Results 41 to 50 of about 18,838 (278)
Cold Spring Harbor Perspectives in Biology, 2019 When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are usually associated with disease including Alzheimer's. However, amyloid has many useful features.
Otzen, Daniel, Riek, Roland
openaire +3 more sources
Setting the Stage for Insulin Granule Dysfunction during Type-1-Diabetes: Is ER Stress the Culprit?
Biomedicines, 2022 Type-1-diabetes (T1D) is a multifactorial disorder with a global incidence of about 8.4 million individuals in 2021. It is primarily classified as an autoimmune disorder, where the pancreatic β-cells are unable to secrete sufficient insulin.
Aishwarya A. Makam +3 more
doaj +1 more source
Nanostructure and stability of calcitonin amyloids [PDF]
, 2017 Calcitonin is a 32-amino acid thyroid hormone that can form amyloid fibrils. The structural basis of the fibril formation and stabilization is still debated and poorly understood.
Gautieri, Alfonso +3 more
core +1 more source
Accumulation of storage proteins in plant seeds is mediated by amyloid formation.
PLoS Biology, 2020 Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital functions in archaea ...
Kirill S Antonets +19 more
doaj +1 more source
Tau acetylation at K331 has limited impact on tau pathology in vivo
FEBS Letters, EarlyView.We mapped tau post‐translational modifications in humanized MAPT knock‐in mice and in amyloid‐bearing double knock‐in mice. Acetylation within the repeat domain, particularly around K331, showed modest increases under amyloid pathology. To test functional relevance, we generated MAPTK331Q knock‐in mice.
Shoko Hashimoto +3 more
wiley +1 more source
\u3cem\u3eDe Novo\u3c/em\u3e [PSI\u3csup\u3e+\u3c/sup\u3e] Prion Formation Involves Multiple Pathways to Form Infectious Oligomers [PDF]
, 2017 Prion and other neurodegenerative diseases are associated with misfolded protein assemblies called amyloid. Research has begun to uncover common mechanisms underlying transmission of amyloids, yet how amyloids form in vivo is still unclear. Here, we take
Manogaran, Anita L. +5 more
core +1 more source
Blessings in disguise: biological benefits of prion-like mechanisms [PDF]
, 2013 Prions and amyloids are often associated with disease, but related mechanisms provide beneficial functions in nature. Prion-like mechanisms (PriLiMs) are found from bacteria to humans, where they alter the biological and physical properties of prion-like
Lindquist, Susan, Newby, Gregory Arthur
core +1 more source
, 2018 Many bacteria can assemble functional amyloid fibers on their cell surface. Most bacterial amyloids contribute to biofilm or other community behaviors where cells interact with a surface or with other cells. Bacterial amyloids, like all functional amyloids, share structural and biochemical properties with disease-associated eukaryotic amyloids.
Margery L, Evans +3 more
openaire +2 more sources
Gut microbiome and aging—A dynamic interplay of microbes, metabolites, and the immune system
FEBS Letters, EarlyView.Age‐dependent shifts in microbial communities engender shifts in microbial metabolite profiles. These in turn drive shifts in barrier surface permeability of the gut and brain and induce immune activation. When paired with preexisting age‐related chronic inflammation this increases the risk of neuroinflammation and neurodegenerative diseases.
Aaron Mehl, Eran Blacher
wiley +1 more source
Frontiers in Immunology, 2020 Pathological self-assembly is a concept that is classically associated with amyloids, such as amyloid-β (Aβ) in Alzheimer's disease and α-synuclein in Parkinson's disease.
Ernest Y. Lee +8 more
doaj +1 more source