Results 61 to 70 of about 288,605 (343)
Enzyme-induced Formation of ß-Lactoglobulin Fibrils by AspN Endoproteinase
, 2008 This paper describes a low temperature, enzymatic route to induce fibrillar structures in a protein solution. The route comprises two steps. First, ß-lactoglobulin was hydrolyzed into peptides at pH 8 and 37°C with the enzyme AspN endoproteinase, which ...
Venema, P. +4 more
core +1 more source
Zinc–dysprosium functionalized amyloid fibrils [PDF]
Dalton Transactions, 2019 The heterometallic Zn2Dy2 entity bearing partially saturated metal centres covalently decorates a highly ordered amyloid fibril core and the functionalised assembly exhibits catalytic Lewis acid behaviour.
Stavroula I. Sampani +4 more
openaire +3 more sources
Fibril Fragmentation Enhances Amyloid Cytotoxicity [PDF]
, 2009 Fibrils associated with amyloid disease are molecular assemblies of key biological importance, yet how cells respond to the presence of amyloid remains unclear. Cellular responses may not only depend on the chemical composition or molecular properties of
Xue, Wei-Feng +5 more
core +1 more source
FEBS Open Bio, EarlyView.Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source
Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils
Journal of the American Chemical Society, 2016 Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that are a hallmark of Alzheimer’s disease (AD).
Michael T. Colvin +10 more
semanticscholar +1 more source
FEBS Open Bio, EarlyView.Repair of neuronal DNA damage in Alzheimer's disease by KCL‐286. (A) Amyloid‐β oligomers and plaques impair neuronal DNA repair pathways, leading to DNA double‐strand breaks and glial activation. (B) KCL‐286 activates RARβ/RXR signalling via retinoic acid response elements (RAREs), associated with increased BRCA1 expression, enhanced DNA repair and ...
Natasha Hill +6 more
wiley +1 more source
Mechanisms and rates of nucleation of amyloid fibrils [PDF]
The Journal of Chemical Physics, 2017 The classical nucleation theory finds the rate of nucleation proportional to the monomer concentration raised to the power, which is the “critical nucleus size,” nc. The implicit assumption, that amyloids nucleate in the same way, has been recently challenged by an alternative two-step mechanism, when the soluble monomers first form a metastable ...
Cheng-Tai Lee, Eugene M. Terentjev
openaire +3 more sources
The growth of amyloid fibrils: rates and mechanisms.
Biochemical Journal, 2019 Amyloid fibrils are β-sheet-rich linear protein polymers that can be formed by a large variety of different proteins. These assemblies have received much interest in recent decades, due to their role in a range of human disorders.
Alexander K. Buell
semanticscholar +1 more source
Initiation and spreading of Tau pathology. is β-Amyloid the only key? [PDF]
, 2009 Neurodegenerative diseases associated with dementia affect 5-10 % of individuals over the age of 65 in the Western world and represent one of the main health-related socioeconomic burdens.
Clavaguera, Florence
core +1 more source
Photothermal‐Activated Antibacterial Amyloid‐Polyphenol‐Iron Hydrogels for Synergistic Wound Healing
Advanced Healthcare Materials, EarlyView.We report a thermally triggered supramolecular hydrogel (LTFe) formed by Fe3+ and tannic acid on lysozyme amyloid fibrils. Fe3+ enables rapid gelation and photothermal transduction with an efficiency of 88.56%. The LTFe hydrogel exhibits excellent biocompatibility, potent antibacterial activity against E. coli and S.
Di Wu +8 more
wiley +1 more source