Background and Aim: Tau protein is a microtubule-associated protein that plays a critical role in microtubule dynamics and maintaining the structure of neurons.
Mohammad Majidi+2 more
doaj
Proteasomal degradation of tau protein [PDF]
AbstractFilamentous inclusions composed of the microtubule‐associated protein tau are a defining characteristic of a large number of neurodegenerative diseases. Here we show that tau degradation in stably transfected and non‐transfected SH‐SY5Y cells is blocked by the irreversible proteasome inhibitor lactacystin.
Michel Goedert+5 more
openaire +3 more sources
Preferential tau aggregation in von Economo neurons and fork cells in frontotemporal lobar degeneration with specific MAPT variants. [PDF]
Tau aggregation is a hallmark feature in a subset of patients with frontotemporal dementia (FTD). Early and selective loss of von Economo neurons (VENs) and fork cells within the frontoinsular (FI) and anterior cingulate cortices (ACC) is observed in ...
Coppola, Giovanni+13 more
core +1 more source
Follow-up investigations of tau protein and S-100B levels in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease [PDF]
Background: S-100B and tau protein have a high differential diagnostic potential for the diagnosis of Creutzfeldt-Jakob disease (CJD). So far there has been only limited information available about the dynamics of these parameters in the cerebrospinal ...
Barbara Ciesielczyk+18 more
core +1 more source
Purification tags markedly affect self‐aggregation of CPEB3
Although recombinant proteins are used to study protein aggregation in vitro, uncleaved tags can interfere with accurate interpretation. Our findings demonstrate that His₆‐GFP and His₁₂ tags significantly affect liquid droplet and amyloid fibril formation in the intrinsically disordered region (IDR) of mouse cytoplasmic polyadenylation element‐binding ...
Harunobu Saito+6 more
wiley +1 more source
Cerebrolysin™ efficacy in a transgenic model of tauopathy: role in regulation of mitochondrial structure. [PDF]
BackgroundAlzheimer's Disease (AD) and Fronto temporal lobar dementia (FTLD) are common causes of dementia in the aging population for which limited therapeutical options are available. These disorders are associated with Tau accumulation.
Adame, Anthony+10 more
core +2 more sources
It has been over a quarter century since the discovery in the mid-1980s that the paired helical filaments of neurofibrillary tangles were made up of abnormally hyperphosphorylated tau. A decade earlier tau had been first isolated from porcine brain as a heat stable protein essential for microtubule assembly.
Jesús Avila, Miguel Medina
openaire +3 more sources
Aβ42 promotes the aggregation of α‐synuclein splice isoforms via heterogeneous nucleation
The aggregation of amyloid‐β (Aβ) and α‐synuclein (αSyn) is associated with Alzheimer's and Parkinson's diseases. This study reveals that Aβ aggregates serve as potent nucleation sites for the aggregation of αSyn and its splice isoforms, shedding light on the intricate interplay between these two pathogenic proteins.
Alexander Röntgen+2 more
wiley +1 more source
Tau phosphorylation at Alzheimer\u27s disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated. [PDF]
Abnormal phosphorylation of the microtubule-associated protein tau is observed in many neurodegenerative diseases, including Alzheimer\u27s disease (AD).
Ando, Kanae+6 more
core +1 more source
Serum heart-type fatty acid-binding protein and cerebrospinal fluid tau: Marker candidates for dementia with Lewy bodies [PDF]
Background: The measurement of biomarkers in cerebrospinal fluid (CSF) has gained increasing acceptance in establishing the diagnosis of some neurodegenerative diseases.
Andreasen N+27 more
core +1 more source