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Showing 1–9 of 9 results
Advanced filters: Author: Christos G. Savva Clear advanced filters

  • Cryo-electron microscopy structures of DNA helicases in various conformations provide insight into an ATP-hydrolysis-dependent ‘entropy switch’ that drives unwinding of DNA for replication, with probable conservation across viral and eukaryotic systems.

    • Taha Shahid
    • Ammar U. Danazumi
    • Alfredo De Biasio
    ResearchOpen Access
    Nature
    Volume: 641, P: 240-249

  • Aryl hydrocarbon receptor (AHR) is a sensor of the chemical environment including pollutants, diet components and metabolites. Here, authors determine the structure of the indirubin-bound AHR cytosolic complex providing mechanistic insights into ligand-binding promiscuity and selectivity.

    • Jakub Gruszczyk
    • Loïc Grandvuillemin
    • William Bourguet
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-13

  • Pol δ bound to the proliferating cell nuclear antigen (PCNA) replicates the lagging strand in eukaryotes and cooperates with flap endonuclease 1 (FEN1) to process the Okazaki fragments for their ligation. Here, the authors present a Cryo-EM structure of the human 4-subunit Pol δ bound to DNA and PCNA in a replicating state with an incoming nucleotide in the active site.

    • Claudia Lancey
    • Muhammad Tehseen
    • Alfredo De Biasio
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • Epsilon toxin (Etx) is a potent pore forming toxin (PFT) produced by Clostridium perfringens. Here authors show the cryo-EM structure of the Etx pore assembled on the membrane of susceptible cells and shed light on pore formation and mutant phenotypes.

    • Christos G. Savva
    • Alice R. Clark
    • Monika Bokori-Brown
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • Lysenin is member of the aerolysin family of small ß-barrel pore-forming toxins that include virulence factors from several human and animal pathogens. Here the authors determine the structure of the lysenin pore by single particle cryo- EM and propose a conserved pore formation mechanism for the aerolysin protein family.

    • Monika Bokori-Brown
    • Thomas G. Martin
    • Christos G. Savva
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-7

  • The MiDAC complex recruits class I histone deacetylases to chromatin but little is known about its precise structure and function. Here, the authors explore the role of MiDAC in the cell cycle and during mouse embryogenesis, and present cryoEM structures that provide insight into MiDAC’s mode of assembly.

    • Robert E. Turnbull
    • Louise Fairall
    • John W. R. Schwabe
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-15

  • This study determines the structure of the spliceosomal tri-snRNP complex (containing three small nuclear RNAs and more than 30 proteins) by single-particle cryo-electron microscopy; the resolution is sufficient to discern the organization of RNA and protein components involved in spliceosome activation, exon alignment and catalysis.

    • Thi Hoang Duong Nguyen
    • Wojciech P. Galej
    • Kiyoshi Nagai
    Research
    Nature
    Volume: 523, P: 47-52