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Showing 1–8 of 8 results
Advanced filters: Author: Julien Robert-Paganin Clear advanced filters
  • Here, Robert-Paganin et al. show that myosin A from Plasmodium falciparum is critical for red blood cell invasion and that non-canonical interactions and regulated phosphorylation are important for force generation during parasite invasion.

    • Julien Robert-Paganin
    • James P. Robblee
    • Anne Houdusse
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12
  • Omecamtiv mecarbil and Mavacamten are small molecules directly modulating the force produced by β-cardiac myosin. In this work, the authors describe how the modulators Omecamtiv mecarbil and Mavacamten can have opposite effects on cardiac myosin force production despite occupying the same pocket.

    • Daniel Auguin
    • Julien Robert-Paganin
    • Anne Houdusse
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14
  • The authors report the high-resolution structure of human β-cardiac myosin in its sequestered state. The results provide insights into the cardiac regulation and represent a tool to investigate the development of inherited cardiomyopathies.

    • Alessandro Grinzato
    • Daniel Auguin
    • Julien Robert-Paganin
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12
  • Hypertrophic cardiomyopathy (HCM) is caused by point mutations in sarcomeric proteins. Here the authors develop an optimized model of the sequestered state of cardiac myosin and define the features affecting the lever arm compliance, allowing them to group mutations in classes and to elucidate the molecular mechanisms leading to cardiac dysfunction in HCM.

    • Julien Robert-Paganin
    • Daniel Auguin
    • Anne Houdusse
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13
  • Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.

    • Julien Robert-Paganin
    • Xiao-Ping Xu
    • Dorit Hanein
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11
  • Omecamtiv mecarbil (OM) is a cardiac myosin activator that is currently in clinical trials for heart failure treatment. Here, the authors give insights into its mode of action and present the crystal structure of OM bound to bovine cardiac myosin, which shows that OM stabilizes the pre-powerstroke state of myosin.

    • Vicente J. Planelles-Herrero
    • James J. Hartman
    • Anne Houdusse
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10