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Showing 1–13 of 13 results
Advanced filters: Author: Olexandr Dybkov Clear advanced filters

  • Ubiquitination is a versatile modification system in eukaryotic cells. Here, the authors unveil that the ubiquitin ligase HUWE1 can modify drug-like small-molecule substrates, beyond proteins. This discovery may be harnessed to develop specific tool substrates or inhibitors of HECT-type ligases.

    • Barbara Orth
    • Pavel Pohl
    • Sonja Lorenz
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-19

  • Sala et al. report the first structural snapshot of the Nipah virus RNA-dependent RNA polymerase in the actively elongating state, uncovering key mechanisms of RNA synthesis by non-segmented negative strand RNA viruses.

    • Fernanda A. Sala
    • Katja Ditter
    • Hauke S. Hillen
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • Here, the authors provide insights into a splicing quality control mechanism. The Gpl1–Gih35 complex binds to the active site of aberrant spliceosomes, blocks splicing progression and triggers the spliceosome discard pathway.

    • Komal Soni
    • Attila Horvath
    • Irmgard Sinning
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 914-925

  • Cryo-electron microscopy structures of the human Integrator complex in three different functional states shed light on how Integrator terminates RNA polymerase II (Pol II) transcription by disengaging Pol II from the DNA template.

    • Isaac Fianu
    • Moritz Ochmann
    • Patrick Cramer
    ResearchOpen Access
    Nature
    Volume: 629, P: 219-227

  • Cryo-electron microscopy structures of cross-exon pre-B and B-like complexes contribute new insights into the molecular mechanisms that mediate the switch from a cross-exon to a cross-intron organized spliceosome.

    • Zhenwei Zhang
    • Vinay Kumar
    • Reinhard Lührmann
    ResearchOpen Access
    Nature
    Volume: 630, P: 1012-1019

  • Using cryo-EM, here the authors structurally delineate the Elongin–RNA polymerase II holocomplex. They show that Elongin allosterically regulates the transcribing RNA polymerase II via a latch that affects its conformational mobility.

    • Ying Chen
    • Goran Kokic
    • Patrick Cramer
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1925-1935

  • The cryo-electron microscopy structure of a newly identified, early spliceosomal complex reveals the mechanism by which the RNA helicase Prp5 enhances the fidelity of the excision of introns from precursor mRNAs.

    • Zhenwei Zhang
    • Norbert Rigo
    • Reinhard Lührmann
    ResearchOpen Access
    Nature
    Volume: 596, P: 296-300

  • The cryo-EM structure of human U2 small nuclear ribonucleoprotein (snRNP) offers insights into what rearrangements are required for this snRNP to be stably incorporated into the spliceosome, and the role that the DEAD-box ATPase PRP5 may have in these rearrangements.

    • Zhenwei Zhang
    • Cindy L. Will
    • Holger Stark
    Research
    Nature
    Volume: 583, P: 310-313

  • The TOM and TIM23 complexes facilitate the transport of nuclear-encoded proteins into the mitochondrial matrix. Here, the authors use a stalled client protein to purify the translocation supercomplex and gain insight into the TOM-TIM23 interface and the mechanism of protein handover from the TOM to the TIM23 complex.

    • Ridhima Gomkale
    • Andreas Linden
    • Peter Rehling
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-17