Results 11 to 20 of about 14,195 (294)
Applied Biochemistry and Biotechnology, 2012 The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease.
Pulawski W +3 more
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Gene Regulation of Biofilm-Associated Functional Amyloids
Pathogens, 2021 Biofilms are bacterial communities encased in a rigid yet dynamic extracellular matrix. The sociobiology of bacterial communities within a biofilm is astonishing, with environmental factors playing a crucial role in determining the switch from planktonic
Khushal Khambhati +4 more
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Catalytically Active Amyloids as Future Bionanomaterials
Nanomaterials, 2022 Peptides and proteins can aggregate into highly ordered and structured conformations called amyloids. These supramolecular structures generally have convergent features, such as the formation of intermolecular beta sheets, that lead to fibrillary ...
Rodrigo Diaz-Espinoza
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Amyloids: The History of Toxicity and Functionality
Biology, 2021 Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures such ...
Elmira I. Yakupova +4 more
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The Evolution of Functional Amyloids and Their Impact on Host–Microbe Interactions
Advanced ScienceAmyloids are highly ordered β‐sheet‐rich structures that are well conserved across the domains of life. Amyloids have a unique repetitive structure that enables autocatalytic self‐replication.
Divya Kolli +3 more
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Alpha-synuclein amyloids catalyze the degradation of ATP and other nucleotides [PDF]
Scientific ReportsIntracellular accumulation of alpha-synuclein amyloids is a main pathological hallmark in a subgroup of human neurodegenerative diseases called synucleinopathies.
Claudio Castillo-Cáceres +2 more
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Why are Functional Amyloids Non-Toxic in Humans? [PDF]
Biomolecules, 2017 Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in ...
Matthew P. Jackson, Eric W. Hewitt
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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
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ATP Hydrolysis by α‐Synuclein Amyloids is Mediated by Enclosing β‐Strand [PDF]
Advanced SciencePathological amyloids, like those formed by α‐synuclein in Parkinson's disease, are recently found to catalyze the hydrolysis of model substrates in vitro.
Lukas Frey +6 more
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AmyloGraph: a comprehensive database of amyloid–amyloid interactions
Nucleic Acids Research, 2022 Abstract Information about the impact of interactions between amyloid proteins on their fibrillization propensity is scattered among many experimental articles and presented in unstructured form. We manually curated information located in almost 200 publications (selected out of 562 initially considered), obtaining details of 883 ...
Michal Burdukiewicz +14 more
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