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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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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The Evolution of Functional Amyloids and Their Impact on Host–Microbe Interactions [PDF]
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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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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Protection against prolonged pneumococcal infection involves structural changes in C-reactive protein and subsequent binding to both phosphocholine and amyloids on the bacterial surface [PDF]
Frontiers in ImmunologyC-reactive protein (CRP) protects mice during the initial stages of Streptococcus pneumoniae infection. In order to be protective against all stages of infection, we hypothesize that CRP binds to two different ligands on pneumococci.
Alok Agrawal +3 more
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Search and Identification of Amyloid Proteins
Methods and Protocols, 2023 Amyloids are fibrillar proteins with a cross-β structure. Pathological amyloids are associated with the development of a number of incurable diseases, while functional amyloids regulate vital processes. The detection of unknown amyloids in living objects
Tatyana A. Belashova +5 more
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Functional Amyloids Are the Rule Rather Than the Exception in Cellular Biology
Microorganisms, 2020 Amyloids are a class of protein aggregates that have been historically characterized by their relationship with human disease. Indeed, amyloids can be the result of misfolded proteins that self-associate to form insoluble, extracellular plaques in ...
Anthony Balistreri +2 more
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Amyloid as a depot for the formulation of long-acting drugs. [PDF]
PLoS Biology, 2008 Amyloids are highly organized protein aggregates that are associated with both neurodegenerative diseases such as Alzheimer disease and benign functions like skin pigmentation. Amyloids self-polymerize in a nucleation-dependent manner by recruiting their
Samir K Maji +5 more
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Functional Mammalian Amyloids and Amyloid-Like Proteins
Life, 2020 Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD ...
Maria S. Rubel +6 more
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Anti-Biofilm Molecules Targeting Functional Amyloids
Antibiotics, 2021 The choice of an effective therapeutic strategy in the treatment of biofilm-related infections is a significant issue. Amyloids, which have been historically related to human diseases, are now considered to be prevailing structural components of the ...
Leticia Matilla-Cuenca +2 more
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