Vitaly V Kushnirov, Alexander A Dergalev, Alexander I Alexandrov
{"title":"朊病毒和淀粉样蛋白的蛋白酶K抗性核心。","authors":"Vitaly V Kushnirov, Alexander A Dergalev, Alexander I Alexandrov","doi":"10.1080/19336896.2019.1704612","DOIUrl":null,"url":null,"abstract":"<p><p>Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained <i>ex vivo</i> and <i>in vitro</i>, as well as the manner in which folding of one region of the amyloid can affect other regions.</p>","PeriodicalId":54585,"journal":{"name":"Prion","volume":null,"pages":null},"PeriodicalIF":1.9000,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336896.2019.1704612","citationCount":"29","resultStr":"{\"title\":\"Proteinase K resistant cores of prions and amyloids.\",\"authors\":\"Vitaly V Kushnirov, Alexander A Dergalev, Alexander I Alexandrov\",\"doi\":\"10.1080/19336896.2019.1704612\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained <i>ex vivo</i> and <i>in vitro</i>, as well as the manner in which folding of one region of the amyloid can affect other regions.</p>\",\"PeriodicalId\":54585,\"journal\":{\"name\":\"Prion\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.9000,\"publicationDate\":\"2020-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/19336896.2019.1704612\",\"citationCount\":\"29\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Prion\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1080/19336896.2019.1704612\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Prion","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1080/19336896.2019.1704612","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Proteinase K resistant cores of prions and amyloids.
Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained ex vivo and in vitro, as well as the manner in which folding of one region of the amyloid can affect other regions.
期刊介绍:
Prion is the first international peer-reviewed open access journal to focus exclusively on protein folding and misfolding, protein assembly disorders, protein-based and structural inheritance. The goal is to foster communication and rapid exchange of information through timely publication of important results using traditional as well as electronic formats. The overriding criteria for publication in Prion are originality, scientific merit and general interest.