Results 41 to 50 of about 6,595 (270)
Alzheimer's Amyloid-β is an Antimicrobial Peptide: A Review of the Evidence [PDF]
, 2018 The final publication is available at IOS Press through http://dx.doi.org/10.3233/JAD-171133.The amyloid-β (Aβ) peptide has long been considered to be the driving force behind Alzheimer’s disease (AD).
Brothers, Holly +2 more
core +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
Direct Identification of Functional Amyloid Proteins by Label-Free Quantitative Mass Spectrometry
Biomolecules, 2017 Functional amyloids are important structural and functional components of many biofilms, yet our knowledge of these fascinating polymers is limited to a few examples for which the native amyloids have been isolated in pure form.
Heidi N. Danielsen +6 more
doaj +1 more source
Periodontitis, microbiomes and their role in Alzheimer’s disease [PDF]
, 2017 As far back as the eighteenth and early nineteenth centuries, microbial infections were responsible for vast numbers of deaths. The trend reversed with the introduction of antibiotics coinciding with longer life.
Crean, Stjohn +3 more
core +2 more sources
Hsp104 Gives Clients the Individual Attention They Need [PDF]
, 2010 Yeast heat shock protein 104 (Hsp104), the only known eukaryotic disaggregase, remodels both disordered protein aggregates and cross-β sheet amyloids. To handle this diverse clientele, DeSantis et al.
Murray, Amber N., Kelly, Jeffery W.
core +4 more sources
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
openaire +2 more sources
The Role of Functional Amyloids in Multicellular Growth and Development of Gram-Positive Bacteria [PDF]
, 2017 Amyloid fibrils play pivotal roles in all domains of life. In bacteria, these fibrillar structures are often part of an extracellular matrix that surrounds the producing organism and thereby provides protection to harsh environmental conditions. Here, we
Claessen, Dennis +2 more
core +4 more sources
Structure of the nonameric bacterial amyloid secretion channel [PDF]
Proceedings of the National Academy of Sciences, 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 subunits in
Baohua, Cao +5 more
openaire +2 more sources
Frontiers in Microbiology, 2016 Microcin E492 (MccE492) is a pore-forming bacteriocin produced and exported by Klebsiella pneumoniae RYC492. Besides its antibacterial activity, excreted MccE492 can form amyloid fibrils in vivo as well as in vitro.
Paulina eAguilera +6 more
doaj +1 more source
PACT - Prediction of amyloid cross-interaction by threading
Scientific Reports, 2023 Amyloid proteins are often associated with the onset of diseases, including Alzheimer’s, Parkinson’s and many others. However, there is a wide class of functional amyloids that are involved in physiological functions, e.g., formation of microbial ...
Jakub W. Wojciechowski +4 more
doaj +1 more source