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Reporters of amyloid structural polymorphism
University of Kentucky, Lexington, USA.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-5582-140X
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
2014 (English)In: Bio-nanoimaging: protein misfolding & aggregation / [ed] Vladimir N. Uversky, Yuri L. Lyubchenko, London: Academic Press, 2014, 69-79 p.Chapter in book (Other academic)
Abstract [en]

Misfolding of proteins induced by environmental conditions or by the presence of destabilizing mutations often triggers squestration (aggresome formation) or cellular removal (unfolded protein response (UPR), autophagy) intracellular responses. Extracellular aggregates are phagocytosed or endocytosed by macrophages in the periphery and microglia and astrocytes in the brain and central nervous system. In some cases a highly stable altemative assembly structure, an amyloid fibril, is formed that is highly resistant to degadation and thus accumulates.

Place, publisher, year, edition, pages
London: Academic Press, 2014. 69-79 p.
Keyword [en]
Misfolding, Proteins, Amyloid fibrils
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-103808ISBN: 978-0-12-394431-3 (print)OAI: oai:DiVA.org:liu-103808DiVA: diva2:691538
Available from: 2014-01-28 Created: 2014-01-28 Last updated: 2014-04-08

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Nilsson, PeterHammarström, Per

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