Results 91 to 100 of about 288,605 (343)

Polymorphism of amyloid-ß fibrils and its effects on human erythrocyte catalase binding

open access: yes, 2009
The Alzheimer's amyloid-β (Aβ) peptide exists as a number of naturally occurring forms due to differential proteolytic processing of its precursor molecule.
Harris, J.R., Milton, N.G.N.
core   +1 more source

Orthogonal Ionic Liquid‐Based Extraction Strategy Enables Amyloid‐Specific Profiling of Aggregate Proteome

open access: yesAdvanced Science, EarlyView.
An orthogonal ionic‐liquid extraction (Orth‐iEA) enables selective isolation of amyloid fibrils. TMGBF4 disrupts hydrogen‐bonded β‐sheet networks to solubilize amyloid aggregates, whereas C12ImCl interacts with hydrophobic regions of non‐amyloid proteins.
Shiying Zheng   +10 more
wiley   +1 more source

Water‐Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils

open access: yesAngewandte Chemie, EarlyView.
Extended 1D phosphoryl “wires” stabilize in‐register amyloid tau fibrils, as demonstrated by multiple‐quantum spin‐counting NMR, TEM, and MD simulations, using fibrils of tau peptide jR2R3‐P301L (tau295–313) with phosphorylation at S305 or Y310. ABSTRACT Hyperphosphorylation of tau is a hallmark of tauopathies, with specific phosphorylation sites ...
Lokeswara Rao Potnuru   +8 more
wiley   +2 more sources

UV-light exposed prion protein fails to form amyloid fibrils. [PDF]

open access: yesPLoS ONE, 2008
Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. We have investigated amyloidogenesis using prion protein as a model system and UV-light as a structural perturbant.
Abhay Kumar Thakur, Ch Mohan Rao
doaj   +1 more source

Self-assembling nanomaterials: Monitoring the formation of amyloid fibrils, with a focus on small-angle x-ray scattering

open access: yes, 2013
Amyloid fibrils are attractive targets for applications in biotechnology. These thin, nanoscale protein fibers are highly ordered structures that self-assemble from their component proteins or peptides.
Sawyer, E.B., Gras, S.L.
core   +1 more source

Lilrb4a Suppression Reprograms Microglia to Mitigate APOE4‐Associated Amyloid Plaques and Cerebral Amyloid Angiopathy in Association With a PPAR‐Linked Pro‐Clearance State

open access: yesAdvanced Science, EarlyView.
Targeting Lilrb4a in Apolipoprotein E4 (APOE4)‐associated Alzheimer's disease (AD) reprograms microglia toward a beneficial, phagocytic state. Genetic deletion or antisense inhibition of Lilrb4a suppresses p‐SHP2/NF‐κB/STAT1 signaling, restores PPAR‐linked lipid and energy metabolism, and reduces amyloid plaque burden and cerebral amyloid angiopathy ...
Changxu Nie   +12 more
wiley   +1 more source

Post‐Translational Isoaspartate Promotes Amyloid Formation in β2‐Microglobulin

open access: yesAngewandte Chemie, EarlyView.
Chemical synthesis of five β2‐microglobulin (β2m) variants reveals the structural impact of Asn deamidation. By introducing Asp or isoAsp at susceptible Asn‐Gly sequences, we demonstrate that isoAsp17 formation specifically accelerates amyloid fibril formation, highlighting its potential contribution to dialysis‐related amyloidosis.
Ryuji Kawakami   +5 more
wiley   +2 more sources

Structural basis for amyloid fibril assembly by the master cell-signaling regulator receptor-interacting protein kinase 1

open access: yesNature Communications
Amyloid fibrils can form biologically relevant functional assemblies. The RIP homotypic interaction motifs (RHIMs) in receptor-interacting protein kinases 1 and 3 (RIPK1 and RIPK3) orchestrate the formation of amyloid-like fibrils essential for ...
Paula Polonio   +7 more
doaj   +1 more source

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration

open access: yesCell Reports, 2015
The accumulation of amyloid-β (Aβ) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer’s disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects ...
Peng Liu   +13 more
doaj   +1 more source

Preparation of Amyloid Fibril Networks

open access: yesBIO-PROTOCOL, 2018
Networks of amyloid nanofibrils fabricated from common globular proteins such as lysozyme and β-lactoglobulin have material properties that mimic the extracellular microenvironment of many cell types. Cells cultured on such amyloid fibril networks show improved attachment, spreading and in the case of mesenchymal stem cells improved differentiation ...
Charnley, Mirren   +3 more
openaire   +5 more sources

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