Results 111 to 120 of about 160,241 (252)

Injectable Peptide‐Based Functional Amyloid Hydrogels as Tunable Depots for Sustained Drug Delivery

open access: yesAdvanced Science, EarlyView.
An injectable and tunable peptide‐based functional amyloid hydrogel provides sustained insulin release while preserving insulin stability and bioactivity. The hydrogel enables prolonged glycemic regulation in vivo, exhibits excellent biocompatibility, and shows no detectable IAPP and α‐Syn heterologous cross‐seeding, highlighting its potential as a ...
Ranjit Shaw   +4 more
wiley   +1 more source

Amyloid‐Guided Assembly of Magnetically Recyclable Enzymatic Nanofibers Toward Sustainable Biocatalysis

open access: yesAdvanced Science, EarlyView.
A hierarchical strategy integrates linker engineering, amyloid‐guided self‐assembly, and magnetic immobilization to construct recyclable DPAO4‐DMAO7 enzymatic nanofibers. The resulting magnetic composites enable biogenic amine conversion in complex food matrices and simulated wastewater, while rapid magnetic separation supports repeated reuse. The work
Shuangping Liu   +5 more
wiley   +1 more source

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.   +3 more
core   +1 more source

Outcomes of Patients With AL Amyloidosis and End‐Stage Renal Disease After Initiation of Therapy

open access: yesAmerican Journal of Hematology, EarlyView.
ABSTRACT In AL amyloidosis, advanced renal disease can impact treatment options and cause significant morbidity. Patients with ESRD requiring dialysis are a group with currently unmet needs. In this collaborative study, we identified 362 patients from three European centers who initiated dialysis during the course of the disease.
Foteini Theodorakakou   +10 more
wiley   +1 more source

Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins

open access: yesNature Communications
Amyloid fibrils are highly ordered protein assemblies characterized by a cross-β architecture. A wide range of proteins can adopt amyloid states, contributing to both disease-related pathology and normal physiological function.
Yiling Zhang   +13 more
doaj   +1 more source

Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue

open access: yesNature Communications, 2019
Alzheimer’s disease is characterised by the deposition of Aβ amyloid fibrils and tau protein neurofibrillary tangles. Here the authors use cryo-EM to structurally characterise brain derived Aβ amyloid fibrils and find that they are polymorphic and right ...
Marius Kollmer   +9 more
doaj   +1 more source

Polymorphism of Alzheimer’s Aβ Amyloid Fibrils and Oligomers

open access: yes, 2017
An overview of the strategy and experimental solid-state NMR, STEM, and AFM methods useful for obtaining structural constraints on Alzheimer’s amyloid-β peptide fibrils is presented.
Antzutkin, Oleg,, Oleg N. Antzutkin
core   +1 more source

Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils

open access: yesScientific Reports, 2017
Fluorescence of thioflavin T (ThT) is a proven tool for amyloid fibrils study. The correct model of ThT binding to fibrils is crucial to clarify amyloid fibrils structure and mechanism of their formation.
Anna I. Sulatskaya   +4 more
doaj   +1 more source

Nanoscale Fluorescence Imaging of Single Amyloid Fibrils

open access: yes, 2015
Amyloid formation is implicated in a variety of human diseases. It is important to perform high-resolution optical imaging of individual amyloid fibrils to delineate the structural basis of supramolecular protein assembly. However, amyloid fibrils do not
Samrat Mukhopadhyay (500272)   +4 more
core   +1 more source

Amyloid Fibrils: Potential Food Safety Implications [PDF]

open access: yes, 2008
The demonstration of oral Amyloid-A (AA) fibril transmissibility has raised food safety questions about the consumption of amyloidotic viscera. In a presumed prion-like mechanism, amyloid fibrils have been shown to trigger and accelerate the development ...
Greger, Michael
core   +2 more sources

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