Ankyrin Repeat

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  Subject Areas on Research

  • A code for RanGDP binding in ankyrin repeats defines a nuclear import pathway. 
  • A single divergent exon inhibits ankyrin-B association with the plasma membrane. 
  • AnkB, a periplasmic ankyrin-like protein in Pseudomonas aeruginosa, is required for optimal catalase B (KatB) activity and resistance to hydrogen peroxide. 
  • Cryo-electron microscopy structure of the TRPV2 ion channel. 
  • Directionality of temperature activation in mouse TRPA1 ion channel can be inverted by single-point mutations in ankyrin repeat six. 
  • Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations. 
  • Integration of cell-free protein coexpression with an enzyme-linked immunosorbent assay enables rapid analysis of protein-protein interactions directly from DNA. 
  • Mechanical anisotropy of ankyrin repeats. 
  • Mechanical unfolding of an ankyrin repeat protein. 
  • Mutation of conserved histidines alters tertiary structure and nanomechanics of consensus ankyrin repeats. 
  • Quantitation of protein-protein interactions by thermal stability shift analysis. 
  • Structural basis of diverse membrane target recognitions by ankyrins. 
  • The Arabidopsis NPR1 gene that controls systemic acquired resistance encodes a novel protein containing ankyrin repeats. 
  • Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor. 
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  Keywords of People

  • Bennett, Vann, George Barth Geller Distinguished Professor of Molecular Biology, Duke Cancer Institute