Acute effects of desmin mutations on cytoskeletal and cellular integrity in cardiac myocytes

This publication has 52 references indexed in Scilit:

• Synemin May Function to Directly Link Muscle Cell Intermediate Filaments to Both Myofibrillar Z-lines and Costameres
  Published by Elsevier ,2001
• Desmin integrates the three-dimensional mechanical properties of muscles.
  American Journal of Physiology-Cell Physiology, 2001
• Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knock-out mice
  Histochemistry and Cell Biology, 2000
• Desmin Myopathy, a Skeletal Myopathy with Cardiomyopathy Caused by Mutations in the Desmin Gene
  New England Journal of Medicine, 2000
• Molecular Characteristics and Interactions of the Intermediate Filament Protein Synemin
  Journal of Biological Chemistry, 1999
• Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
  Proceedings of the National Academy of Sciences, 1999
• A homozygous nonsense mutation in the PLEC1 gene in patients with epidermolysis bullosa simplex with muscular dystrophy.
  Journal of Clinical Investigation, 1996
• A nontetrameric species is the major soluble form of keratin in Xenopus oocytes and rabbit reticulocyte lysates.
  The Journal of cell biology, 1996
• Differential organization of desmin and vimentin in muscle is due to differences in their head domains.
  The Journal of cell biology, 1994
• Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: Genetic and functional analyses
  Cell, 1991