Results 21 to 30 of about 13,480 (279)

J Proteins Counteract Amyloid Propagation and Toxicity in Yeast

open access: yesBiology, 2022
The accumulation of misfolded proteins as amyloids is associated with pathology in dozens of debilitating human disorders, including diabetes, Alzheimer’s, Parkinson’s, and Huntington’s diseases.
Daniel C. Masison   +2 more
doaj   +1 more source

Amyloids assemble as part of recognizable structures during oogenesis in Xenopus

open access: yesBiology Open, 2016
A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic.
Michael H. Hayes, Daniel L. Weeks
doaj   +1 more source

Microbial amyloids in neurodegenerative amyloid diseases

open access: yesThe FEBS Journal, 2023
Human‐disease associated amyloidogenic proteins are not unique in their ability to form amyloid fibrillar structures. Numerous microbes produce amyloidogenic proteins that have distinct functions for their physiology in their amyloid form, rather than solely detrimental. Emerging data indicate associations between various microbial organisms, including
openaire   +2 more sources

SynBio and the Boundaries between Functional and Pathogenic RepA-WH1 Bacterial Amyloids

open access: yesmSystems, 2020
Amyloids are protein polymers that were initially linked to human diseases. Across the whole Tree of Life, many disease-unrelated proteins are now emerging for which amyloids represent distinct functional states.
Rafael Giraldo
doaj   +3 more sources

M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils. [PDF]

open access: yesPLoS ONE, 2018
Amyloids are protein fibrils with a characteristic spatial structure. Amyloids were long perceived as the pathogens involved in a set of lethal diseases in humans and animals.
Mikhail V Belousov   +9 more
doaj   +1 more source

Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases

open access: yesFrontiers in Aging Neuroscience, 2021
Amyloids are highly ordered aggregates composed of proteins or peptides. They are involved in several pathologies, including hallmark neurodegenerative disorders such as Alzheimer’s (AD) and Parkinson’s (PD).
Rodrigo Diaz-Espinoza
doaj   +1 more source

Pharmacological Agents Targeting the Cellular Prion Protein

open access: yesPathogens, 2018
Prion diseases are associated with the conversion of the cellular prion protein (PrPC), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrPSc) that accumulates in brain ...
Maria Letizia Barreca   +4 more
doaj   +1 more source

Amyloidogenic Peptides in Human Neuro-Degenerative Diseases and in Microorganisms: A Sorrow Shared Is a Sorrow Halved?

open access: yesMolecules, 2020
The term “amyloid” refers to proteinaceous deposits of peptides that might be generated from larger precursor proteins e.g., by proteolysis.
Kristina Endres
doaj   +1 more source

Direct Identification of Functional Amyloid Proteins by Label-Free Quantitative Mass Spectrometry

open access: yesBiomolecules, 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

Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains

open access: yesViruses, 2019
The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc ...
Yuzuru Taguchi   +2 more
doaj   +1 more source

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