Results 51 to 60 of about 6,595 (270)
Frontiers in Cellular and Infection Microbiology, 2022 The bacterial amyloid curli, produced by Enterobacteriales including Salmonella species and Escherichia coli, is implicated in the pathogenesis of several complex autoimmune diseases.
Kaitlyn Grando +6 more
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Ultra rapid in vivo screening for anti-Alzheimer anti-amyloid drugs [PDF]
, 2016 More than 46 million people worldwide suffer from Alzheimer's disease. A large number of potential treatments have been proposed; among these, the inhibition of the aggregation of amyloid β-peptide (Aβ), considered one of the main culprits in Alzheimer's
Di Pietro, O. +4 more
core +1 more source
Bacterial Amyloid Formation: Structural Insights into Curli Biogensis [PDF]
Trends in Microbiology, 2015 Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface ...
Van Gerven, Nani +3 more
openaire +2 more sources
The role of microbial amyloid in neurodegeneration. [PDF]
PLoS Pathogens, 2017 It has become apparent that the intestinal microbiota orchestrates important aspects of our metabolism, immunity, and development. Recent work has demonstrated that the microbiota also influences brain function in healthy and diseased individuals.
Robert P Friedland, Matthew R Chapman
doaj +1 more source
Yeast prions form infectious amyloid inclusion bodies in bacteria [PDF]
, 2012 Background: Prions were first identified as infectious proteins associated with fatal brain diseases in mammals. However, fungal prions behave as epigenetic regulators that can alter a range of cellular processes.
Espargaró Colomé, Alba +3 more
core +3 more sources
Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule Bacterium Rhizobium leguminosarum
Biomolecules, 2019 Amyloids represent protein fibrils with a highly ordered spatial structure, which not only cause dozens of incurable human and animal diseases but also play vital biological roles in Archaea, Bacteria, and Eukarya.
Anastasiia O. Kosolapova +16 more
doaj +1 more source
A Bacterial Shortcut to Amyloidosis [PDF]
, 2017 21 p.-10 fig.The synthetic bacterial prionoid RepA-WH1 causes a vertically transmissible amyloid proteinopathy in Escherichia coli that inhibits growth and eventually kills the cells.
Alonso-del Valle, Aída +9 more
core +1 more source
Directing curli polymerization with DNA origami nucleators
Nature Communications, 2019 Curli are bacterial functional amyloids that have gained interest as self-assembling biomaterial for biotechnology applications. Here, the authors show that DNA origami decorated with CsgB nucleator proteins induced the site-specific nucleation and ...
Xiuhai Mao +13 more
doaj +1 more source
The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor. [PDF]
, 2017 Streptomyces bacteria form reproductive aerial hyphae that are covered with a pattern of pairwise aligned fibrils called rodlets. The presence of the rodlet layer requires two homologous rodlin proteins, RdlA and RdlB, and the functional amyloid chaplin ...
Claessen, Dennis +8 more
core +3 more sources
Amyloid Histology Stain for Rapid Bacterial Endospore Imaging [PDF]
Journal of Clinical Microbiology, 2011 ABSTRACTBacterial endospores are some of the most resilient forms of life known to us, with their persistent survival capability resulting from a complex and effective structural organization. The outer membrane of endospores is surrounded by the densely packed endospore coat and exosporium, containing amyloid or amyloid-like proteins.
Bing, Xia +11 more
openaire +2 more sources