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DOI | 10.1126/science.aao2825 |
Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy | |
Gremer, Lothar1,2; Schoelzel, Daniel1,2; Schenk, Carla1; Reinartz, Elke2; Labahn, Joerg1,2,3; Ravelli, Raimond B. G.4; Tusche, Markus1; Lopez-Iglesias, Carmen4; Hoyer, Wolfgang1,2; Heise, Henrike1,2; Willbold, Dieter1,2; Schroeder, Gunnar F.1,5 | |
2017-10-06 | |
发表期刊 | SCIENCE |
ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 358期号:6359页码:116-+ |
文章类型 | Article |
语种 | 英语 |
国家 | Germany; Netherlands |
英文摘要 | Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-beta protein (A beta) are the main component of the senile plaques found in brains of Alzheimer's disease patients. We present the structure of an A beta(1-42) fibril composed of two intertwined protofilaments determined by cryo-electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. The backbone of all 42 residues and nearly all side chains are well resolved in the EM density map, including the entire N terminus, which is part of the cross-beta structure resulting in an overall "LS"-shaped topology of individual subunits. The dimer interface protects the hydrophobic C termini from the solvent. The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed "groove" and "ridge," leading to different binding pathways on both fibril ends, which has implications for fibril growth. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000412359600065 |
WOS关键词 | ATOMIC-RESOLUTION STRUCTURE ; AMYLOID-BETA FIBRILS ; ALZHEIMERS-DISEASE ; POLYMORPHISM ; DIMER |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/197017 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Forschungszentrum Julich, Inst Complex Syst, Struct Biochem ICS 6, D-52425 Julich, Germany; 2.Heinrich Heine Univ Dusseldorf, Inst Phys Biol, D-40225 Dusseldorf, Germany; 3.DESY, CSSB, D-22607 Hamburg, Germany; 4.Maastricht Univ, Maastricht Multimodal Mol Imaging Inst, Univ Singel 50, NL-6229 ER Maastricht, Netherlands; 5.Heinrich Heine Univ Dusseldorf, Phys Dept, D-40225 Dusseldorf, Germany |
推荐引用方式 GB/T 7714 | Gremer, Lothar,Schoelzel, Daniel,Schenk, Carla,et al. Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy[J]. SCIENCE,2017,358(6359):116-+. |
APA | Gremer, Lothar.,Schoelzel, Daniel.,Schenk, Carla.,Reinartz, Elke.,Labahn, Joerg.,...&Schroeder, Gunnar F..(2017).Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy.SCIENCE,358(6359),116-+. |
MLA | Gremer, Lothar,et al."Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy".SCIENCE 358.6359(2017):116-+. |
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