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 1–5 of 5 results
Advanced filters: Author: Shifra Lansky Clear advanced filters
  • An improved structure of the TRPV3 pentamer, together with molecular dynamics simulations, provides insights into its conformation, subunit interfaces, permeability to large cations, and the mechanism of transition to the canonical tetrameric state.

    • Shifra Lansky
    • Zhaokun Wang
    • Simon Scheuring
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15
  • Lansky et al. describe the structural analysis of an ultra-multimodular GH43 arabinanase, AbnA. They discover a new carbohydrate binding module and analyze the large conformational transitions of the enzyme with the integrative structure determination approach, which may be applied to the conformational studies of other ultramultimodular proteins as well.

    • Shifra Lansky
    • Rachel Salama
    • Gil Shoham
    ResearchOpen Access
    Communications Biology
    Volume: 5, P: 1-14
  • High-speed atomic force microscopy single-molecule imaging and cryo-EM analysis discover and reveal the structure of a TRPV3 pentamer, providing evidence for a non-canonical pentameric TRP-channel assembly, laying the foundation for new directions in TRP channel research.

    • Shifra Lansky
    • John Michael Betancourt
    • Simon Scheuring
    Research
    Nature
    Volume: 621, P: 206-214
  • A localization algorithm is applied to datasets obtained with conventional and high-speed atomic force microscopy to increase image resolution beyond the limits set by the radius of the tip used.

    • George R. Heath
    • Ekaterina Kots
    • Simon Scheuring
    Research
    Nature
    Volume: 594, P: 385-390
  • Hirudin is a widely studied model for folding of disulfide-rich proteins, which folds through a slow pathway with highly heterogeneous intermediates and scrambled isomers before it reaches its native state. Here the effect of native and non-native diselenide bridges on the kinetics, yield, and heterogeneity of hirudin folding are systematically explored.

    • Reem Mousa
    • Taghreed Hidmi
    • Norman Metanis
    ResearchOpen Access
    Communications Chemistry
    Volume: 4, P: 1-9