Analysis of amyloid aggregates using agarose gel electrophoresis.
about
Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentationA systematic survey identifies prions and illuminates sequence features of prionogenic proteinsNew insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautionsThe NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotypeModulation of Mitochondrial Antiviral Signaling by Human Herpesvirus 8 Interferon Regulatory Factor 1Interaction of Prions Causes Heritable Traits in Saccharomyces cerevisiaeAggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast modelSUMOylation Is an Inhibitory Constraint that Regulates the Prion-like Aggregation and Activity of CPEB3Determinants of Amyloid Formation for the Yeast Termination Factor Nab3Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieusDe novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Modulation of Abeta42 low-n oligomerization using a novel yeast reporter systemHeterologous prion interactions are altered by mutations in the prion protein Rnq1p.Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.Small molecule microarrays enable the discovery of compounds that bind the Alzheimer's Aβ peptide and reduce its cytotoxicity.Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast.Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Conversion of a yeast prion protein to an infectious form in bacteriaLow activity of select Hsp104 mutants is sufficient to propagate unstable prion variantsPrion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Identification of PrP sequences essential for the interaction between the PrP polymers and Aβ peptide in a yeast-based assayIncreasing prion propensity by hydrophobic insertion.Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selectionLocalization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component.An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicityAmyloid-like assembly of the low complexity domain of yeast Nab3.Prions in yeast.The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.Study of amyloids using yeastStrain conformation, primary structure and the propagation of the yeast prion [PSI+].Generating extracellular amyloid aggregates using E. coli cells.[PSI(+) ] prion variant establishment in yeastA yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity.Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein compositionStudying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.
P2860
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P2860
Analysis of amyloid aggregates using agarose gel electrophoresis.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Analysis of amyloid aggregates using agarose gel electrophoresis.
@ast
Analysis of amyloid aggregates using agarose gel electrophoresis.
@en
Analysis of amyloid aggregates using agarose gel electrophoresis.
@nl
type
label
Analysis of amyloid aggregates using agarose gel electrophoresis.
@ast
Analysis of amyloid aggregates using agarose gel electrophoresis.
@en
Analysis of amyloid aggregates using agarose gel electrophoresis.
@nl
prefLabel
Analysis of amyloid aggregates using agarose gel electrophoresis.
@ast
Analysis of amyloid aggregates using agarose gel electrophoresis.
@en
Analysis of amyloid aggregates using agarose gel electrophoresis.
@nl
P1476
Analysis of amyloid aggregates using agarose gel electrophoresis.
@en
P2093
Sviatoslav N Bagriantsev
Vitaly V Kushnirov
P356
10.1016/S0076-6879(06)12003-0
P407
P577
2006-01-01T00:00:00Z