Results 1 to 10 of about 13,480 (279)
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.
Slawomir Filipek +2 more
exaly +4 more sources
Anti-Biofilm Molecules Targeting Functional Amyloids [PDF]
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 ...
Alejandro Toledo-Arana +2 more
exaly +4 more sources
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 ...
Matthew Chapman, Anthony Balistreri
exaly +4 more sources
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 ...
Eric Hewitt
exaly +4 more sources
Alpha-synuclein amyloids catalyze the degradation of ATP and other nucleotides. [PDF]
Sci RepIntracellular accumulation of alpha-synuclein amyloids is a main pathological hallmark in a subgroup of human neurodegenerative diseases called synucleinopathies.
Castillo-Cáceres C +2 more
europepmc +2 more sources
The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions. [PDF]
Adv Sci (Weinh)Amyloids 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.
Kolli D, Rout SK, Riek R, Chapman MR.
europepmc +2 more sources
ATP Hydrolysis by α-Synuclein Amyloids is Mediated by Enclosing β-Strand. [PDF]
Adv Sci (Weinh)Pathological amyloids, like those formed by α‐synuclein in Parkinson's disease, are recently found to catalyze the hydrolysis of model substrates in vitro.
Frey L +6 more
europepmc +2 more sources
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
doaj +1 more source
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
openaire +6 more sources
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
doaj +1 more source