Results 31 to 40 of about 18,947 (293)
Viruses, 2019 The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc ...
Yuzuru Taguchi +2 more
doaj +1 more source
, 2012 Many bacteria can assemble functional amyloid fibers on their cell surface. The majority of bacterial amyloids contribute to biofilm or other community behaviors where cells interact with a surface or with another cell. Bacterial amyloids, like all functional amyloids, share structural and biochemical properties with disease-associated eukaryotic ...
Yizhou, Zhou +3 more
openaire +2 more sources
Direct Identification of Functional Amyloid Proteins by Label-Free Quantitative Mass Spectrometry
Biomolecules, 2017 Functional amyloids are important structural and functional components of many biofilms, yet our knowledge of these fascinating polymers is limited to a few examples for which the native amyloids have been isolated in pure form.
Heidi N. Danielsen +6 more
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Clinical Kidney Journal, 2014 Amyloidosis is an uncommon disease that is characterized by abnormal extracellular deposition of misfolded protein fibrils leading to organ dysfunction. The deposited proteins display common chemical and histologic properties but can vary dramatically in their origin. Kidney disease is a common manifestation in patients with systemic amyloidosis with a
Khalighi, Mazdak A. +2 more
openaire +2 more sources
Amyloid Fragmentation and Disaggregation in Yeast and Animals
Biomolecules, 2021 Amyloids are filamentous protein aggregates that are associated with a number of incurable diseases, termed amyloidoses. Amyloids can also manifest as infectious or heritable particles, known as prions. While just one prion is known in humans and animals,
Vitaly V. Kushnirov +2 more
doaj +1 more source
Molecular Basis of Orb2 Amyloidogenesis and Blockade of Memory Consolidation.
PLoS Biology, 2016 Amyloids are ordered protein aggregates that are typically associated with neurodegenerative diseases and cognitive impairment. By contrast, the amyloid-like state of the neuronal RNA binding protein Orb2 in Drosophila was recently implicated in memory ...
Rubén Hervás +15 more
doaj +1 more source
STITCHER: Dynamic assembly of likely amyloid and prion β-structures from secondary structure predictions [PDF]
, 2011 The supersecondary structure of amyloids and prions, proteins of intense clinical and biological interest, are difficult to determine by standard experimental or computational means.
Berger, Bonnie +5 more
core +1 more source
Amyloid and the origin of life : self-replicating catalytic amyloids as prebiotic informational and protometabolic entities [PDF]
, 2018 A crucial stage in the origin of life was the emergence of the first molecular entity that was able to replicate, transmit information, and evolve on the early Earth. The amyloid world hypothesis posits that in the pre-RNA era, information processing was
Maury, Carl Peter J.
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
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