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Journal of Molecular Biology, 2023
Functional amyloids are a rapidly expanding class of fibrillar protein structures, with a core cross-β scaffold, where novel and advantageous biological function is generated by the assembly of the amyloid. The growing number of amyloid structures determined at high resolution reveal how this supramolecular template both accommodates a wide variety of ...
Jessica A, Buchanan +3 more
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Functional amyloids are a rapidly expanding class of fibrillar protein structures, with a core cross-β scaffold, where novel and advantageous biological function is generated by the assembly of the amyloid. The growing number of amyloid structures determined at high resolution reveal how this supramolecular template both accommodates a wide variety of ...
Jessica A, Buchanan +3 more
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Function of amyloid and amyloid protein precursor
Clinical Neurology and Neurosurgery, 1992A short review is given of the functions of amyloid (beta/A4) and its precursor protein (APP). The possible relationship between amyloid deposition and dementia is discussed.
R A, Roos, J, Haan
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Functional amyloids in the human body
Bioorganic & Medicinal Chemistry Letters, 2021Amyloids have long been associated with a variety of human degenerative diseases. Discoveries indicate, however, that there are several amyloids that serve functional roles in the human body. These amyloids are involved in a variety of biological processes ranging from storage of peptide hormones to necroptosis of cells.
Amy Brown, Marianna Török
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Amyloids: from pathogenesis to function
Biochemistry (Moscow), 2015The term "amyloids" refers to fibrillar protein aggregates with cross-β structure. They have been a subject of intense scrutiny since the middle of the previous century. First, this interest is due to association of amyloids with dozens of incurable human diseases called amyloidoses, which affect hundreds of millions of people. However, during the last
A A, Nizhnikov +2 more
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While amyloid has traditionally been viewed as a harmful formation, emerging evidence suggests that amyloids may also play a functional role in cell biology, contributing to normal physiological processes that have been conserved throughout evolution.
Mansoureh, Mirza Agha +2 more
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Mansoureh, Mirza Agha +2 more
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Immune Functions of Serum Amyloid A
Critical Reviews in Immunology, 2012Serum amyloid A (SAA) is a highly conserved, acute-phase protein synthesized predominantly by the liver. After secretion into the circulation, it associates with high-density lipoprotein (HDL) particles. During acute inflammation, serum SAA levels may rise up to 1000-fold, and under these conditions, SAA displaces apolipoprotein A-I from HDL, thus ...
Kari K, Eklund, K, Niemi, P T, Kovanen
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Functional Bacterial Amyloids in Biofilms
2011Functional bacterial amyloids constitute a group of important proteinaceous surface structures. Most amyloids are highly insoluble in water and resistant to most enzymes and thermal and chemical denaturants. Their functions in bacteria are still not well described but seem to include fimbriae and other cell appendages for adhesion and biofilm formation,
Nielsen, Per Halkjær +4 more
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Functional amyloids in insect immune response
Insect Biochemistry and Molecular Biology, 2012The innate immune system of insects consists of humoural and cellular responses that provide protection against invading pathogens and parasites. Defence reactions against these latter include encapsulation by immune cells and targeted melanin deposition, which is usually restricted to the surface of the foreign invader, to prevent systemic damage ...
Falabella P. +12 more
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Transthyretin: Its function and amyloid formation
Neurochemistry International, 2022Transthyretin (TTR), which is one of the major amyloidogenic proteins in systemic amyloidosis, forms extracellular amyloid deposits in the systemic organs such as nerves, ligaments, heart, and arterioles, and causes two kinds of systemic amyloidosis, hereditary ATTR (ATTRv) amyloidosis induced by variant TTR and aging-related wild-type ATTR (ATTRwt ...
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Functional amyloid – from bacteria to humans
Trends in Biochemical Sciences, 2007Amyloid--a fibrillar, cross beta-sheet quaternary structure--was first discovered in the context of human disease and tissue damage, and was thought to always be detrimental to the host. Recent studies have identified amyloid fibers in bacteria, fungi, insects, invertebrates and humans that are functional.
Douglas M, Fowler +3 more
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