Results 41 to 50 of about 11,568 (285)
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
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
Pharmaceutics, 2022 The coordination between histidine-rich peptides and divalent cations supports the formation of nano- and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems.
Julieta María Sánchez +10 more
doaj +1 more source
AmyPro: a database of proteins with validated amyloidogenic regions [PDF]
, 2017 Soluble functional proteins may transform into insoluble amyloid fibrils that deposit in a variety of tissues. Amyloid formation is a hallmark of age-related degenerative disorders.
De Baets, G. +4 more
core +1 more source
Biochemical, Cell Biological, and Genetic Assays to Analyze Amyloid and Prion Aggregation in Yeast [PDF]
, 2010 Protein aggregates are associated with a variety of debilitating human diseases, but they can have functional roles as well. Both pathological and nonpathological protein aggregates display tremendous diversity, with substantial differences in aggregate ...
Alberti, Simon +2 more
core +1 more source
Pathogens, 2022 Candida-macrophage interactions are important immune defense responses associated with disseminated and deep-seated candidiasis in humans. Cells of Candida spp.
Stephen A. Klotz +2 more
doaj +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
The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor. [PDF]
, 2017 Streptomyces bacteria form reproductive aerial hyphae that are covered with a pattern of pairwise aligned fibrils called rodlets. The presence of the rodlet layer requires two homologous rodlin proteins, RdlA and RdlB, and the functional amyloid chaplin ...
Claessen, Dennis +8 more
core +3 more sources
Failure of Aβ(1-40) amyloid fibrils under tensile loading [PDF]
, 2010 Amyloid fibrils and plaques are detected in the brain tissue of patients affected by Alzheimer’s disease, but have also been found as part of normal physiological processes such as bacterial adhesion.
Buehler, Markus J, Paparcone, Raffaella
core +1 more source
Scientific Reports, 2018 Here, we report that minimal functional gelsolin i.e. fragment 28–161 can display F-actin depolymerizing property even after heating the protein to 80 °C. Small angle X-ray scattering (SAXS) data analysis confirmed that under Ca2+-free conditions, 28–161
Maulik D. Badmalia +6 more
doaj +1 more source