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Amyloid assembly and disassembly
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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Journal of Cell Science, 131, 2018, 8 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Chuang, Edward Hori, Acacia M. Hesketh, Christina D. Shorter, James Chuang, Edward Hori, Acacia M. Hesketh, Christina D. Shorter, James |
|---|---|
| author |
Chuang, Edward Hori, Acacia M. Hesketh, Christina D. Shorter, James |
| spellingShingle |
Chuang, Edward Hori, Acacia M. Hesketh, Christina D. Shorter, James Journal of Cell Science Amyloid assembly and disassembly Cell Biology |
| author_sort |
chuang, edward |
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Chuang, Edward Hori, Acacia M. Hesketh, Christina D. Shorter, James 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.189928 <jats:title>ABSTRACT</jats:title> <jats:p>Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. Conversely, functional amyloids play beneficial roles in melanosome biogenesis, long-term memory formation and release of peptide hormones. Here, we showcase advances in our understanding of amyloid assembly and structure, and how distinct amyloid strains formed by the same protein can cause distinct neurodegenerative diseases. We discuss how mutant steric zippers promote deleterious amyloidogenesis and aberrant liquid-to-gel phase transitions. We also highlight effective strategies to combat amyloidogenesis and related toxicity, including: (1) small-molecule drugs (e.g. tafamidis) to inhibit amyloid formation or (2) stimulate amyloid degradation by the proteasome and autophagy, and (3) protein disaggregases that disassemble toxic amyloid and soluble oligomers. We anticipate that these advances will inspire therapeutics for several fatal neurodegenerative diseases.</jats:p> Amyloid assembly and disassembly Journal of Cell Science |
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| title |
Amyloid assembly and disassembly |
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Amyloid assembly and disassembly |
| title_full |
Amyloid assembly and disassembly |
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Amyloid assembly and disassembly |
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Amyloid assembly and disassembly |
| title_short |
Amyloid assembly and disassembly |
| title_sort |
amyloid assembly and disassembly |
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Cell Biology |
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http://dx.doi.org/10.1242/jcs.189928 |
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2018 |
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<jats:title>ABSTRACT</jats:title>
<jats:p>Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. Conversely, functional amyloids play beneficial roles in melanosome biogenesis, long-term memory formation and release of peptide hormones. Here, we showcase advances in our understanding of amyloid assembly and structure, and how distinct amyloid strains formed by the same protein can cause distinct neurodegenerative diseases. We discuss how mutant steric zippers promote deleterious amyloidogenesis and aberrant liquid-to-gel phase transitions. We also highlight effective strategies to combat amyloidogenesis and related toxicity, including: (1) small-molecule drugs (e.g. tafamidis) to inhibit amyloid formation or (2) stimulate amyloid degradation by the proteasome and autophagy, and (3) protein disaggregases that disassemble toxic amyloid and soluble oligomers. We anticipate that these advances will inspire therapeutics for several fatal neurodegenerative diseases.</jats:p> |
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| author | Chuang, Edward, Hori, Acacia M., Hesketh, Christina D., Shorter, James |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p>Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. Conversely, functional amyloids play beneficial roles in melanosome biogenesis, long-term memory formation and release of peptide hormones. Here, we showcase advances in our understanding of amyloid assembly and structure, and how distinct amyloid strains formed by the same protein can cause distinct neurodegenerative diseases. We discuss how mutant steric zippers promote deleterious amyloidogenesis and aberrant liquid-to-gel phase transitions. We also highlight effective strategies to combat amyloidogenesis and related toxicity, including: (1) small-molecule drugs (e.g. tafamidis) to inhibit amyloid formation or (2) stimulate amyloid degradation by the proteasome and autophagy, and (3) protein disaggregases that disassemble toxic amyloid and soluble oligomers. We anticipate that these advances will inspire therapeutics for several fatal neurodegenerative diseases.</jats:p> |
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| series | Journal of Cell Science |
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| spelling | Chuang, Edward Hori, Acacia M. Hesketh, Christina D. Shorter, James 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.189928 <jats:title>ABSTRACT</jats:title> <jats:p>Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. Conversely, functional amyloids play beneficial roles in melanosome biogenesis, long-term memory formation and release of peptide hormones. Here, we showcase advances in our understanding of amyloid assembly and structure, and how distinct amyloid strains formed by the same protein can cause distinct neurodegenerative diseases. We discuss how mutant steric zippers promote deleterious amyloidogenesis and aberrant liquid-to-gel phase transitions. We also highlight effective strategies to combat amyloidogenesis and related toxicity, including: (1) small-molecule drugs (e.g. tafamidis) to inhibit amyloid formation or (2) stimulate amyloid degradation by the proteasome and autophagy, and (3) protein disaggregases that disassemble toxic amyloid and soluble oligomers. We anticipate that these advances will inspire therapeutics for several fatal neurodegenerative diseases.</jats:p> Amyloid assembly and disassembly Journal of Cell Science |
| spellingShingle | Chuang, Edward, Hori, Acacia M., Hesketh, Christina D., Shorter, James, Journal of Cell Science, Amyloid assembly and disassembly, Cell Biology |
| title | Amyloid assembly and disassembly |
| title_full | Amyloid assembly and disassembly |
| title_fullStr | Amyloid assembly and disassembly |
| title_full_unstemmed | Amyloid assembly and disassembly |
| title_short | Amyloid assembly and disassembly |
| title_sort | amyloid assembly and disassembly |
| title_unstemmed | Amyloid assembly and disassembly |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.189928 |