Results 11 to 20 of about 92,288 (249)
Bacterial Extracellular DNA Promotes β-Amyloid Aggregation [PDF]
Microorganisms, 2021 Alzheimer’s disease is associated with prion-like aggregation of the amyloid β (Aβ) peptide and the subsequent accumulation of misfolded neurotoxic aggregates in the brain.
George Tetz, Victor Tetz
doaj +3 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
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Bacterial inclusion bodies contain amyloid-like structure. [PDF]
PLoS Biology, 2008 Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can
Lei Wang +4 more
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Force spectra of single bacterial amyloid CsgA nanofibers. [PDF]
RSC Adv, 2020 Magnetic tweezers were used to study the force spectra of CsgA, a major protein subunit of Escherichia coli biofilms, at fibril level.
Lv J +8 more
europepmc +4 more sources
Molecules, 2023 Microcin E492 (MccE492) is an antimicrobial peptide and proposed virulence factor produced by some Klebsiella pneumoniae strains, which, under certain conditions, form amyloid fibers, leading to the loss of its antibacterial activity.
Paulina Aguilera +8 more
doaj +1 more source
Frontiers in Plant Science, 2022 Amyloids represent protein aggregates with highly ordered fibrillar structure associated with the development of various disorders in humans and animals and involved in implementation of different vital functions in all three domains of life.
Anastasiia O. Kosolapova +15 more
doaj +1 more source
, 2018 Many bacteria can assemble functional amyloid fibers on their cell surface. Most bacterial amyloids contribute to biofilm or other community behaviors where cells interact with a surface or with other cells. Bacterial amyloids, like all functional amyloids, share structural and biochemical properties with disease-associated eukaryotic amyloids.
Margery L, Evans +3 more
openaire +2 more sources
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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Bacterial amyloid formation: structural insights into curli biogensis. [PDF]
Trends Microbiol, 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 N +3 more
europepmc +4 more sources
, 2012 Many bacteria can assemble functional amyloid fibers on their cell surface. The majority of bacterial amyloids contribute to biofilm or other community behaviors where cells interact with a surface or with another cell. Bacterial amyloids, like all functional amyloids, share structural and biochemical properties with disease-associated eukaryotic ...
Yizhou, Zhou +3 more
openaire +2 more sources