Results 61 to 70 of about 18,947 (293)
A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein
Nature CommunicationsReversible and irreversible amyloids are two diverging cases of protein (mis)folding associated with the cross-β motif in the protein folding and aggregation energy landscape.
Lukas Frey +13 more
doaj +1 more source
“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine
Molecules, 2020 Amyloid proteins are linked to the pathogenesis of several diseases including Alzheimer’s disease, but at the same time a range of functional amyloids are physiologically important in humans.
Sherin Abdelrahman +5 more
doaj +1 more source
An Amyloid Organelle: Solid State NMR Evidence for Cross-Beta Assembly of Gas Vesicles [PDF]
, 2011 Functional amyloids have been identified in a wide range of organisms, taking on a variety of biological roles and being controlled by remarkable mechanisms of directed assembly.
Bayro +35 more
core +1 more source
Systemic dysregulation of apolipoproteins in amyotrophic lateral sclerosis serum
FEBS Open Bio, EarlyView.Amyotrophic lateral sclerosis (ALS) is a fatal disease that damages motor neurons. This study found that people with ALS show significant changes in blood fats and the proteins that carry them. Several apolipoproteins were higher, lipid balances were altered, and normal protein–lipid relationships were disrupted.
Finula I. Isik +6 more
wiley +1 more source
Amyloids in bladder cancer hijack cancer-related proteins and are positive correlated to tumor stage
Scientific ReportsDespite the current diagnostic and therapeutic approaches to bladder cancer being widely accepted, there have been few significant advancements in this field over the past decades.
Diego Alem +13 more
doaj +1 more source
Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]
, 2017 The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M +2 more
core +2 more sources
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
Nanophotonics of protein amyloids
Nanophotonics, 2014 Technological breakthroughs in the super-resolution optical imaging techniques have enriched our current understanding of a range of biological systems and biomolecular processes at the nanoscopic spatial resolution.
Bhattacharya Mily, Mukhopadhyay Samrat
doaj +1 more source
Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity. [PDF]
, 2017 Peptide-based supramolecular assemblies are a promising class of nanomaterials with important biomedical applications, specifically in drug delivery and tissue regeneration.
Adler-Abramovich, Lihi +10 more
core +3 more sources
Journal of Internal Medicine, 2016 AbstractThere are around 30 human diseases associated with protein misfolding and amyloid formation, each one caused by a certain protein or peptide. Many of these diseases are lethal and together they pose an enormous burden to society. The prion protein has attracted particular interest as being shown to be the pathogenic agent in transmissible ...
L O, Tjernberg +4 more
openaire +2 more sources