Results 31 to 40 of about 1,155,621 (272)
Structure of the nonameric bacterial amyloid secretion channel. [PDF]
Proc Natl Acad Sci U S A, 2014 Significance Numerous bacteria produce a unique class of “functional” amyloids termed curli that are important for the fitness of the organism by mediating biofilm formation, host cell adhesion, and colonization on inert surfaces. Here, we report the crystal structure of CsgG, a lipoprotein that forms a secretion channel for curli ...
Cao B +5 more
europepmc +4 more sources
Bacterial biofilm functionalization through Bap amyloid engineering
npj Biofilms and Microbiomes, 2022 Biofilm engineering has emerged as a controllable way to fabricate living structures with programmable functionalities. The amyloidogenic proteins comprising the biofilms can be engineered to create self-assembling extracellular functionalized surfaces ...
Leticia Matilla-Cuenca +5 more
doaj +1 more source
Amyloids in bacterial inclusion bodies
Trends in Biochemical Sciences, 2009 Protein misfolding and aggregation into amyloid structures are associated with dozens of human diseases. Recent studies have provided compelling evidence for the existence of highly ordered, amyloid-like conformations in the insoluble inclusion bodies produced during heterologous protein expression in bacteria.
Natalia S, de Groot +2 more
openaire +3 more sources
Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters [PDF]
, 2010 Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular functions is therefore
Xue, Wei-Feng +7 more
core +1 more source
Bacterial inclusion bodies are industrially exploitable amyloids [PDF]
FEMS Microbiology Reviews, 2018 Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids ...
Ario de Marco +9 more
openaire +3 more sources
Mitochondrial β-amyloid in Alzheimer's disease [PDF]
, 2011 This research is supported by Alzheimer's Research UK, the Wellcome Trust and the Biotechnology and Biological Sciences Research Council.It is well established that the intracellular accumulation of beta-amyloid is associated with Alzheimer’s disease and
Ainge, JA +23 more
core +1 more source
Microbial Cell Factories, 2012 An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms.
Villar-Piqué Anna, Ventura Salvador
doaj +1 more source
Structural analysis of the bacterial amyloid curli [PDF]
, 2022 Abstract Two decades have passed since the initial proposition that amyloids are not only (toxic) byproducts of an unintended aggregation cascade, but that they can also be produced by an organism to serve a defined biological function.
Mike Sleutel +2 more
openaire +1 more source
Nature Communications, 2020 Curli amyloid fibers are important components of bacterial biofilms formed by E. coli and Salmonella. Here, Tursi et al. show that a human monoclonal antibody with pan-amyloid binding activity can disrupt biofilms formed by Salmonella Typhimurium in ...
Sarah A. Tursi +10 more
doaj +1 more source
Intercellular Transmission of a Synthetic Bacterial Cytotoxic Prion-Like Protein in Mammalian Cells
mBio, 2020 RepA is a bacterial protein that builds intracellular amyloid oligomers acting as inhibitory complexes of plasmid DNA replication. When carrying a mutation enhancing its amyloidogenesis (A31V), the N-terminal domain (WH1) generates cytosolic amyloid ...
Aida Revilla-García +5 more
doaj +1 more source