Results 101 to 110 of about 75,180 (286)
The 10B‐enriched monocarbonyl analog of curcumin (BMAC) 10B‐9 enables site‐specific Boron Neutron Capture Therapy (BNCT) on amyloid‐β (Aβ) fibrils. Neutron irradiation induces histidine oxidation and fibril destabilization, as revealed by 1H‐NMR and FESEM analyses.
Sebastiano Micocci +12 more
wiley +1 more source
The question of strains in AA amyloidosis
The existence of transmissible amyloid fibril strains has long intrigued the scientific community. The strain theory originates from prion disorders, but here, we provide evidence of strains in systemic amyloidosis.
Gunilla T. Westermark +5 more
doaj +1 more source
Toxic species in amyloid disorders: Oligomers or mature fibrils
Protein aggregation is the hallmark of several neurodegenerative disorders. These protein aggregation (fibrillization) disorders are also known as amyloid disorders. The mechanism of protein aggregation involves conformation switch of the native protein,
Meenakshi Verma +2 more
doaj +1 more source
Preparation of Amyloid Fibril Networks
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
Living Hydrogels: Harnessing Microorganism–Material Synergy for Next‐Generation Therapeutics
. ABSTRACT Microorganism‐based therapies, particularly those utilizing probiotics, have emerged as a powerful biomedical strategy owing to their inherent living functionalities. These living systems can dynamically interact with host environments and self‐regulate their activity, offering superior adaptability, prolonged functionality, and ...
Shuifang Mao +3 more
wiley +1 more source
Background Immunoglobulin heavy-and-light-chain amyloidosis (AHL amyloidosis) is a newly established disease entity where both the immunoglobulin heavy-chain and light-chain compose amyloid fibrils. The immunoglobulins responsible for the amyloid fibrils
Shun Manabe +6 more
doaj +1 more source
Molecular recycling within amyloid fibrils
Amyloid fibrils are thread-like protein aggregates with a core region formed from repetitive arrays of beta-sheets oriented parallel to the fibril axis. Such structures were first recognized in clinical disorders, but more recently have also been linked to a variety of non-pathogenic phenomena ranging from the transfer of genetic information to ...
Carulla, N +8 more
openaire +3 more sources
The 3K‐AP system forms infinite supramolecular fibrils that undergo controlled degradation into shorter fragments upon enzymatic hydrolysis. Multitechnique imaging reveals a stepwise bacteriolytic mechanism involving bacterial entrapment, disassembly into lethal constructs, and associated extracellular vesicle release, highlighting the dynamic ...
Sohini Chakraborty +21 more
wiley +1 more source
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞
Serum amyloid P (SAP) is a common component of human amyloid deposits and has been identified in atherosclerotic lesions. We investigated the extent of the colocalization of SAP with apolipoprotein A-I (apoA-I), apoB, apoC-II, and apoE in human coronary ...
Cameron R. Stewart +8 more
doaj +1 more source
Structure of amyloid-β (20-34) with Alzheimer's-associated isomerization at Asp23 reveals a distinct protofilament interface. [PDF]
Amyloid-β (Aβ) harbors numerous posttranslational modifications (PTMs) that may affect Alzheimer's disease (AD) pathogenesis. Here we present the 1.1 Å resolution MicroED structure of an Aβ 20-34 fibril with and without the disease-associated PTM, L ...
Boyer, David R +8 more
core

