A. O. Nikitina, A. Yulmetov, A. Kusova, V. Klochkov, D. S. Blokhin
{"title":"PAP248-286缩氨酸寡聚的原子模拟","authors":"A. O. Nikitina, A. Yulmetov, A. Kusova, V. Klochkov, D. S. Blokhin","doi":"10.26907/2542-064x.2022.2.185-195","DOIUrl":null,"url":null,"abstract":"Amyloid fibrils are ordered aggregates that from a wide variety of soluble proteins and peptides. Amyloid fibrils take part into more than 20 human diseases, including Alzheimer’s, Parkinson, Huntington and HIV infection. The association of certain proteins with the fibril structure formation characterizes the pathological manifestation of amyloid diseases. Clarification of the physicochemical parameters of the amyloid fibril formation is critical to our understanding and subsequent treatment of amyloid diseases. There are several comprehensive studies of self-assembly mechanisms of functional and pathogenic polypeptides. peptide","PeriodicalId":23418,"journal":{"name":"Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki","volume":null,"pages":null},"PeriodicalIF":0.4000,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Atomistic Simulations of PAP248-286 Peptide Oligomerization\",\"authors\":\"A. O. Nikitina, A. Yulmetov, A. Kusova, V. Klochkov, D. S. Blokhin\",\"doi\":\"10.26907/2542-064x.2022.2.185-195\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Amyloid fibrils are ordered aggregates that from a wide variety of soluble proteins and peptides. Amyloid fibrils take part into more than 20 human diseases, including Alzheimer’s, Parkinson, Huntington and HIV infection. The association of certain proteins with the fibril structure formation characterizes the pathological manifestation of amyloid diseases. Clarification of the physicochemical parameters of the amyloid fibril formation is critical to our understanding and subsequent treatment of amyloid diseases. There are several comprehensive studies of self-assembly mechanisms of functional and pathogenic polypeptides. peptide\",\"PeriodicalId\":23418,\"journal\":{\"name\":\"Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.4000,\"publicationDate\":\"2022-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.26907/2542-064x.2022.2.185-195\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.26907/2542-064x.2022.2.185-195","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
Atomistic Simulations of PAP248-286 Peptide Oligomerization
Amyloid fibrils are ordered aggregates that from a wide variety of soluble proteins and peptides. Amyloid fibrils take part into more than 20 human diseases, including Alzheimer’s, Parkinson, Huntington and HIV infection. The association of certain proteins with the fibril structure formation characterizes the pathological manifestation of amyloid diseases. Clarification of the physicochemical parameters of the amyloid fibril formation is critical to our understanding and subsequent treatment of amyloid diseases. There are several comprehensive studies of self-assembly mechanisms of functional and pathogenic polypeptides. peptide