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amyloid oligomer

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https://www.readbyqxmd.com/read/27919808/attenuation-of-amyloid-fibrillation-in-presence-of-warfarin-a-biophysical-investigation
#1
Mohammad Khursheed Siddiqi, Parvez Alam, Sumit Kumar Chaturvedi, Saima Nusrat, Yasser E Shahein, Rizwan Hasan Khan
Protein misfolding and aggregation are associated with more than twenty diseases, such as neurodegenerative diseases. The amyloid oligomers and fibrils may induce cell membrane disruption and lead to cell apoptosis. A great number of studies have focused on discovery of amyloid inhibitors which may prevent or treat amyloidosis. In this study, we used human serum albumin (HSA) as an amyloid model to test the anti-amyloid effects of warfarin (WFN), a very well-known drug for treatment of thrombosis and also used by biophysicists to characterize the specific binding site on HSA (site I of subdomain IIA)...
December 2, 2016: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/27911757/local-and-use-dependent-effects-of-%C3%AE-amyloid-oligomers-on-nmda-receptor-function-revealed-by-optical-quantal-analysis
#2
Brooke L Sinnen, Aaron B Bowen, Emily S Gibson, Matthew J Kennedy
: Beta amyloid (Aβ) triggers the elimination of excitatory synaptic connections in the CNS, an early manifestation of Alzheimer's disease. Oligomeric assemblies of Aβ peptide associate with excitatory synapses resulting in synapse elimination through a process that requires NMDA-type glutamate receptor activation. Whether Aβ affects synaptic NMDA receptor (NMDAR) function directly and acts locally at synapses to which it has bound and whether synaptic activity influences Aβ synaptic binding and synaptotoxicity have remained fundamental questions...
November 9, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/27908246/inhibition-of-chaperonin-groel-by-a-monomer-of-ovine-prion-protein-and-its-oligomeric-forms
#3
S S Kudryavtseva, Y Y Stroylova, I A Zanyatkin, T Haertle, V I Muronetz
The possibility of inhibition of chaperonin functional activity by amyloid proteins was studied. It was found that the ovine prion protein PrP as well as its oligomeric and fibrillar forms are capable of binding with the chaperonin GroEL. Besides, GroEL was shown to promote amyloid aggregation of the monomeric and oligomeric PrP as well as PrP fibrils. The monomeric PrP was shown to inhibit the GroEL-assisted reactivation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The oligomers of PrP decelerate the GroEL-assisted reactivation of GAPDH, and PrP fibrils did not affect this process...
October 2016: Biochemistry. Biokhimii︠a︡
https://www.readbyqxmd.com/read/27905353/-twenty-five-years-of-the-amyloid-hypothesis-of-alzheimer-disease-advances-failures-and-new-perspectives
#4
O S Levin, E E Vasenina
Amyloid hypothesis of Alzheimer's disease (AD) has been long the primary one. During the 25-year history the concept has been dramatically changed. Accumulation of β-amyloid is associated not only with the disruption of its synthesis (as it seemed after the discovery of genetic mechanisms of some familial cases of AD) but rather with the disruption of its clearance and elimination from the brain tissue via the microcirculatory system. It has been recognized that soluble oligomers of β-amyloid, but not senile plaques that consisted of insoluble conjugates described by A...
2016: Zhurnal Nevrologii i Psikhiatrii Imeni S.S. Korsakova
https://www.readbyqxmd.com/read/27904493/beta-2-adrenergic-receptor-activation-enhances-neurogenesis-in-alzheimer-s-disease-mice
#5
Gao-Shang Chai, Yang-Yang Wang, Amina Yasheng, Peng Zhao
Impaired hippocampal neurogenesis is one of the early pathological features of Alzheimer's disease. Enhancing adult hippocampal neurogenesis has been pursued as a potential therapeutic strategy for Alzheimer's disease. Recent studies have demonstrated that environmental novelty activates β2-adrenergic signaling and prevents the memory impairment induced by amyloid-β oligomers. Here, we hypothesized that β2-adrenoceptor activation would enhance neurogenesis and ameliorate memory deficits in Alzheimer's disease...
October 2016: Neural Regeneration Research
https://www.readbyqxmd.com/read/27903721/cross-talk-between-brain-innate-immunity-and-serotonin-signaling-underlies-depressive-like-behavior-induced-by-alzheimer-s-amyloid-%C3%AE-oligomers-in-mice
#6
Jose Henrique Ledo, Estefania P Azevedo, Danielle Beckman, Felipe C Ribeiro, Luis E Santos, Daniela S Razolli, Grasielle C Kincheski, Helen M Melo, Maria Bellio, Antonio L Teixeira, Licio A Velloso, Debora Foguel, Fernanda G De Felice, Sergio T Ferreira
: Considerable clinical and epidemiological evidence links Alzheimer's disease (AD) and depression. However, the molecular mechanisms underlying this connection are largely unknown. We reported recently that soluble Aβ oligomers (AβOs), toxins that accumulate in AD brains and are thought to instigate synapse damage and memory loss, induce depressive-like behavior in mice. Here, we report that the mechanism underlying this action involves AβO-induced microglial activation, aberrant TNF-α signaling, and decreased brain serotonin levels...
November 30, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/27900617/new-and-evolving-concepts-regarding-the-prognosis-and-treatment-of-cardiac-amyloidosis
#7
REVIEW
Stefano Perlini, Roberta Mussinelli, Francesco Salinaro
Systemic amyloidoses are rare and proteiform diseases, caused by extracellular accumulation of insoluble misfolded fibrillar proteins. Prognosis is dictated by cardiac involvement, which is especially frequent in light chain (AL) and in transthyretin variants (ATTR, both mutated, (ATTRm), and wild-type, (ATTRwt)). Recently, ATTRwt has emerged as a potentially relevant cause of a heart failure with preserved ejection fraction (HFpEF). Cardiac amyloidosis is an archetypal example of restrictive cardiomyopathy, with signs and symptoms of global heart failure and diastolic dysfunction...
November 29, 2016: Current Heart Failure Reports
https://www.readbyqxmd.com/read/27881781/blocking-the-interaction-between-ephb2-and-addls-by-a-small-peptide-rescues-impaired-synaptic-plasticity-and-memory-deficits-in-a-mouse-model-of-alzheimer-s-disease
#8
Xiao-Dong Shi, Kai Sun, Rui Hu, Xiao-Ya Liu, Qiu-Mei Hu, Xiao-Yu Sun, Bin Yao, Nan Sun, Jing-Ru Hao, Pan Wei, Yuan Han, Can Gao
: Soluble amyloid-β (Aβ) oligomers, also known as Aβ-derived diffusible ligands (ADDLs), are thought to be the key pathogenic factor in Alzheimer's disease (AD), but there is still no effective treatment for preventing or reversing the progression of the disease. Targeting NMDA receptor trafficking and regulation is a new strategy for early treatment of AD. Aβ oligomers have been found to bind to the fibronectin (FN) type III repeat domain of EphB2 to trigger EphB2 degradation, thereby impairing the normal functioning of NMDA receptors and resulting in cognitive deficits...
November 23, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/27878186/towards-an-understanding-of-amyloid-%C3%AE-oligomers-characterization-toxicity-mechanisms-and-inhibitors
#9
Shin Jung C Lee, Eunju Nam, Hyuck Jin Lee, Masha G Savelieff, Mi Hee Lim
Alzheimer's disease (AD) is characterized by an imbalance between production and clearance of amyloid-β (Aβ) species. Aβ peptides can transform structurally from monomers into β-stranded fibrils via multiple oligomeric states. Among the various Aβ species, structured oligomers are proposed to be more toxic than fibrils; however, the identification of Aβ oligomers has been challenging due to their heterogeneous and metastable nature. Multiple techniques have recently helped us gain a better understanding of oligomers' assembly details and structural properties...
November 23, 2016: Chemical Society Reviews
https://www.readbyqxmd.com/read/27865831/rutin-suppresses-human-amylin-hiapp-misfolding-and-oligomer-formation-in-vitro-and-ameliorates-diabetes-and-its-impacts-in-human-amylin-hiapp-transgenic-mice
#10
Jacqueline F Aitken, Kerry M Loomes, Isabel Riba-Garcia, Richard D Unwin, Gordana Prijic, Ashley S Phillips, Anthony R J Phillips, Donghai Wu, Sally D Poppitt, Ke Ding, Perdita E Barran, Andrew W Dowsey, Garth J S Cooper
Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D...
November 16, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27864869/anthoxanthin-polyphenols-attenuate-a%C3%AE-oligomer-induced-neuronal-responses-associated-with-alzheimer-s-disease
#11
Kayla M Pate, McCall Rogers, John Will Reed, Nicholas van der Munnik, Steven Zebulon Vance, Melissa A Moss
AIMS: Epidemiological evidence implicates polyphenols as potential natural therapeutics for Alzheimer's disease (AD). To investigate this prospect, five anthoxanthin polyphenols were characterized for their ability to reduce amyloid-β (Aβ) oligomer-induced neuronal responses by two mechanisms of action, modulation of oligomerization and antioxidant activity, as well as the synergy between these two mechanisms. METHODS: Anthoxanthin oligomerization modulation and antioxidant capabilities were evaluated and correlated with anthoxanthin attenuation of oligomer-induced intracellular reactive oxygen species (ROS) and caspase activation using human neuroblastoma cell treatments designed to isolate these mechanisms of action and to achieve dual-action...
November 18, 2016: CNS Neuroscience & Therapeutics
https://www.readbyqxmd.com/read/27863716/antibodies-against-the-c-terminus-of-%C3%AE-synuclein-modulate-its-fibrillation
#12
Cagla Sahin, Nikolai Lorenzen, Lasse Lemminger, Gunna Christiansen, Ian Max Møller, Louise Buur Vesterager, Lars Østergaard Pedersen, Karina Fog, Pekka Kallunki, Daniel E Otzen
The 140-residue natively disordered protein α-synuclein (aSN) is a central component in the development of a family of neurodegenerative diseases termed synucleinopathies. This is attributed to its ability to form cytotoxic aggregates such as oligomers and amyloid fibrils. Consequently there have been intense efforts to avoid aggregation or reroute the aggregation pathway using pharmaceutical agents such as small molecules, chaperones and antibodies. aSN's lack of persistent structure in the monomeric state, as well as the multitude of different oligomeric and even different fibrillar states, makes it difficult to raise antibodies that would be efficacious in neutralizing all conformations of aSN...
January 2017: Biophysical Chemistry
https://www.readbyqxmd.com/read/27861127/nec-1-alleviates-cognitive-impairment-with-reduction-of-a%C3%AE-and-tau-abnormalities-in-app-ps1-mice
#13
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...
November 17, 2016: EMBO Molecular Medicine
https://www.readbyqxmd.com/read/27856006/insights-into-the-aggregation-mechanism-of-a%C3%AE-25-40
#14
Jian Xiong, Renee D JiJi
The hydrophobic fragment of the Alzheimer's related β-amyloid (Aβ) peptide, Aβ(25-40), aggregates and forms insoluble amyloid fibrils at a rate similar to the full-length peptide. In order to gain insight into the fibrillization of Aβ(25-40) and the ability of the flavonoid myricetin to inhibit its aggregation, the isoleucine at position 32 (I32A) and the glycine at position 37 (G37A) in the full-length peptide were replaced with alanine. Thioflavin T assays indicate that substitution of isoleucine for alanine significantly reduces the rate and extent of fibrillization compared to the Aβ(25-40) and G37A peptides...
January 2017: Biophysical Chemistry
https://www.readbyqxmd.com/read/27853315/a%C3%AE-42-oligomers-modulate-%C3%AE-secretase-through-an-xbp-1s-dependent-pathway-involving-hrd1
#15
Yannis Gerakis, Julie Dunys, Charlotte Bauer, Fréderic Checler
The aspartyl protease β-site APP cleaving enzyme, BACE1, is the rate-limiting enzyme involved in the production of amyloid-β peptide, which accumulates in both sporadic and familial cases of Alzheimer's disease and is at the center of gravity of the amyloid cascade hypothesis. In this context, unravelling the molecular mechanisms controlling BACE1 expression and activity in both physiological and pathological conditions remains of major importance. We previously demonstrated that Aβ controlled BACE1 transcription in an NFκB-dependent manner...
November 17, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27852777/amyloid-%C3%AE-peptide-nitrotyrosination-stabilizes-oligomers-and-enhances-nmdar-mediated-toxicity
#16
Biuse Guivernau, Jaume Bonet, Victòria Valls-Comamala, Mònica Bosch-Morató, Juan A Godoy, Nibaldo C Inestrosa, Alex Perálvarez-Marín, Xavier Fernández-Busquets, David Andreu, Baldomero Oliva, Francisco J Muñoz
: Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the pathological aggregation of the amyloid-β peptide (Aβ). Monomeric soluble Aβ can switch from helicoidal to β-sheet conformation, promoting its assembly into oligomers and subsequently to amyloid fibrils. Oligomers are highly toxic to neurons and have been reported to induce synaptic transmission impairments. The progression from oligomers to fibrils forming senile plaques is currently considered a protective mechanism to avoid the presence of the highly toxic oligomers...
November 16, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/27844078/probing-oligomerization-of-amyloid-beta-peptide-in-silico
#17
L Dorosh, M Stepanova
Aggregation of amyloid β (Aβ) peptide is implicated in fatal Alzheimer's disease, for which no cure is available. Understanding the mechanisms responsible for this aggregation is required in order for therapies to be developed. In an effort to better understand the molecular mechanisms involved in spontaneous aggregation of Aβ peptide, extensive molecular dynamics simulations are reported, and the results are analyzed through a combination of structural biology tools and a novel essential collective dynamics method...
November 15, 2016: Molecular BioSystems
https://www.readbyqxmd.com/read/27834776/genetic-risk-as-a-marker-of-amyloid-%C3%AE-and-tau-burden-in-cerebrospinal-fluid
#18
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...
November 6, 2016: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/27830689/-isomerization-of-asp7-increases-the-toxic-effects-of-amyloid-%C3%AE-and-its-phosphorylated-form-in-sh-sy5y-neuroblastoma-cells
#19
E P Barykin, I Yu Petrushanko, K M Burnysheva, A A Makarov, V A Mitkevich
The generation of amyloid β (Aβ) toxic oligomers during the formation of senile plaques and amyloid fibrils is thought to play a central role in the onset and progression of Alzheimer's disease. Aβ production is a physiological process, but the factors that trigger a transition to pathogenic Aβ aggregation remain unknown. Posttranslational modifications of Aβ could potentially induce the transition. The effects of Aβ and its modified forms containing isomerized Asp7, phosphorylated Ser8, or both, were studied in SH-SY5Y human neuroblastoma cells...
September 2016: Molekuliarnaia Biologiia
https://www.readbyqxmd.com/read/27829339/improved-brain-expression-of-anti-amyloid-%C3%AE-scfv-by-complexation-of-mrna-including-a-secretion-sequence-with-peg-based-block-catiomer
#20
Federico Perche, Satoshi Uchida, Hiroki Akiba, Chin-Yu Lin, Masaru Ikegami, Anjaneyulu Dirisala, Toshihiro Nakashima, Keiji Itaka, Kohei Tsumoto, Kazunori Kataoka
Amyloid β aggregates have been proposed as central effectors in Alzheimer's disease, as evidenced by several passive immunotherapies in clinical trials. We used mRNA encoding anti-amyloid β (Aβ) scFv for passive immunotherapy. These scFvs could recognize amyloid oligomers with significant affinity, delay the aggregation of amyloid β in vitro, and dissociate Aβ aggregates in vitro. Intra-cerebroventricular injection of pDNA and mRNA encoding the scFv resulted in detectable scFv levels in the brain, with higher in vivo expression from mRNA...
November 8, 2016: Current Alzheimer Research
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