L
Leemor Joshua-Tor
Researcher at Cold Spring Harbor Laboratory
Publications - 98
Citations - 13000
Leemor Joshua-Tor is an academic researcher from Cold Spring Harbor Laboratory. The author has contributed to research in topics: Argonaute & RNA interference. The author has an hindex of 41, co-authored 90 publications receiving 11865 citations. Previous affiliations of Leemor Joshua-Tor include Weizmann Institute of Science & University of Southern California.
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Journal ArticleDOI
Argonaute2 Is the Catalytic Engine of Mammalian RNAi
Jidong Liu,Michelle A. Carmell,Michelle A. Carmell,Fabiola V. Rivas,Carolyn G. Marsden,J. Michael Thomson,Ji-Joon Song,Scott M. Hammond,Leemor Joshua-Tor,Gregory J. Hannon +9 more
TL;DR: The evidence supports a model in which Argonaute contributes “Slicer” activity to RISC, providing the catalytic engine for RNAi.
Journal ArticleDOI
Crystal Structure of Argonaute and Its Implications for RISC Slicer Activity
Ji-Joon Song,Ji-Joon Song,Stephanie K. Smith,Gregory J. Hannon,Leemor Joshua-Tor,Leemor Joshua-Tor +5 more
TL;DR: The architecture of the molecule and the placement of the PAZ and PIWI domains define a groove for substrate binding and suggest a mechanism for siRNA-guided mRNA cleavage.
Journal ArticleDOI
Purified Argonaute2 and an siRNA form recombinant human RISC.
Fabiola V. Rivas,Niraj H. Tolia,Niraj H. Tolia,Ji-Joon Song,Ji-Joon Song,Juan P Aragon,Jidong Liu,Gregory J. Hannon,Leemor Joshua-Tor,Leemor Joshua-Tor +9 more
TL;DR: It is demonstrated that recombinant, human Argonaute2 can combine with a small interfering RNA (siRNA) to form minimal RISC that accurately cleaves substrate RNAs and provide a source of recombinant enzyme for detailed biochemical studies of the RNAi effector complex.
Journal ArticleDOI
Analysis of the C. elegans Argonaute Family Reveals that Distinct Argonautes Act Sequentially during RNAi
Erbay Yigit,Pedro J. Batista,Yanxia Bei,Ka Ming Pang,Chun-Chieh G. Chen,Niraj H. Tolia,Leemor Joshua-Tor,Shohei Mitani,Martin J. Simard,Craig C. Mello +9 more
TL;DR: Analysis of single- and multiple-AGO mutant strains reveals functions in several pathways, including chromosome segregation, fertility, and at least two separate steps in the RNAi pathway, supporting a two-step model for RNAi.
Journal ArticleDOI
The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes
Ji-Joon Song,Jidong Liu,Niraj H. Tolia,Niraj H. Tolia,Jonathan I. Schneiderman,Stephanie K. Smith,Stephanie K. Smith,Robert A. Martienssen,Gregory J. Hannon,Leemor Joshua-Tor,Leemor Joshua-Tor +10 more
TL;DR: The crystal structure of the PAZ domain of Drosophila Argonaute2 is solved, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.