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Functional amyloids in bacteria.
International microbiology : the official journal of the Spanish Society for Microbiology, 2014The term amyloidosis is used to refer to a family of pathologies altering the homeostasis of human organs. Despite having a name that alludes to starch content, the amyloid accumulations are made up of proteins that polymerize as long and rigid fibers.
Romero, Diego, Kolter , Roberto
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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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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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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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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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Not just amyloid: physiological functions of the amyloid precursor protein family
Nature Reviews Neuroscience, 2017Amyloid precursor protein (APP) gives rise to the amyloid-β peptide and thus has a key role in the pathogenesis of Alzheimer disease. By contrast, the physiological functions of APP and the closely related APP-like proteins (APLPs) remain less well understood.
Ulrike C, Müller +2 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 materials at surfaces/interfaces
Biomaterials Science, 2018With the development of nanotechnology, functional amyloid materials at surfaces/interfaces are drawing increasing attention, and numerous remarkable applications are emerging, which are outlined in this reivew.
Chen Li +4 more
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Nanomechanics of functional and pathological amyloid materials
Nature Nanotechnology, 2011Amyloid or amyloid-like fibrils represent a general class of nanomaterials that can be formed from many different peptides and proteins. Although these structures have an important role in neurodegenerative disorders, amyloid materials have also been exploited for functional purposes by organisms ranging from bacteria to mammals.
Tuomas P J, Knowles, Markus J, Buehler
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