N-terminal region of Drosophila melanogaster Argonaute2 forms amyloid-like aggregates

被引:0
作者
Haruka Narita
Tomohiro Shima
Ryo Iizuka
Sotaro Uemura
机构
[1] The University of Tokyo,Department of Biological Sciences, Graduate School of Science
来源
BMC Biology | / 21卷
关键词
Argonaute; Aggregation; Amyloid; Prion; RNA interference;
D O I
暂无
中图分类号
学科分类号
摘要
引用
收藏
相关论文
共 221 条
[1]  
Denli AM(2003)RNAi: an ever-growing puzzle Trends Biochem Sci 28 196-201
[2]  
Hannon GJ(2009)On the road to reading the RNA-interference code Nature 457 396-404
[3]  
Siomi H(2004)Distinct roles for Argonaute proteins in small RNA-directed RNA cleavage pathways Genes Dev 18 1655-1666
[4]  
Siomi MC(2018)Argonaute proteins and mechanisms of RNA interference in eukaryotes and prokaryotes Biochemistry Moscow 83 483-497
[5]  
Okamura K(2012)The N domain of Argonaute drives duplex unwinding during RISC assembly Nat Struct Mol Biol 19 145-151
[6]  
Ishizuka A(2010)Crystal structure and ligand binding of the MID domain of a eukaryotic Argonaute protein EMBO Rep 11 522-527
[7]  
Siomi H(2005)Structural basis for 5′-end-specific recognition of guide RNA by the A. fulgidus Piwi protein Nature 434 666-70
[8]  
Siomi MC(2003)Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain Nature 426 465-469
[9]  
Olina AV(2004)Crystal structure of a PIWI protein suggests mechanisms for siRNA recognition and slicer activity EMBO J 23 4727-4737
[10]  
Kulbachinskiy AV(2004)Crystal structure of Argonaute and its implications for RISC slicer activity Science 305 1434-1437