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Transforming binding affinities from three dimensions to two with application to cadherin clustering

Author

Listed:
  • Yinghao Wu

    (Columbia University
    Howard Hughes Medical Institute, Columbia University
    Center for Computational Biology and Bioinformatics, Columbia University)

  • Jeremie Vendome

    (Columbia University
    Howard Hughes Medical Institute, Columbia University
    Center for Computational Biology and Bioinformatics, Columbia University)

  • Lawrence Shapiro

    (Columbia University
    Edward S. Harkness Eye Institute, Columbia University)

  • Avinoam Ben-Shaul

    (Institute of Chemistry and the Fritz Haber Research Center, The Hebrew University)

  • Barry Honig

    (Columbia University
    Howard Hughes Medical Institute, Columbia University
    Center for Computational Biology and Bioinformatics, Columbia University)

Abstract

Interactions on the cell surface Relating the strengths of interactions occurring in two dimensions on membrane surfaces to those measured in three dimensions in solution is a perennial problem in cell biology. Barry Honig and colleagues use a computational and theoretical approach that enables a new type of structurally- and biophysically-driven analysis of processes that occur on cell surfaces. Applying this approach to cadherin-mediated cell adhesion reveals novel principles about how cell–cell interactions drive receptor clustering on membrane surfaces.

Suggested Citation

  • Yinghao Wu & Jeremie Vendome & Lawrence Shapiro & Avinoam Ben-Shaul & Barry Honig, 2011. "Transforming binding affinities from three dimensions to two with application to cadherin clustering," Nature, Nature, vol. 475(7357), pages 510-513, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7357:d:10.1038_nature10183
    DOI: 10.1038/nature10183
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    Cited by:

    1. Lucas M. P. Chataigner & Christos Gogou & Maurits A. Boer & Cátia P. Frias & Dominique M. E. Thies-Weesie & Joke C. M. Granneman & Albert J. R. Heck & Dimphna H. Meijer & Bert J. C. Janssen, 2022. "Structural insights into the contactin 1 – neurofascin 155 adhesion complex," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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