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Structures and Activities of Prions and Prion Proteins

Structures and Activities of Prions and Prion Proteins
朊病毒和朊病毒蛋白的结构和活性
批准号：
10272040
负责人：
BYRON CAUGHEY
金额：
$16.26万
依托单位：
NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES
依托单位国家：
美国
项目类别：
财政年份：
--
资助国家：
美国
项目状态：
未结题
起止时间：
至
来源：
https://reporter.nih.gov/project-details/10272040
关键词：
AmyloidAmyloid FibrilsAmyloid ProteinsBovine Spongiform EncephalopathyBrainChronic Wasting DiseaseCreutzfeldt-Jakob SyndromeCryoelectron MicroscopyDiseaseGoalsLateralMolecularNeurodegenerative DisordersPathogenesisPathologicPrPPrPSc ProteinsPrion DiseasesResolutionRunningScrapieStructureVertebral columnbasebeta pleated sheetdisease transmissionimage reconstructionsynucleintau Proteinstransmission process

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中文摘要
翻译
PrPSc是一种传染性蛋白，其结构尚不清楚。最近一种解决蛋白质淀粉样原纤维结构的方法是冷冻电子显微镜，最近其他研究小组也使用这种方法来揭示与疾病相关的tau和突触核蛋白原纤维的淀粉样核心结构。我们继续寻求基于冷冻电子显微镜的PrPSc结构的阐明。已经取得了进展，侧视图和图像重建显示堆叠的贝塔薄片垂直于纤维轴运行。两张纸之间的间距是4.8A。然而，到目前为止，所获得的分辨率还不足以破译脑源性PrPSc淀粉样纤维核心的骨干折叠。
英文摘要
The structure of the infectious form of prion protein, PrPSc, remains unclear. One recent approach to solving protein amyloid fibril structures is cryo-electron microscopy, which has recently been used by other groups to reveal the amyloid core structures of disease-associated tau and synuclein fibrils. We have continued to pursue cryo-electron microscopy-based elucidation of PrPSc structure. Progress has been made, with lateral views and image reconstructions revealing stacked beta sheets running perpendicular to the fibril axis. The spacing between the sheets is 4.8 A. However, so far the resolution obtained has been insufficient to decipher the backbone folding of the core of amyloid fibrils of brain-derived PrPSc.
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会议论文
Prion Disease Therapeutics
Structures and Activities of Prions and Prion Proteins
Prion Disease Therapeutics
Detection of Prions
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