Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
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Gui, Xinrui , Luo, Feng , Li, Yichen , Zhou, Heng , Qin, Zhenheng , Liu, Zhenying , Gu, Jinge , Xie, Muyun , Zhao, Kun , Dai, Bin , Shin, Woo Shik , He, Jianhua , He, Lin , Jiang, Lin , Zhao, Minglei , Sun, Bo , Li, Xueming , Liu, Cong and Li, Dan
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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Contents
Subcellular membrane-less organelles consist of proteins with low complexity domains. Many of them, such as hnRNPA1, can assemble into both a polydisperse liquid phase and an ordered solid phase of amyloid fibril. The former mirrors biological granule assembly, while the latter is usually associated with neurodegenerative disease. Here, we observe...
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Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
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TN_cdi_doaj_primary_oai_doaj_org_article_a160475f7cbf47d1b2ddb73a38f8b907
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a160475f7cbf47d1b2ddb73a38f8b907
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-019-09902-7
