Results 31 to 40 of about 92,288 (249)
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
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Surveillance of Amyloid Deposition and Bacterial Contamination in Chicken Liver from Meat Market
The Journal of Poultry Science, 2014 From the standpoint of poultry meat hygiene, amyloid deposition and bacterial contamination in livers of 197 mature white layer chickens from a slaughterhouse and 100 young broiler breeder chickens from 5 different retail butcher shops were examined ...
Naotaka Ishiguro +3 more
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Fold modulating function: bacterial toxins to functional amyloids [PDF]
Frontiers in Microbiology, 2014 Many bacteria produce cytolytic toxins that target host cells or other competing microbes. It is well known that environmental factors control toxin expression, however, recent work suggests that some bacteria manipulate the fold of these protein toxins to control their function.
Syed, Adnan K., Boles, Blaise R.
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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
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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
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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
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Bacterial functional amyloids: Order from disorder
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2019 The discovery of intrinsic disorderness in proteins and peptide regions has given a new and useful insight into the working of biological systems. Due to enormous plasticity and heterogeneity, intrinsically disordered proteins or regions in proteins can perform myriad of functions.
Neha, Jain, Matthew R, Chapman
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Amyloid-DNA Composites of Bacterial Biofilms Stimulate Autoimmunity [PDF]
Immunity, 2015 Research on the human microbiome has established that commensal and pathogenic bacteria can influence obesity, cancer, and autoimmunity through mechanisms mostly unknown. We found that a component of bacterial biofilms, the amyloid protein curli, irreversibly formed fibers with bacterial DNA during biofilm formation.
Gallo, Paul M. +9 more
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Bacterial Amyloids: The Link between Bacterial Infections and Autoimmunity
Trends in Microbiology, 2019 Molecular mimicry is a common mechanism used by many bacteria to evade immune responses. In recent years, it has become evident that bacteria also decorate the extracellular matrix (ECM) of their biofilms with molecules that resemble those of the host.
Lauren, Nicastro, Çagla, Tükel
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Gene Regulation of Biofilm-Associated Functional Amyloids
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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