Publications by authors named "M C Peckham"

Biallelic mutations in multiple EGF domain protein 10 (MEGF10) gene cause EMARDD (early myopathy, areflexia, respiratory distress and dysphagia) in humans, a severe recessive myopathy, associated with reduced numbers of PAX7 positive satellite cells. To better understand the role of MEGF10 in satellite cells, we overexpressed human MEGF10 in mouse H-2k-tsA58 myoblasts and found that it inhibited fusion. Addition of purified extracellular domains of human MEGF10, with (ECD) or without (EGF) the N-terminal EMI domain to H-2k-tsA58 myoblasts, showed that the ECD was more effective at reducing myoblast adhesion and fusion by day 7 of differentiation, yet promoted adhesion of myoblasts to non-adhesive surfaces, highlighting the importance of the EMI domain in these behaviours.

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Article Synopsis
  • The chapter explains the process of expressing and purifying myosin, a type of cytoskeletal molecular motor, using an insect cell system.
  • It details methods for characterizing the quality of the purified myosin through techniques like mass photometry and negative-stain electron microscopy (EM).
  • Lastly, it describes how to conduct in vitro assays to observe how fluorescently labeled myosin moves along actin tracks and mentions adapting these assays for MINFLUX imaging.
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  • Facets synovial cysts (FSCs) are benign growths from facet joints that can lead to nerve pain, and this study explored the effectiveness of CT-guided procedures for their treatment, comparing IPCR and DF methods.
  • The retrospective review examined 90 FSC rupture attempts on 75 patients over 10 years, revealing that IPCR alone had a 70% success rate, but when combined with DF after IPCR failure, the success rate rose to 90.6%.
  • The study concluded that having the option to use DF after IPCR failure significantly improves treatment outcomes, highlighting the advantages of using CT guidance for these procedures.
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Cortical formins, pivotal for the assembly of linear actin filaments beneath the membrane, exert only minor effects on unconfined cell migration of weakly and moderately adherent cells. However, their impact on migration and mechanostability of highly adherent cells remains poorly understood. Here, we demonstrate that loss of cortical actin filaments generated by the formins mDia1 and mDia3 drastically compromises cell migration and mechanics in highly adherent fibroblasts.

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