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La noción de la muerte como objeto de investigación de la psicología del desarrollo
Cuadernos de Neuropsicología, 2014 Ramiro Tau
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Somatostatin, tau, and B-amyloid within the anterior olfactory nucleus in alzheimer disease
, 2010 Ricardo Insausti +6 more
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Sex Differences in Alzheimer Disease Imaging Biomarkers in a Diverse, Community-Based Cohort.
JAMA Netw OpenAkinci M +8 more
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Tau acetylation at K280 regulates tau phosphorylation
International Journal of Neuroscience, 2022Accumulation of hyperphosphorylated tau is a key pathological finding of Alzheimer's disease. Recently, acetylation of tau is emerging as another key pathogenic modification, especially regarding the acetylation of tau at K280 of the hexapeptide 275VQIINK280, a critical sequence in driving tau aggregation.
Min-Seok, Kim +6 more
openaire +2 more sources
2019
Many proteins, particularly those that are intrinsically disordered and carry charges have a tendency to undergo liquid liquid phase separation (LLPS). Phase separation is a widespread mechanism by which cells concentrate a set of proteins to perform molecular reactions, and appear to compartmentalize molecular functions.
Kenneth S, Kosik, Songi, Han
openaire +2 more sources
Many proteins, particularly those that are intrinsically disordered and carry charges have a tendency to undergo liquid liquid phase separation (LLPS). Phase separation is a widespread mechanism by which cells concentrate a set of proteins to perform molecular reactions, and appear to compartmentalize molecular functions.
Kenneth S, Kosik, Songi, Han
openaire +2 more sources
2019
The accumulation of tau filaments in neurons is a pathological hallmark of various neurodegenerative diseases, including Alzheimer's disease. However, it is not the filamentous aggregates themselves, but non-filamentous tau species, tau oligomer, that is thought to be the culprit in tau-mediated neurodegeneration.
Sumihiro, Maeda, Akihiko, Takashima
openaire +2 more sources
The accumulation of tau filaments in neurons is a pathological hallmark of various neurodegenerative diseases, including Alzheimer's disease. However, it is not the filamentous aggregates themselves, but non-filamentous tau species, tau oligomer, that is thought to be the culprit in tau-mediated neurodegeneration.
Sumihiro, Maeda, Akihiko, Takashima
openaire +2 more sources
Tau protein and tau aggregation inhibitors
Neuropharmacology, 2010Alzheimer disease is characterized by pathological aggregation of two proteins, tau and Abeta-amyloid, both of which are considered to be toxic to neurons. In this review we summarize recent advances on small molecule inhibitors of protein aggregation with emphasis on tau, with activities mediated by the direct interference of self-assembly.
Bulic, B. +3 more
openaire +3 more sources
2019
The pathological propagation of Tau protein is a hallmark of multiple neurodegenerative disorders, collectively referred to tauopathies with Alzheimer's disease (AD) being most prevalent, but including a range of frontotemporal dementias (FTDs). The extracellular Tau is important during the progression of tauopathies, although Tau is mainly expressed ...
Zhi, Ruan, Tsuneya, Ikezu
openaire +2 more sources
The pathological propagation of Tau protein is a hallmark of multiple neurodegenerative disorders, collectively referred to tauopathies with Alzheimer's disease (AD) being most prevalent, but including a range of frontotemporal dementias (FTDs). The extracellular Tau is important during the progression of tauopathies, although Tau is mainly expressed ...
Zhi, Ruan, Tsuneya, Ikezu
openaire +2 more sources
2012
The protein tau is the most abundant microtubule associated protein in the central and peripheral nervous system. In the brain, tau plays a role in the assembly and stabilization of microtubules. The function of tau, however, appears to overlap with other microtubule binding proteins.
Nitin, Chaudhary, Ramakrishnan, Nagaraj
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The protein tau is the most abundant microtubule associated protein in the central and peripheral nervous system. In the brain, tau plays a role in the assembly and stabilization of microtubules. The function of tau, however, appears to overlap with other microtubule binding proteins.
Nitin, Chaudhary, Ramakrishnan, Nagaraj
openaire +2 more sources