Results 11 to 20 of about 18,838 (278)

Ubiquitous Amyloids [PDF]

open access: yesApplied Biochemistry and Biotechnology, 2012
The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease.
Pulawski W   +3 more
openaire   +2 more sources

Multifunctional Amyloids in the Biology of Gram-Positive Bacteria

open access: yesMicroorganisms, 2020
Since they were discovered, amyloids have proven to be versatile proteins able to participate in a variety of cellular functions across all kingdoms of life.
Ana Álvarez-Mena   +3 more
doaj   +1 more source

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

Amyloid neuropathies [PDF]

open access: yesCurrent Opinion in Neurology, 2012
As amyloid neuropathies have benefited from recent major progress, this review is timely and relevant.The main recent articles on amyloid neuropathy cover its description, methods for diagnosis and therapies. Varied clinical presentations are described in transthyretin (TTR)-familial amyloidosis with polyneuropathy (FAP) and light chain amyloid ...
David, Adams   +2 more
openaire   +4 more sources

Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids

open access: yesMolecules, 2023
To date, most research on amyloid aggregation has focused on describing the structure of amyloids and the kinetics of their formation, while the conformational stability of fibrils remains insufficiently explored.
Natalya Katina   +6 more
doaj   +1 more source

Amyloid prions in fungi [PDF]

open access: yes, 2016
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi   +122 more
core   +2 more sources

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

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

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

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

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