Functional Amyloids Signal Their Arrival [PDF]
Science Signaling, 2009 Several peptide and protein hormones are stored in an amyloid configuration in secretory granules.
Matthew P, Badtke +2 more
openaire +2 more sources
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology [PDF]
, 2017 Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as
Arosio, Paolo +6 more
core +1 more source
“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine
Molecules, 2020 Amyloid proteins are linked to the pathogenesis of several diseases including Alzheimer’s disease, but at the same time a range of functional amyloids are physiologically important in humans.
Sherin Abdelrahman +5 more
doaj +1 more source
Bacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs [PDF]
, 2016 Altres ajuts: MARATOTV3/2013/3930In the human endocrine system many protein hormones including urotensin, glucagon, obestatin, bombesin and secretin, among others, are supplied from amyloidal secretory granules.
Abasolo, Ibane +15 more
core +2 more sources
Amyloids — a functional coat for microorganisms [PDF]
Nature Reviews Microbiology, 2005 Amyloids are filamentous protein structures approximately 10 nm wide and 0.1-10 mum long that share a structural motif, the cross-beta structure. These fibrils are usually associated with degenerative diseases in mammals. However, recent research has shown that these proteins are also expressed on bacterial and fungal cell surfaces.
Gebbink, M.F.B.G. +4 more
openaire +3 more sources
The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils
Nature Communications, 2022 In this work the authors provide high-resolution structural support for the amyloid-antimicrobial link via functional amyloids displaying propeller-like and kinked cross-β fibrils.
Robert Bücker +6 more
doaj +1 more source
Structure-function analysis of the curli accessory protein CsgE defines surfaces essential for coordinating amyloid fiber formation [PDF]
, 2018 Curli amyloid fibers are produced as part of the extracellular biofilm matrix and are composed primarily of the major structural subunit CsgA. The CsgE chaperone facilitates the secretion of CsgA through CsgG by forming a cap at the base of the nonameric
Amarasinghe, Gaya K +13 more
core +2 more sources
Good Amyloid, Bad Amyloid-What's the Difference? [PDF]
PLoS Biology, 2016 Why do some amyloids cause serious neurodegenerative diseases, while others have important biological functions? A new study of the functional amyloid Orb2 suggests that it's all about speed. Read the Research Article.
Roland G Roberts
doaj +1 more source
An Amyloid Organelle: Solid State NMR Evidence for Cross-Beta Assembly of Gas Vesicles [PDF]
, 2011 Functional amyloids have been identified in a wide range of organisms, taking on a variety of biological roles and being controlled by remarkable mechanisms of directed assembly.
Bayro +35 more
core +1 more source
Prion, 2010 Evidence is growing at an increasing -pace that amyloid fibers are not just the result of aberrant protein folding associated with neurodegenerative diseases, but are widespread in nature for beneficial reasons. Amyloid is an attractive building material because its robust design and simple repetitive structure make for very durable and metabolically ...
openaire +3 more sources