Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion
Misfolded SOD1 has been linked to both familial and sporadic ALS. Here the authors have determined the cryo-EM structure of SOD1 fibrils, providing insights into the conversion of SOD1 from its immature form into an aggregated form during pathogenesis of ALS.
| Main Authors: | , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-31240-4 |
| _version_ | 1811241177373999104 |
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| author | Li-Qiang Wang Yeyang Ma Han-Ye Yuan Kun Zhao Mu-Ya Zhang Qiang Wang Xi Huang Wen-Chang Xu Bin Dai Jie Chen Dan Li Delin Zhang Zhengzhi Wang Liangyu Zou Ping Yin Cong Liu Yi Liang |
| author_facet | Li-Qiang Wang Yeyang Ma Han-Ye Yuan Kun Zhao Mu-Ya Zhang Qiang Wang Xi Huang Wen-Chang Xu Bin Dai Jie Chen Dan Li Delin Zhang Zhengzhi Wang Liangyu Zou Ping Yin Cong Liu Yi Liang |
| author_sort | Li-Qiang Wang |
| collection | DOAJ |
| description | Misfolded SOD1 has been linked to both familial and sporadic ALS. Here the authors have determined the cryo-EM structure of SOD1 fibrils, providing insights into the conversion of SOD1 from its immature form into an aggregated form during pathogenesis of ALS. |
| first_indexed | 2024-04-12T13:31:42Z |
| format | Article |
| id | doaj.art-1fb6b2ede32243acbbe9925f98323c3c |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-12T13:31:42Z |
| publishDate | 2022-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-1fb6b2ede32243acbbe9925f98323c3c2022-12-22T03:31:09ZengNature PortfolioNature Communications2041-17232022-06-0113111010.1038/s41467-022-31240-4Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversionLi-Qiang Wang0Yeyang Ma1Han-Ye Yuan2Kun Zhao3Mu-Ya Zhang4Qiang Wang5Xi Huang6Wen-Chang Xu7Bin Dai8Jie Chen9Dan Li10Delin Zhang11Zhengzhi Wang12Liangyu Zou13Ping Yin14Cong Liu15Yi Liang16Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesHubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesHubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityNational Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Huazhong Agricultural UniversityDepartment of Neurology, the Second Clinical Medical College, Jinan University (Shenzhen People’s Hospital)Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityInstitute of Nano Biomedicine and Engineering, Department of Instrument Science and Engineering, School of Electronic Information and Electrical Engineering, Shanghai Jiao Tong UniversityHubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityKey Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Bio-X Institutes, Shanghai Jiao Tong UniversityNational Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Huazhong Agricultural UniversitySchool of Civil Engineering, Wuhan UniversityDepartment of Neurology, the Second Clinical Medical College, Jinan University (Shenzhen People’s Hospital)National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Huazhong Agricultural UniversityInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesHubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityMisfolded SOD1 has been linked to both familial and sporadic ALS. Here the authors have determined the cryo-EM structure of SOD1 fibrils, providing insights into the conversion of SOD1 from its immature form into an aggregated form during pathogenesis of ALS.https://doi.org/10.1038/s41467-022-31240-4 |
| spellingShingle | Li-Qiang Wang Yeyang Ma Han-Ye Yuan Kun Zhao Mu-Ya Zhang Qiang Wang Xi Huang Wen-Chang Xu Bin Dai Jie Chen Dan Li Delin Zhang Zhengzhi Wang Liangyu Zou Ping Yin Cong Liu Yi Liang Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion Nature Communications |
| title | Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion |
| title_full | Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion |
| title_fullStr | Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion |
| title_full_unstemmed | Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion |
| title_short | Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion |
| title_sort | cryo em structure of an amyloid fibril formed by full length human sod1 reveals its conformational conversion |
| url | https://doi.org/10.1038/s41467-022-31240-4 |
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