Results 1 to 10 of about 11,568 (285)
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 ...
Leticia Matilla-Cuenca +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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New insight into the molecular control of bacterial functional amyloids [PDF]
Frontiers in Cellular and Infection Microbiology, 2015 Amyloid protein structure has been discovered in a variety of functional or pathogenic contexts. What distinguishes the former from the latter is that functional amyloid systems possess dedicated molecular control systems that determine the timing ...
Stephen eMatthews, Jonathan eTaylor
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Functional Mammalian Amyloids and Amyloid-Like Proteins [PDF]
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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Gene Regulation of Biofilm-Associated Functional Amyloids [PDF]
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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Functional Amyloids Are the Rule Rather Than the Exception in Cellular Biology [PDF]
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
doaj +2 more sources
Cold Spring Harb Perspect Biol, 2019 When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are usually associated with disease including Alzheimer's. However, amyloid has many useful features.
Otzen D, Riek R.
europepmc +5 more sources
Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids [PDF]
eLife, 2022 Synergistic-aggregation and cross-seeding by two different proteins/peptides in the amyloid aggregation are well evident in various neurological disorders including Alzheimer’s disease.
Debdeep Chatterjee +16 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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Functional Amyloids in Reproduction. [PDF]
Biomolecules, 2017 Amyloids are traditionally considered pathological protein aggregates that play causative roles in neurodegenerative disease, diabetes and prionopathies. However, increasing evidence indicates that in many biological systems nonpathological amyloids are formed for functional purposes.
Hewetson A +6 more
europepmc +4 more sources