oblasti neurověd</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2012
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
International Journal of Alzheimer's Disease
ISSN
2090-0252
e-ISSN
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Svazek periodika
2012
Číslo periodika v rámci svazku
Art.ID 731526, Online 29 May
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
13
Strana od-do
1-13
Kód UT WoS článku
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EID výsledku v databázi Scopus
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