fcspp evaluation software version 2.0 (Evotec Inc)
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Evotec Inc
fcspp evaluation software version 2.0
Fcspp Evaluation Software Version 2.0, supplied by Evotec Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fcspp+evaluation+software+version+2%2E0/fcspp+evaluation+software+version+2+0/pmc06591385-224-11-16
Average 90 stars, based on 1 article reviews
Fcspp Evaluation Software Version 2.0, supplied by Evotec Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fcspp+evaluation+software+version+2%2E0/fcspp+evaluation+software+version+2+0/pmc06591385-224-11-16
Average 90 stars, based on 1 article reviews
fcspp evaluation software version 2.0 - by Bioz Stars,
2026-09
90/100 stars
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Fluorescence:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Article Title: CADASIL mutations enhance spontaneous multimerization of NOTCH3. Article Snippet: Data of FIDA measurements were analyzed with Article Title: Generation of Ferric Iron Links Oxidative Stress to α-Synuclein Oligomer Formation Article Snippet: Background: Synucleinopathies such as Parkinson’s disease are characterized by the deposition of aggregated -synuclein in affected brain areas.. As genes involved in mitochondrial function, mitochondrial toxins, and age-related mitochondrial impairment have been implicated in Parkinson’s disease pathogenesis, an increase in reactive oxygen species resulting from mitochondrial dysfunction has been speculated to induce -synuclein aggregation.. In vitro, pore-forming, SDS-resistant -synuclein oligomers are formed in presence of ferric iron and may represent an important toxic particle species. Article Title: Divergent Molecular Effects of Desmin Mutations on Protein Assembly in Myofibrillar Myopathy Article Snippet: Mutations in the intermediate filament protein desmin cause a distinct class of myofibrillar myopathies that are characterized by deposition of aggregated desmin.. To assess the effect of different disease-associated mutations at the molecular level, we applied confocal single-particle fluorescence spectroscopy.. We studied the de novo aggregation properties of desmin in vitro and the aggregation state of desmin in homogenates of transfected cells rendering purification unnecessary. Article Title: Iron-mediated aggregation and toxicity in a novel neuronal cell culture model with inducible alpha-synuclein expression Article Snippet: Data were analysed by fluorescence intensity distribution analysis (FIDA) using the Article Title: AMPA-receptor-mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers. Article Snippet: All measurements were performed at 22 C. For FIDA the fluorescence data were evaluated by using the Article Title: Co-aggregate formation of CADASIL-mutant NOTCH3: a single-particle analysis. Article Snippet: Data of FCS measurements were analyzed with the Software:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Article Title: CADASIL mutations enhance spontaneous multimerization of NOTCH3. Article Snippet: Data of FIDA measurements were analyzed with Article Title: Generation of Ferric Iron Links Oxidative Stress to α-Synuclein Oligomer Formation Article Snippet: Background: Synucleinopathies such as Parkinson’s disease are characterized by the deposition of aggregated -synuclein in affected brain areas.. As genes involved in mitochondrial function, mitochondrial toxins, and age-related mitochondrial impairment have been implicated in Parkinson’s disease pathogenesis, an increase in reactive oxygen species resulting from mitochondrial dysfunction has been speculated to induce -synuclein aggregation.. In vitro, pore-forming, SDS-resistant -synuclein oligomers are formed in presence of ferric iron and may represent an important toxic particle species. Article Title: Divergent Molecular Effects of Desmin Mutations on Protein Assembly in Myofibrillar Myopathy Article Snippet: Mutations in the intermediate filament protein desmin cause a distinct class of myofibrillar myopathies that are characterized by deposition of aggregated desmin.. To assess the effect of different disease-associated mutations at the molecular level, we applied confocal single-particle fluorescence spectroscopy.. We studied the de novo aggregation properties of desmin in vitro and the aggregation state of desmin in homogenates of transfected cells rendering purification unnecessary. Article Title: Iron-mediated aggregation and toxicity in a novel neuronal cell culture model with inducible alpha-synuclein expression Article Snippet: Data were analysed by fluorescence intensity distribution analysis (FIDA) using the Article Title: AMPA-receptor-mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers. Article Snippet: All measurements were performed at 22 C. For FIDA the fluorescence data were evaluated by using the Article Title: Co-aggregate formation of CADASIL-mutant NOTCH3: a single-particle analysis. Article Snippet: Data of FCS measurements were analyzed with the |