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Showing 1–12 of 12 results
Advanced filters: Author: Dimitry Tegunov Clear advanced filters

  • BamA carries out the essential process of folding outer membrane β-barrels in Gram-negative bacteria and is a potential antibiotic target. Here, the authors discover macrocyclic peptide inhibitors that trap BamA in distinct structural conformations.

    • Dawei Sun
    • Kelly M. Storek
    • Jian Payandeh
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15

  • Small proteins (<50 kDa) are difficult to resolve by cryo-EM due to low signal-to-noise ratios and alignment challenges. Here, authors engineered conformationally rigid antibody fragments (Rigid Fabs) enabling high-resolution cryo-EM structures of small (~20 kDa) proteins like KRAS.

    • Jennifer E. Kung
    • Matthew C. Johnson
    • Jawahar Sudhamsu
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • Remdesivir is a nucleoside analog that inhibits the SARS-CoV-2 RNA dependent RNA polymerase (RdRp) and is used as a drug to treat COVID19 patients. Here, the authors provide insights into the mechanism of remdesivir-induced RdRp stalling by determining the cryo-EM structures of SARS-CoV-2 RdRp with bound RNA molecules that contain remdesivir at defined positions and observe that addition of the fourth nucleotide following remdesivir incorporation into the RNA product is impaired by a barrier to further RNA translocation.

    • Goran Kokic
    • Hauke S. Hillen
    • Patrick Cramer
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-7

  • A cryo-electron microscopy structure of the RNA-dependent RNA polymerase of SARS-CoV-2 sheds light on coronavirus replication and enables the analysis of the inhibitory mechanisms of candidate antiviral drugs.

    • Hauke S. Hillen
    • Goran Kokic
    • Patrick Cramer
    Research
    Nature
    Volume: 584, P: 154-156

  • Jochheim et al report an alternative, dimeric form of the coronavirus SARS-CoV-2 RNA dependent RNA polymerase (RdRp), which is used to replicate and transcribe its genome. They resolve its structure at 5.5 Å resolution and speculate that the dimer facilitates template switching during production of sub-genomic RNAs.

    • Florian A. Jochheim
    • Dimitry Tegunov
    • Patrick Cramer
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-5

  • The NER machinery contains the multisubunit transcription factor IIH (TFIIH) that opens the DNA repair bubble, scans for the lesion, and coordinates excision of the damaged site. Here the authors resolve the cryo-electron microscopy structure of the human core TFIIH-XPA-DNA complex and provide insights into its activation.

    • Goran Kokic
    • Aleksandar Chernev
    • Patrick Cramer
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9

  • The cryo-electron microscopy structure of the 16-subunit yeast SWI/SNF complex RSC in complex with a nucleosome substrate provides insights into the chromatin-remodelling function of this family of protein complexes.

    • Felix R. Wagner
    • Christian Dienemann
    • Patrick Cramer
    Research
    Nature
    Volume: 579, P: 448-451

  • Cryo-electron tomography is used to reveal the structural dynamics and functional diversity of translating ribosomes in Mycoplasma pneumoniae, providing insight into the translation elongation cycle inside cells and how it is reshaped by antibiotics.

    • Liang Xue
    • Swantje Lenz
    • Julia Mahamid
    ResearchOpen Access
    Nature
    Volume: 610, P: 205-211

  • The user-friendly software tool Warp enables automated, on-the-fly preprocessing of cryo-EM data, including motion correction, defocus estimation, particle picking and image denoising.

    • Dimitry Tegunov
    • Patrick Cramer
    Research
    Nature Methods
    Volume: 16, P: 1146-1152

  • The Paf1 complex (Paf1C) is an elongation factor assembly that forms the interface between transcribing Pol II and chromatin factors. Here the authors describe the architecture of Paf1C and its interface with Pol II, and show that Paf1C is globally required for normal mRNA transcription in yeast.

    • Youwei Xu
    • Carrie Bernecky
    • Patrick Cramer
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13