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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：
10014041
负责人：
BYRON CAUGHEY
金额：
$17.55万
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/10014041
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
感染性朊病毒蛋白PrPSc的结构仍不清楚。最近解决蛋白质淀粉样纤维结构的一种方法是冷冻电子显微镜，其最近已被其他小组用于揭示疾病相关的tau和突触核蛋白纤维的淀粉样蛋白核心结构。我们已经开始追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β片层垂直于原纤维轴。板之间的间距为4.8 A。然而，到目前为止，所获得的分辨率还不足以破译脑源性PrPSc的淀粉样纤维核心的骨架折叠。
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 begun 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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