Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–10 of 10 results
Advanced filters: Author: Doryen Bubeck Clear advanced filters

  • Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming virulence factors. Cryo-EM structure of an early conformation of the CDC ILY from Streptococcus intermedius, bound to the human immune receptor CD59, provides insight into ILY oligomerization and role of cholesterol in membrane lysis.

    • Nita R. Shah
    • Tomas B. Voisin
    • Doryen Bubeck
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • The membrane attack complex (MAC) is an immune effector that kills pathogens by forming pores in their membrane. Here the authors use cryo-electron microscopy to reveal that the full MAC is an asymmetric pore with a split-washer configuration and identify a network of interactions that provide a basis for sequential assembly.

    • Marina Serna
    • Joanna L. Giles
    • Doryen Bubeck
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-7

  • CD59 protects human cells from damage by the MAC immune pore. The authors show how CD59 inhibits MAC, by deflecting pore-forming β-hairpins of complement proteins. As well as how the membrane environment influences the role of CD59 in complement regulation and in host-pathogen interactions.

    • Emma C. Couves
    • Scott Gardner
    • Doryen Bubeck
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-13

  • To prevent unregulated complement activation, extracellular chaperones capture soluble precursors to the membrane attack complex (sMAC). Here, structural analysis of sMAC reveals how clusterin recognizes heterogeneous sMAC complexes and inhibits polymerization of complement protein C9.

    • Anaïs Menny
    • Marie V. Lukassen
    • Doryen Bubeck
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11

  • The complement membrane attack complex (MAC) is a lytic immune pore that kills pathogens. Here the authors use cryoEM to provide a structural and biophysical mechanism for how β-pore forming proteins breach the lipid bilayer, providing pathways to explore pore-formation in molecular detail.

    • Anaïs Menny
    • Marina Serna
    • Doryen Bubeck
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11

  • The membrane attack complex (MAC) is a hetero-oligomeric protein assembly that kills pathogens by perforating their cell envelopes. Here, the authors use atomic force microscopy to show that MAC proteins oligomerize within the membrane, allowing them to identify the kinetic bottleneck of MAC formation.

    • Edward S. Parsons
    • George J. Stanley
    • Bart W. Hoogenboom
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10