Search Results - "Tavassoly, Omid"
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Inhibition of Brain Epidermal Growth Factor Receptor Activation: A Novel Target in Neurodegenerative Diseases and Brain Injuries
Published in Molecular pharmacology (01-07-2020)Get full text
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Pharmacological Inhibition of Brain EGFR Activation By a BBB-penetrating Inhibitor, AZD3759, Attenuates α-synuclein Pathology in a Mouse Model of α-Synuclein Propagation
Published in Neurotherapeutics (01-04-2021)“…Aggregation and deposition of α-synuclein (α-syn) in Lewy bodies within dopamine neurons of substantia nigra (SN) is the pathological hallmark of Parkinson’s…”
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A light-inducible protein clustering system for in vivo analysis of α-synuclein aggregation in Parkinson disease
Published in PLoS biology (01-03-2022)“…Neurodegenerative disorders refer to a group of diseases commonly associated with abnormal protein accumulation and aggregation in the central nervous system…”
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Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations
Published in Open biology (01-01-2018)“…The accumulation of various metabolites appears to be associated with diverse human diseases. However, the aetiological link between metabolic alteration and…”
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Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins
Published in Prion (01-04-2012)“…Nanopore analysis is an emerging technique that enables the investigation of the conformation of a single peptide or protein molecule. Briefly, a pore is…”
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Heparin-binding Peptides as Novel Therapies to Stop SARS-CoV-2 Cellular Entry and Infection
Published in Molecular pharmacology (01-11-2020)“…Heparan sulfate proteoglycans (HSPGs) are cell surface receptors that are involved in the cellular uptake of pathologic amyloid proteins and viruses, including…”
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EGFR Aggregation in the Brain
Published in ACS chemical neuroscience (02-06-2021)“…Recent findings showed that preformed fibrils (PFFs) of misfolded proteins, including α-synuclein (α-syn) and amyloid-β (Aβ), activate EGFR in cell cultures…”
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Seeding Brain Protein Aggregation by SARS-CoV‑2 as a Possible Long-Term Complication of COVID-19 Infection
Published in ACS chemical neuroscience (18-11-2020)“…Postinfection complications of coronavirus disease 2019 (COVID-19) are still unknown, and one of the long-term concerns in infected people are brain…”
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Pharmacological inhibition and knockdown of O‐GlcNAcase reduces cellular internalization of α‐synuclein preformed fibrils
Published in The FEBS journal (01-01-2021)“…The pathological hallmark of Parkinson's disease (PD) is Lewy bodies that form within the brain from aggregated forms of α‐synuclein (α‐syn). These toxic α‐syn…”
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Pharmacological Functionalization of Protein-Based Nanorobots as a Novel Tool for Drug Delivery in Cancer
Published in ACS pharmacology & translational science (13-08-2021)“…The delivery of hydrophobic therapeutic agents to tumors is a challenge in the treatment of cancers. Here, we review recent advances in coiled-coil protein…”
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Quinolinic Acid Amyloid-like Fibrillar Assemblies Seed α-Synuclein Aggregation
Published in Journal of molecular biology (12-10-2018)“…Quinolinic acid (QA), a downstream neurometabolite in the kynurenine pathway, the biosynthetic pathway of tryptophan, is associated with neurodegenerative…”
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Methamphetamine binds to α-synuclein and causes a conformational change which can be detected by nanopore analysis
Published in FEBS letters (21-09-2012)“…► α-Synuclein translocates the α-hemolysin pore. ► In the presence of methamphetamine the proportion of translocation events is decreased. ► A conformational…”
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Cu(II) and dopamine bind to α‐synuclein and cause large conformational changes
Published in The FEBS journal (01-06-2014)“…α‐Synuclein (AS) is an intrinsically disordered protein that can misfold and aggregate to form Lewy bodies in dopaminergic neurons, a classic hallmark of…”
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The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease
Published in European journal of medicinal chemistry (17-12-2014)“…A major feature of Parkinson's disease is the formation of Lewy bodies in dopaminergic neurons which consist of misfolded α-synuclein. The binding of natural…”
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SMPD1 mutations, activity, and α‐synuclein accumulation in Parkinson's disease
Published in Movement disorders (01-04-2019)“…Background SMPD1 (acid‐sphingomyelinase) variants have been associated with Parkinson's disease in recent studies. The objective of this study was to further…”
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Inhibition of Brain EGFR Activation: A Novel Target in Neurodegenerative Diseases and Brain Injuries
Published in Molecular pharmacology (29-04-2020)“…Several reports have been published recently demonstrating a beneficial effect of epidermal growth factor receptor (EGFR) inhibitors in improving pathological…”
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Rasagiline, a Suicide Inhibitor of Monoamine Oxidases, Binds Reversibly to α‑Synuclein
Published in ACS chemical neuroscience (18-02-2015)“…Rasagiline (N-propargyl-1-R-aminoindan) and selegiline (1-deprenyl) are MAO-B inhibitors which are used in the treatment of Parkinson’s disease. The binding of…”
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A light-inducible protein clustering system for in vivo analysis of [alpha]-synuclein aggregation in Parkinson disease
Published in PLoS biology (09-03-2022)“…Neurodegenerative disorders refer to a group of diseases commonly associated with abnormal protein accumulation and aggregation in the central nervous system…”
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Cu(II) and dopamine bind to [alpha]-synuclein and cause large conformational changes
Published in The FEBS journal (01-06-2014)“…[alpha]-Synuclein (AS) is an intrinsically disordered protein that can misfold and aggregate to form Lewy bodies in dopaminergic neurons, a classic hallmark of…”
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Chaos game representation of mitochondrial DNA: is it useful in phylogenetic studies?
Published in BMC systems biology (08-05-2007)Get full text
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