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In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study [PDF]

open access: yesPathogens, 2019
Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an ...
David Partouche   +5 more
doaj   +6 more sources

Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC [PDF]

open access: yesAdvanced Science, 2020
The gut–brain axis has attracted increasing attention in recent years, fueled by accumulating symptomatic, physiological, and pathological findings. In this study, the aggregation and toxicity of amyloid beta (Aβ), the pathogenic peptide associated with ...
Ibrahim Javed   +10 more
doaj   +11 more sources

Identification and characterization of the Hfq bacterial amyloid region DNA interactions [PDF]

open access: yesBBA Advances, 2021
Nucleic acid amyloid proteins interactions have been observed in the past few years. These interactions often promote protein aggregation. Nevertheless, molecular basis and physiological consequences of these interactions are still poorly understood ...
Florian Turbant   +6 more
doaj   +4 more sources

Bacterial Extracellular DNA Promotes β-Amyloid Aggregation [PDF]

open access: yesMicroorganisms, 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   +5 more sources

Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies

open access: yesMolecules, 2022
Functional amyloid is produced by many organisms but is particularly well understood in bacteria, where proteins such as CsgA (E. coli) and FapC (Pseudomonas) are assembled as functional bacterial amyloid (FuBA) on the cell surface in a carefully ...
Thorbjørn Vincent Sønderby   +2 more
doaj   +3 more sources

Surveillance of Amyloid Deposition and Bacterial Contamination in Chicken Liver from Meat Market

open access: yesThe 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
doaj   +3 more sources

Functional bacterial amyloid increases Pseudomonas biofilm hydrophobicity and stiffness [PDF]

open access: yesFrontiers in Microbiology, 2015
The success of Pseudomonas species as opportunistic pathogens derives in great part from their ability to form stable biofilms that offer protection against chemical and mechanical attack.
Guanghong eZeng   +8 more
doaj   +2 more sources

Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli

open access: yesQRB Discovery, 2022
Interactions between proteins and single-stranded DNA (ssDNA) are crucial for many fundamental biological processes, including DNA replication and genetic recombination.
Krzysztof Kubiak   +10 more
doaj   +1 more source

The Amyloid Region of Hfq Riboregulator Promotes DsrA:rpoS RNAs Annealing

open access: yesBiology, 2021
Hfq is a bacterial RNA chaperone which promotes the pairing of small noncoding RNAs to target mRNAs, allowing post-transcriptional regulation. This RNA annealing activity has been attributed for years to the N-terminal region of the protein that forms a ...
Florian Turbant   +3 more
doaj   +1 more source

Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq

open access: yesAntibiotics, 2021
Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance
Florian Turbant   +6 more
doaj   +1 more source

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