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Impact of membrane curvature on amyloid aggregation
| Content Provider | Scilit |
|---|---|
| Author | Terakawa, Mayu S. Lin, Yuxi Kinoshita, Misaki Kanemura, Shingo Itoh, Dai Sugiki, Toshihiko Okumura, Masaki Ramamoorthy, Ayyalusamy Lee, Young-Ho |
| Copyright Year | 2018 |
| Description | Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes The misfolding, amyloid aggregation, and fibril formation of intrinsically disordered proteins/peptides (or amyloid proteins) have been shown to cause a number of disorders. The underlying mechanisms of amyloid fibrillation and structural properties of amyloidogenic precursors, intermediates, and amyloid fibrils have been elucidated in detail; however, in-depth examinations on physiologically relevant contributing factors that induce amyloidogenesis and lead to cell death remain challenging. A large number of studies have attempted to characterize the roles of biomembranes on protein aggregation and membrane-mediated cell death by designing various membrane components, such as gangliosides, cholesterol, and other lipid compositions, and by using various membrane mimetics, including liposomes, bicelles, and different types of lipid-nanodiscs. |
| Related Links | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6205921/pdf |
| Ending Page | 1764 |
| Page Count | 24 |
| Starting Page | 1741 |
| ISSN | 00052736 |
| DOI | 10.1016/j.bbamem.2018.04.012 |
| Journal | Biochimica et Biophysica Acta (BBA) - Biomembranes |
| Issue Number | 9 |
| Volume Number | 1860 |
| Language | English |
| Publisher | Elsevier BV |
| Publisher Date | 2018-04-28 |
| Access Restriction | Open |
| Subject Keyword | Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes Membrane Interaction Protein Misfolding Disease |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Biophysics |
