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Showing 1–10 of 10 results
Advanced filters: Author: Vladimir Svetlov Clear advanced filters
  • Cryo-EM analysis of the human CST–Polα/primase complex reveals a metazoan-specific mode of interaction between CST and DNA polymerase α that is proposed to function in telomeric recruitment of Polα/primase for C-strand maintenance.

    • Sarah W. Cai
    • John C. Zinder
    • Titia de Lange
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 813-819
  • The exact mechanism by which cellular RNA polymerases translocate and maintain exceptionally high fidelity during transcription remains an important unresolved issue. Two recent structural studies of yeast RNA polymerase II in complex with its potent inhibitor, the fungal toxin α-amanitin, address this matter by describing crucial and surprising details about the dynamic organization of the enzyme catalytic center.

    • Vladimir Svetlov
    • Evgeny Nudler
    News & Views
    Nature Structural & Molecular Biology
    Volume: 15, P: 777-779
  • Direct time-resolved single-molecule observations of promoter search by Escherichia coli RNA polymerase indicate no evidence of facilitated diffusion, according to a new report.

    • Vladimir Svetlov
    • Evgeny Nudler
    News & Views
    Nature Structural & Molecular Biology
    Volume: 20, P: 141-142
  • Polycomb Repressive Complex 2 (PRC2) is a histone methyltransferase whose silencing activity is regulated in part by the selective incorporation of its catalytic subunits EZH1 or EZH2. Here, the authors capture an EZH1-containing PRC2 dimer on a nucleosome, demonstrating significant conformational changes during the process.

    • Daniel Grau
    • Yixiao Zhang
    • Karim-Jean Armache
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12
  • Integrated structure–function studies show that transcription-coupled DNA repair (TCR)—rather than global genomic repair—is responsible for most chromosomal repair events in bacteria, and that TCR mainly occurs independently of the Mfd translocase.

    • Binod K. Bharati
    • Manjunath Gowder
    • Evgeny Nudler
    Research
    Nature
    Volume: 604, P: 152-159
  • Structures of Cdc48 with heterodimeric cofactor Ufd1–Npl4 reveal the location of Npl4's MPN domain above Cdc48’s central pore, thus suggesting how Npl4 engages with polyubiquitinated substrates and promotes their translocation into the ATPase.

    • Nicholas O. Bodnar
    • Kelly H. Kim
    • Tom A. Rapoport
    Research
    Nature Structural & Molecular Biology
    Volume: 25, P: 616-622
  • UvrD acts in nucleotide excision repair by using its helicase/translocase activity to induce RNA polymerase backtracking, enabling repair enzymes to access DNA lesions.

    • Vitaly Epshtein
    • Venu Kamarthapu
    • Evgeny Nudler
    Research
    Nature
    Volume: 505, P: 372-377
  • Small molecules and peptide inhibitors have their benefits and faults when it comes to inhibiting protein-protein interactions. Here, the authors designed a peptoid-peptide hybrid that inhibited β-catenin/TCF interactions, leading to inhibition of Wnt signalling in models of prostate cancer.

    • Jeffrey A. Schneider
    • Timothy W. Craven
    • Susan K. Logan
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10