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https://www.readbyqxmd.com/read/28088900/synaptic-plasticity-dementia-and-alzheimer-disease
#1
Pietro Giusti, Stephen D Skaper, Laura Facci, Morena Zusso
Neuroplasticity is not only shaped by learning and memory but is also a mediator of responses to neuron attrition and injury (compensatory plasticity). As an ongoing process it reacts to neuronal cell activity and injury, death, and genesis, which encompasses the modulation of structural and functional processes of axons, dendrites, and synapses. The range of structural elements that comprise plasticity includes long-term potentiation (a cellular correlate of learning and memory), synaptic efficacy and remodelling, synaptogenesis, axonal sprouting and dendritic remodelling, and neurogenesis and recruitment...
January 13, 2017: CNS & Neurological Disorders Drug Targets
https://www.readbyqxmd.com/read/28077166/threonine-175-a-novel-pathological-phosphorylation-site-on-tau-protein-linked-to-multiple-tauopathies
#2
Alexander J Moszczynski, Wencheng Yang, Robert Hammond, Lee Cyn Ang, Michael J Strong
Microtubule associated protein tau (tau) deposition is associated with a spectrum of neurodegenerative diseases collectively termed tauopathies. We have previously shown that amyotrophic lateral sclerosis (ALS) with cognitive impairment (ALSci) is associated with tau phosphorylation at Thr(175) and that this leads to activation of GSK3β which then induces phosphorylation at tau Thr(231). This latter step leads to dissociation of tau from microtubules and pathological tau fibril formation. To determine the extent to which this pathway is unique to ALS, we have investigated the expression of pThr(175) tau and pThr(231) tau across a range of frontotemporal degenerations...
January 11, 2017: Acta Neuropathologica Communications
https://www.readbyqxmd.com/read/28067492/the-polyphenol-altenusin-inhibits-in-vitro-fibrillization-of-tau-and-reduces-induced-tau-pathology-in-primary-neurons
#3
Sook Wern Chua, Alberto Cornejo, Janet van Eersel, Claire H Stevens, Inmaculada Vaca, Mercedes Cueto, Michael Kassiou, Amadeus Gladbach, Alex Macmillan, Lev Lewis, Renee Megan Whan, Lars Matthias Ittner
In Alzheimer´s disease the microtubule-associated protein tau forms intracellular neurofibrillary tangles (NFTs). A critical step in the formation of NFTs is the conversion of soluble tau into insoluble filaments. Accordingly, a current therapeutic strategy in clinical trials is aimed at preventing tau aggregation. Here, we assessed altenusin, a bioactive polyphenolic compound, for its potential to inhibit tau aggregation. Altenusin inhibits aggregation of tau protein into paired helical filaments in vitro...
January 9, 2017: ACS Chemical Neuroscience
https://www.readbyqxmd.com/read/28053038/large-soluble-oligomers-of-amyloid-%C3%AE-protein-from-alzheimer-brain-are-far-less-neuroactive-than-the-smaller-oligomers-to-which-they-dissociate
#4
Ting Yang, Shaomin Li, Huixin Xu, Dominic M Walsh, Dennis J Selkoe
: Soluble oligomers of amyloid β-protein (oAβ) isolated from the brains of Alzheimer's disease (AD) patients have been shown experimentally (in the absence of amyloid plaques) to impair hippocampal synaptic plasticity, decrease synapses, induce tau hyperphosphorylation and neuritic dystrophy, activate microglial inflammation, and impair memory in normal adult rodents. Nevertheless, there has been controversy about what types of oligomers actually confer these AD-like phenotypes. Here, we show that the vast majority of soluble Aβ species obtained from brains of humans who died with confirmed AD elute at high molecular weight (HMW) on nondenaturing size-exclusion chromatography...
January 4, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/28035925/novel-phospho-tau-monoclonal-antibody-generated-using-a-liposomal-vaccine-with-enhanced-recognition-of-a-conformational-tauopathy-epitope
#5
Clara Theunis, Oskar Adolfsson, Natalia Crespo-Biel, Kasia Piorkowska, Maria Pihlgren, David T Hickman, Valérie Gafner, Peter Borghgraef, Herman Devijver, Andrea Pfeifer, Fred Van Leuven, Andreas Muhs
The microtubule-associated protein Tau is an intrinsically unfolded, very soluble neuronal protein. Under still unknown circumstances, Tau protein forms soluble oligomers and insoluble aggregates that are closely linked to the cause and progression of various brain pathologies, including Alzheimer's disease. Previously we reported the development of liposome-based vaccines and their efficacy and safety in preclinical mouse models for tauopathy. Here we report the use of a liposomal vaccine for the generation of a monoclonal antibody with particular characteristics that makes it a valuable tool for fundamental studies as well as a candidate antibody for diagnostic and therapeutic applications...
December 30, 2016: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28009077/inflammasomes-as-therapeutic-targets-for-alzheimer-s-disease
#6
Claire S White, Catherine B Lawrence, David Brough, Jack Rivers-Auty
Alzheimer's disease is the most common form of progressive dementia, typified initially by short term memory deficits which develop into a dramatic global cognitive decline. The classical hall marks of Alzheimer's disease include the accumulation of amyloid oligomers and fibrils, and the intracellular formation of neurofibrillary tangles of hyperphosphorylated tau. It is now clear that inflammation also plays a central role in the pathogenesis of the disease through a number of neurotoxic mechanisms. Microglia are the key immune regulators of the CNS which detect amyloidopathy through cell surface and cytosolic pattern recognition receptors (PRRs) and respond by initiating inflammation through the secretion of cytokines such as interleukin-1β (IL-1β)...
December 23, 2016: Brain Pathology
https://www.readbyqxmd.com/read/28006031/selection-and-characterization-of-tau-binding-%C3%A1-enantiomeric-peptides-with-potential-for-therapy-of-alzheimer-disease
#7
Christina Dammers, Deniz Yolcu, Laura Kukuk, Dieter Willbold, Marcus Pickhardt, Eckhard Mandelkow, Anselm H C Horn, Heinrich Sticht, Marwa Nidal Malhis, Nadja Will, Judith Schuster, Susanne Aileen Funke
A variety of neurodegenerative disorders, including Alzheimer disease (AD), are associated with neurofibrillary tangles composed of the tau protein, as well as toxic tau oligomers. Inhibitors of pathological tau aggregation, interrupting tau self-assembly, might be useful for the development of therapeutics. Employing mirror image phage display with a large peptide library (over 109 different peptides), we have identified tau fibril binding peptides consisting of d-enantiomeric amino acids. d-enantiomeric peptides are extremely protease stable and not or less immunogenic than l-peptides, and the suitability of d-peptides for in vivo applications have already been demonstrated...
2016: PloS One
https://www.readbyqxmd.com/read/27979768/a-state-of-delirium-deciphering-the-effect-of-inflammation-on-tau-pathology-in-alzheimer-s-disease
#8
Matthew Barron, Jane Gartlon, Lee A Dawson, Peter J Atkinson, Marie-Christine Pardon
Alzheimer's disease (AD), the predominant form of dementia, is highly correlated with the abnormal hyperphosphorylation and aggregation of tau. Immune responses are key drivers of AD and how they contribute to tau pathology in human disease remains largely unknown. This review summarises current knowledge on the association between inflammatory processes and tau pathology. While, preclinical evidence suggests that inflammation can indeed induce tau hyperphosphorylation at both pre- and post-tangles epitopes, a better understanding of whether this develops into advanced pathological features such as neurofibrillary tangles is needed...
December 12, 2016: Experimental Gerontology
https://www.readbyqxmd.com/read/27975249/tau-oligomers-as-pathogenic-seeds-preparation-and-propagation-in-vitro-and-in-vivo
#9
Julia E Gerson, Urmi Sengupta, Rakez Kayed
Tau oligomers have been shown to be the main toxic tau species in a number of neurodegenerative disorders. In order to study tau oligomers both in vitro and in vivo, we have established methods for the reliable preparation, isolation, and detection of tau oligomers. Methods for the seeding of tau oligomers, isolation of tau oligomers from tissue, and detection of tau oligomers using tau oligomer-specific antibodies by biochemical and immunohistochemical methods are detailed below.
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27975246/detection-and-quantification-methods-for-fibrillar-products-of-in-vitro-tau-aggregation-assays
#10
Niki Nanavaty, Lauren Lin, Samantha H Hinckley, Jeff Kuret
Alzheimer's disease is characterized in part by the intracellular misfolding and aggregation of tau protein. The aggregates, which range in size from small oligomers to large filaments, are markers for disease diagnosis and staging, potential vectors for disease propagation, and candidate sources of neurotoxicity. Here we present protocols for synthesizing large tau aggregates characterized by filamentous morphology and cross-β-sheet structure from monomeric full-length tau precursors in vitro. We also describe their detection and quantification through thioflavin dye binding, filter trap, and transmission electron microscopy methods...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27975245/x-ray-structural-study-of-amyloid-like-fibrils-of-tau-peptides-bound-to-small-molecule-ligands
#11
Einav Tayeb-Fligelman, Meytal Landau
Atomic structures of Tau involved in Alzheimer's disease complexed with small molecule binders are the first step to define the Tau pharmacophore, leading the way to a structure-based design of improved diagnostics and therapeutics. Yet the partially disordered and polymorphic nature of Tau hinders structural analyses. Fortunately, short segments from amyloid proteins, which exhibit similar biophysical properties to the full-length proteins, also form fibrils and oligomers, and their atomic structures can be determined using X-ray microcrystallography...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27943341/pittsburgh-compound-b-pib-binds-amyloid-%C3%AE-protein-protofibrils
#12
Ghiam Yamin, David B Teplow
The neuropathology of Alzheimer's disease (AD) includes amyloid plaque formation by the amyloid β-protein (Aβ) and intracellular paired helical filament formation by tau protein. These neuropathogenetic features correlate with disease progression and have been revealed in brains of AD patients using positron emission tomography (PET). One of the most useful positron emission tomography imaging agents has been Pittsburgh Compound-B (PiB). However, since its introduction in 2002, substantial evidence has accumulated suggesting that Aβ oligomerization and protofibril formation, rather than fibril formation per se, may be the more important pathogenetic event in AD...
January 2017: Journal of Neurochemistry
https://www.readbyqxmd.com/read/27877124/tau-structures
#13
REVIEW
Jesus Avila, Juan S Jiménez, Carmen L Sayas, Marta Bolós, Juan C Zabala, Germán Rivas, Felix Hernández
Tau is a microtubule-associated protein that plays an important role in axonal stabilization, neuronal development, and neuronal polarity. In this review, we focus on the primary, secondary, tertiary, and quaternary tau structures. We describe the structure of tau from its specific residues until its conformation in dimers, oligomers, and larger polymers in physiological and pathological situations.
2016: Frontiers in Aging Neuroscience
https://www.readbyqxmd.com/read/27864661/molecular-anti-inflammatory-mechanisms-of-retinoids-and-carotenoids-in-alzheimer-s-disease-a-review-of-current-evidence
#14
REVIEW
Niyaz Mohammadzadeh Honarvar, Ahmad Saedisomeolia, Mina Abdolahi, Amir Shayeganrad, Gholamreza Taheri Sangsari, Babak Hassanzadeh Rad, Gerald Muench
Alzheimer's disease (AD) is considered as one of the most prevalent neurodegenerative disorders characterized by progressive loss of mental function and ability to learn. AD is a multifactorial disorder. Various hypotheses are suggested for the pathophysiology of AD including "Aβ hypothesis," "tau hypothesis," and "cholinergic hypothesis." Recently, it has been demonstrated that neuroinflammation is involved in the pathogenesis of AD. Neuroinflammation causes synaptic dysfunction and neuronal death within the brain...
November 18, 2016: Journal of Molecular Neuroscience: MN
https://www.readbyqxmd.com/read/27861127/nec-1-alleviates-cognitive-impairment-with-reduction-of-a%C3%AE-and-tau-abnormalities-in-app-ps1-mice
#15
Seung-Hoon Yang, Dongkeun Kenneth Lee, Jisu Shin, Sejin Lee, Seungyeop Baek, Jiyoon Kim, Hoyong Jung, Jung-Mi Hah, YoungSoo Kim
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by cognitive symptoms of learning and memory deficits. Such cognitive impairments are attributed to brain atrophy resulting from progressive neuronal and synaptic loss; therefore, alleviation of neural cell death is as an important target of treatment as other classical hallmarks of AD, such as aggregation of amyloid-β (Aβ) and hyperphosphorylation of tau. Here, we found that an anti-necroptotic molecule necrostatin-1 (Nec-1) directly targets Aβ and tau proteins, alleviates brain cell death and ameliorates cognitive impairment in AD models...
January 2017: EMBO Molecular Medicine
https://www.readbyqxmd.com/read/27834776/genetic-risk-as-a-marker-of-amyloid-%C3%AE-and-tau-burden-in-cerebrospinal-fluid
#16
Nicola Voyle, Hamel Patel, Amos Folarin, Stephen Newhouse, Caroline Johnston, Pieter Jelle Visser, Richard J B Dobson, Steven J Kiddle
BACKGROUND: The search for a biomarker of Alzheimer's disease (AD) pathology (amyloid-β (Aβ) and tau) is ongoing, with the best markers currently being measurements of Aβ and tau in cerebrospinal fluid (CSF) and via positron emission tomography (PET) scanning. These methods are relatively invasive, costly, and often have high screening failure rates. Consequently, research is aiming to elucidate blood biomarkers of Aβ and tau. OBJECTIVE: This study aims to investigate a case/control polygenic risk score (PGRS) as a marker of tau and investigate blood markers of a combined Aβ and tau outcome for the first time...
2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/27785513/modulating-the-microtubule-tau-interactions-in-biomotility-systems-by-altering-the-chemical-environment
#17
S Bhattacharyya, K Kim, H Nakazawa, M Umetsu, W Teizer
Obstacles in microtubule mediated neuronal transport can trigger dementia. We use bio-motility assays, that simulate the neuron chemistry in axonopathy, to screen chemicals, that retain the microtubule dynamics in healthy neuronal activity. Tau protein inhibits microtubule activity and leads to oligomerization. Iron(iii) untangles, whereas mono-sodium-glutamate destabilizes the microtubule oligomer.
December 5, 2016: Integrative Biology: Quantitative Biosciences From Nano to Macro
https://www.readbyqxmd.com/read/27770234/soluble-pre-fibrillar-tau-and-%C3%AE-amyloid-species-emerge-in-early-human-alzheimer-s-disease-and-track-disease-progression-and-cognitive-decline
#18
David J Koss, Glynn Jones, Anna Cranston, Heidi Gardner, Nicholas M Kanaan, Bettina Platt
Post-mortem investigations of human Alzheimer's disease (AD) have largely failed to provide unequivocal evidence in support of the original amyloid cascade hypothesis, which postulated deposition of β-amyloid (Aβ) aggregates to be the cause of a demented state as well as inductive to tau neurofibrillary tangles (NFTs). Conflicting evidence suggests, however, that Aβ plaques and NFTs, albeit to a lesser extent, are present in a substantial subset of non-demented individuals. Hence, a range of soluble tau and Aβ species has more recently been implicated as the disease-relevant toxic entities...
December 2016: Acta Neuropathologica
https://www.readbyqxmd.com/read/27760426/cl-nqtrp-alleviates-tauopathy-symptoms-in-a-model-organism-through-the-inhibition-of-tau-aggregation-engendered-toxicity
#19
Moran Frenkel-Pinter, Sharon Tal, Roni Scherzer-Attali, Malak Abu-Hussien, Idan Alyagor, Tal Eisenbaum, Ehud Gazit, Daniel Segal
Alzheimer's disease (AD) is the most abundant tauopathy and is characterized by Aβ-derived plaques and tau-derived tangles, resulting from the unfolding of the corresponding monomeric subunits into ordered β-sheet oligomers and fibrils. Intervening in the toxic aggregation process is a promising therapeutic approach, but, to date, a disease-modifying therapy is neither available for AD nor for other tauopathies. Along these lines, we have previously demonstrated that a small naphthoquinone-tryptophan hybrid, termed NQTrp, is an effective modulator of tauopathy in vitro and in vivo...
October 20, 2016: Neuro-degenerative Diseases
https://www.readbyqxmd.com/read/27731899/formation-release-and-internalization-of-stable-tau-oligomers-in-cells
#20
Susanne Wegmann, Samantha Nicholls, Shuko Takeda, Zhanyun Fan, Bradley T Hyman
Tau is a neuronal microtubule-binding protein that, in Alzheimer's disease and other neurodegenerative diseases, can form oligomeric and large fibrillar aggregates, which deposit in neurofibrillary tangles. Tau's physiological state of multimerization appears to vary across conditions, and a stable dimeric form of soluble tau has been suggested from experiments using recombinant tau in vitro. We tested if tau dimerization or oligomerization, also occurs in cells, and if soluble tau oligomers are relevant for the release and internalization of tau...
December 2016: Journal of Neurochemistry
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