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CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-tRNA synthetase

Author

Listed:
  • Weiwei He

    (The Scripps Research Institute)

  • Ge Bai

    (Howard Hughes Medical Institute and Gene Expression Laboratory, The Salk Institute for Biological Studies)

  • Huihao Zhou

    (The Scripps Research Institute)

  • Na Wei

    (The Scripps Research Institute)

  • Nicholas M. White

    (Howard Hughes Medical Institute and Gene Expression Laboratory, The Salk Institute for Biological Studies)

  • Janelle Lauer

    (The Scripps Research Institute)

  • Huaqing Liu

    (University of California San Diego)

  • Yi Shi

    (The Scripps Research Institute)

  • Calin Dan Dumitru

    (The Scripps Research Institute)

  • Karen Lettieri

    (Howard Hughes Medical Institute and Gene Expression Laboratory, The Salk Institute for Biological Studies)

  • Veronica Shubayev

    (University of California San Diego)

  • Albena Jordanova

    (Molecular Neurogenomics Group, University of Antwerp)

  • Velina Guergueltcheva

    (Medical University of Sofia)

  • Patrick R. Griffin

    (The Scripps Research Institute)

  • Robert W. Burgess

    (The Jackson Laboratory)

  • Samuel L. Pfaff

    (Howard Hughes Medical Institute and Gene Expression Laboratory, The Salk Institute for Biological Studies)

  • Xiang-Lei Yang

    (The Scripps Research Institute)

Abstract

Charcot–Marie–Tooth diseases are hereditary peripheral neuropathies for which there are currently no effective therapies; here the type 2D subtype of these diseases is shown to be caused by mutations impeding a signalling pathway necessary for motor neuron survival.

Suggested Citation

  • Weiwei He & Ge Bai & Huihao Zhou & Na Wei & Nicholas M. White & Janelle Lauer & Huaqing Liu & Yi Shi & Calin Dan Dumitru & Karen Lettieri & Veronica Shubayev & Albena Jordanova & Velina Guergueltcheva, 2015. "CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-tRNA synthetase," Nature, Nature, vol. 526(7575), pages 710-714, October.
    • Handle: RePEc:nat:nature:v:526:y:2015:i:7575:d:10.1038_nature15510
    DOI: 10.1038/nature15510
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    Cited by:

    1. Noemi Gioelli & Lisa J. Neilson & Na Wei & Giulia Villari & Wenqian Chen & Bernhard Kuhle & Manuel Ehling & Federica Maione & Sander Willox & Serena Brundu & Daniele Avanzato & Grigorios Koulouras & M, 2022. "Neuropilin 1 and its inhibitory ligand mini-tryptophanyl-tRNA synthetase inversely regulate VE-cadherin turnover and vascular permeability," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Biljana Ermanoska & Bob Asselbergh & Laura Morant & Maria-Luise Petrovic-Erfurth & Seyyedmohsen Hosseinibarkooie & Ricardo Leitão-Gonçalves & Leonardo Almeida-Souza & Sven Bervoets & Litao Sun & LaTas, 2023. "Tyrosyl-tRNA synthetase has a noncanonical function in actin bundling," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

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