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Showing 1–4 of 4 results
Advanced filters: Author: S. L. Reck-Peterson Clear advanced filters

  • LRRK2 is one of the most commonly mutated genes in familial Parkinson’s disease. Here, the authors report a cryo-EM structure of the catalytic half of LRRK2 bound to microtubules, revealing determinants of binding that are independent of LRRK2 kinase activity.

    • David M. Snead
    • Mariusz Matyszewski
    • Samara L. Reck-Peterson
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 1196-1207

  • The processivity of myosins and kinesins has been well studied, but how the dynein homodimer achieves continuous motion is unknown. Two-dimensional analysis of labeled, DNA-dimerized dynein demonstrates that dynein has an unusual stepping pattern and can alternate between stochastic- and tension-based stepping to achieve processivity.

    • Weihong Qiu
    • Nathan D Derr
    • Samara L Reck-Peterson
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 193-200

  • Reimer et al. used cryo-EM and cellular assays to reveal the structural and regulatory features that distinguish LRRK1 from LRRK2, and placed these features in the context of the evolution of the LRRK family of proteins.

    • Janice M. Reimer
    • Andrea M. Dickey
    • Andres E. Leschziner
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1735-1745