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Search and Identification of Amyloid Proteins
Methods and Protocols, 2023 Amyloids are fibrillar proteins with a cross-β structure. Pathological amyloids are associated with the development of a number of incurable diseases, while functional amyloids regulate vital processes. The detection of unknown amyloids in living objects
Tatyana A. Belashova +5 more
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Functional Amyloids Are the Rule Rather Than the Exception in Cellular Biology
Microorganisms, 2020 Amyloids are a class of protein aggregates that have been historically characterized by their relationship with human disease. Indeed, amyloids can be the result of misfolded proteins that self-associate to form insoluble, extracellular plaques in ...
Anthony Balistreri +2 more
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Amyloid as a depot for the formulation of long-acting drugs. [PDF]
PLoS Biology, 2008 Amyloids are highly organized protein aggregates that are associated with both neurodegenerative diseases such as Alzheimer disease and benign functions like skin pigmentation. Amyloids self-polymerize in a nucleation-dependent manner by recruiting their
Samir K Maji +5 more
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Functional Mammalian Amyloids and Amyloid-Like Proteins
Life, 2020 Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD ...
Maria S. Rubel +6 more
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Anti-Biofilm Molecules Targeting Functional Amyloids
Antibiotics, 2021 The choice of an effective therapeutic strategy in the treatment of biofilm-related infections is a significant issue. Amyloids, which have been historically related to human diseases, are now considered to be prevailing structural components of the ...
Leticia Matilla-Cuenca +2 more
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Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids
Molecules, 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
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Multifunctional Amyloids in the Biology of Gram-Positive Bacteria
Microorganisms, 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
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J Proteins Counteract Amyloid Propagation and Toxicity in Yeast
Biology, 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
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Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
Biology 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
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SynBio and the Boundaries between Functional and Pathogenic RepA-WH1 Bacterial Amyloids
mSystems, 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
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