Results 151 to 160 of about 288,605 (343)
ESC Heart Failure, Volume 12, Issue 2, Page 1326-1335, April 2025.Abstract Aims Amyloid cardiomyopathy is caused by the deposition of light chain (AL) or transthyretin amyloid (ATTR) fibrils, that leads to a restrictive cardiomyopathy, often resulting in heart failure (HF) with preserved or reduced ejection fraction.
Robin Willixhofer +25 more
wiley +1 more source
A compendium of extracellular vesicle biogenesis inhibitors: From bench to bedside
Interdisciplinary Medicine, EarlyView.This review explores a decade of research on extracellular vesicles (EVs), detailing their biogenesis and roles in health and disease. It emphasizes EVs' relevance for potential medical applications covering various conditions such as cancer, neurodegeneration, inflammation, and infectious diseases, bridging experimental findings with clinical ...
Stefano Vecchione +2 more
wiley +1 more source
Structural polymorphism of α-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation
The EMBO JournalPathological aggregation of α-synuclein into amyloid fibrils is a hallmark of synucleinopathies, including Parkinson’s disease. Despite this commonality, synucleinopathies display divergent disease phenotypes that have been attributed to disease-specific
Svenja Jäger +10 more
doaj +1 more source
Assessing the Catalytic Role of Native Glucagon Amyloid Fibrils
Glucagon stands out as a pivotal peptide hormone, instrumental in controlling blood glucose levels and lipid metabolism. While the formation of glucagon amyloid fibrils has been documented, their biological functions remain enigmatic.
Elad, Arad +4 more
core +1 more source
Journal of the Chinese Chemical Society, EarlyView.Model for how α‐syn modulates the positioning of endolysosomes in melanoma cells. (a) α‐syn tethers endolysosomes to the plasma membrane, a last step in anterograde transport. (b) Loss of α‐syn expression causes the loss of the tethering function, which leads to perinuclear vesicle clustering. Reproduced from the open access article.
Stephan N. Witt
wiley +1 more source
Nanomechanical Properties of Amyloid Fibrils Formed in a Water Nanofilm on Mica Surface
, 2016 The assessment of nanomechanical properties of a single amyloid fibril in a confined space provides important information for understanding the role of fibrils in a cell microenvironment.
Zhang, Gong-Jun +5 more
core
Journal of Clinical Laboratory Analysis, EarlyView.Schematic overview of the human microbiome and major microbiota‐derived metabolites across body sites, highlighting the gut–brain, gut–heart, and gut–kidney axes in host physiology and disease. ABSTRACT Background The human microbiome is a dynamic and diverse community of microorganisms that affects susceptibility to illness and promotes wellness ...
Awadh Alanazi
wiley +1 more source
Nanoscale Fluorescence Imaging of Single Amyloid Fibrils
, 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
Journal of the Science of Food and Agriculture, EarlyView.Abstract Neurodegenerative conditions such as Alzheimer's disease and Parkinson's disease are characterized by progressive neuronal loss driven by oxidative stress and inflammation. Quercetin, a dietary flavonoid with established antioxidant and anti‐inflammatory properties, has emerged as a potential neuroprotective agent.
In Ho Cho +6 more
wiley +1 more source