{"title":"蛋白质聚集:折叠聚集体、包涵体和淀粉样蛋白","authors":"Anthony L Fink","doi":"10.1016/S1359-0278(98)00002-9","DOIUrl":null,"url":null,"abstract":"<div><p>Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve <em>β</em> sheets.</p></div>","PeriodicalId":79488,"journal":{"name":"Folding & design","volume":"3 1","pages":"Pages R9-R23"},"PeriodicalIF":0.0000,"publicationDate":"1998-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1359-0278(98)00002-9","citationCount":"1081","resultStr":"{\"title\":\"Protein aggregation: folding aggregates, inclusion bodies and amyloid\",\"authors\":\"Anthony L Fink\",\"doi\":\"10.1016/S1359-0278(98)00002-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve <em>β</em> sheets.</p></div>\",\"PeriodicalId\":79488,\"journal\":{\"name\":\"Folding & design\",\"volume\":\"3 1\",\"pages\":\"Pages R9-R23\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S1359-0278(98)00002-9\",\"citationCount\":\"1081\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Folding & design\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1359027898000029\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Folding & design","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1359027898000029","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Protein aggregation: folding aggregates, inclusion bodies and amyloid
Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve β sheets.
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