Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases
[...]a wide variety of misfolded structures are formed, ranging from small soluble oligomers to large fibrillar deposits. Since nuclei are formed, the aggregation increases in an exponential manner from small oligomers to fibers.
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| Veröffentlicht in: | PLoS pathogens 2013-09, Vol.9 (9), p.e1003537-e1003537 |
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| container_issue | 9 |
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| container_title | PLoS pathogens |
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| creator | Morales, Rodrigo Moreno-Gonzalez, Ines Soto, Claudio |
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[...]a wide variety of misfolded structures are formed, ranging from small soluble oligomers to large fibrillar deposits. Since nuclei are formed, the aggregation increases in an exponential manner from small oligomers to fibers. |
| doi_str_mv | 10.1371/journal.ppat.1003537 |
| format | Article |
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[...]a wide variety of misfolded structures are formed, ranging from small soluble oligomers to large fibrillar deposits. Since nuclei are formed, the aggregation increases in an exponential manner from small oligomers to fibers.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24068917</pmid><doi>10.1371/journal.ppat.1003537</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Disease Models, Animal Experiments Humans Models, Biological Oxidative stress Pathogenesis Pearls Physiology, Pathological Polymerization Prions Protein Aggregation, Pathological - etiology Protein Folding Protein Interaction Domains and Motifs Proteins - chemistry Proteostasis Deficiencies - etiology Proteostasis Deficiencies - physiopathology Seeds Signal transduction |
| title | Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases |
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