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Showing 1–17 of 17 results
Advanced filters: Author: Leemor Joshua-Tor Clear advanced filters

  • The structure of mouse Dis3l2 bound to an oligoU substrate shows a funnel-like substrate-binding site with the RNA being fed into the active site along a path that is distinct from that seen in the related catalytic subunit of the exosome — 12 uracils of the oligoU-tailed RNA are recognized in a complex network of interactions, suggesting the basis for target specificity.

    • Christopher R. Faehnle
    • Jack Walleshauser
    • Leemor Joshua-Tor
    Research
    Nature
    Volume: 514, P: 252-256

  • Examination of the viral E1 hexameric helicase structure finds that a loop of each subunit becomes attached to a nucleotide and remains associated with it during the next six steps of translocation, thereby escorting a single nucleotide through the channel.

    • Eric J. Enemark
    • Leemor Joshua-Tor
    Research
    Nature
    Volume: 442, P: 270-275

  • Garg et al. determined structures of human Fructosamine-3-kinase (FN3K) bound with different nucleotide analogues and a small molecule sugar mimic substrate. Accompanied by biochemical analysis, they revealed features of the enzyme important for kinase activity and sugar moiety dynamics, providing mechanistic insights into FN3K function.

    • Ankur Garg
    • Kin Fan On
    • Leemor Joshua-Tor
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • RNA interference (RNAi) is a process by which small noncoding RNAs direct molecular machinery to silence gene expression. In this Review, Ipsaro and Joshua-Tor discuss the mechanisms and structures that govern RNAi in higher organisms.

    • Jonathan J Ipsaro
    • Leemor Joshua-Tor
    Reviews
    Nature Structural & Molecular Biology
    Volume: 22, P: 20-28

  • The authors employ cryogenic electron microscopy and kinetic analysis to characterize the discrete steps of how the Dis3L2 3′–5′ exoribonuclease recognizes and degrades structured RNA targets.

    • Katarina Meze
    • Armend Axhemi
    • Leemor Joshua-Tor
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 339-347

  • Structural analysis of the uridyl transferases TUT4 and TUT7 reveals the use of two functional modules in the switch from monouridylation of pre-let-7, which promotes let-7 expression, to oligouridylation of pre-let-7, which marks it for degradation.

    • Christopher R Faehnle
    • Jack Walleshauser
    • Leemor Joshua-Tor
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 658-665

  • The RITS complex links the RNAi pathway with centromeric heterochromatin formation in fission yeast and comprises the chromodomain protein Chp1, the GW protein Tas3 and the argonaute protein Ago1. X-ray analysis of the structured core of the Chp1–Tas3 subcomplex reveals the presence of a C-terminal PIN domain in Chp1, which contributes to post-transcriptional gene silencing of subtelomeric transcripts independently of RNAi.

    • Thomas Schalch
    • Godwin Job
    • Leemor Joshua-Tor
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1351-1357

  • PIWI-interacting RNAs (piRNAs) are regulatory RNAs that bind to PIWI proteins to control transposons and maintain genome integrity. Here the authors characterized their binding specificity and reveal the 5′ nucleotide bias of the Drosophila Piwi protein, through mutation of its specificity loop.

    • Chad B. Stein
    • Pavol Genzor
    • Astrid D. Haase
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-8

  • Independent but complementary studies from Vakoc and Stegmaier identify and characterize a role for ETV6 in counteracting the transcriptional activity of EWS-FLI1 during Ewing sarcoma development, which may be targeted for therapeutic benefits.

    • Yuan Gao
    • Xue-Yan He
    • Christopher R. Vakoc
    Research
    Nature Cell Biology
    Volume: 25, P: 298-308

  • The activity of protein tyrosine phosphatase PTP1B, a major metabolic regulator, depends on its oxidation state. Here the authors identify and characterize a small molecule that targets the oxidized, inactive form of PTP1B, suggesting a new therapeutic approach to diabetes and obesity.

    • Navasona Krishnan
    • Christopher A. Bonham
    • Nicholas K. Tonks
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-17