Results 11 to 20 of about 1,155,621 (272)
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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Role of the Bacterial Amyloid-like Hfq in Fluoroquinolone Fluxes. [PDF]
Microorganisms, 2023 Due to their two-cell membranes, Gram-negative bacteria are particularly resistant to antibiotics. Recent investigations aimed at exploring new target proteins involved in Gram-negative bacteria adaptation helped to identify environmental changes encountered during infection.
Turbant F +6 more
europepmc +5 more sources
Structural analysis and architectural principles of the bacterial amyloid curli. [PDF]
Nat Commun, 2023 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. That revolutionary idea was borne out of the realization that a large fraction of the extracellular
Sleutel M +3 more
europepmc +5 more sources
Herpes simplex virus interferes with amyloid precursor protein processing. [PDF]
, 2005 Background The early events underlying Alzheimer's disease (AD) remain uncertain, although environmental factors may be involved. Work in this laboratory has shown that the combination of herpes simplex virus type 1 (HSV1) in brain and carriage of the ...
Shipley, Suzanne J. +3 more
core +6 more sources
Structural Studies of Cystatin B Amyloid Fibre and Oligomer [PDF]
, 2013 Amyloid fibres are characteristic of over 25 degenerative human diseases including Alzheimer’s and Parkinson’s disease. Amyloid fibres are insoluble, highly stable, ordered cross-β sheet structures, which form as a result of conformational change and ...
Davis, Peter J.
core +5 more sources
The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid. [PDF]
Adv Sci (Weinh)Abstract Amyloids, once viewed solely as pathological hallmarks, are now recognized as widespread and versatile functional protein assemblies. Bacterial functional amyloids (FuBAs), particularly curli (CsgA) from Escherichia coli and FapC from Pseudomonas
Peña-Díaz S +12 more
europepmc +5 more sources
BBA Advances, 2022 Functional amyloids (FA) are proteins which are evolutionarily optimized to form highly stable fibrillar structures that strengthen the bacterial biofilm matrix. FA such as CsgA (E. coli) and FapC (Pseudomonas) are secreted to the bacterial surface where
Zahra Najarzadeh +6 more
doaj +1 more source
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
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Anti-Amyloid Drug Screening Methods Using Bacterial Inclusion Bodies [PDF]
, 2023 Amyloid aggregation is linked to a number of human disorders that range from non-neurological illnesses such as type 2 diabetes to neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. The formation of insoluble protein aggregates with
Gámez Enamorado, Patrick +3 more
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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