The Alexander Disease–Causing Glial Fibrillary Acidic Protein Mutant, R416W, Accumulates into Rosenthal Fibers by a Pathway That Involves Filament Aggregation and the Association of αB-Crystallin and HSP27

Ítems similars

• Glial Fibrillary Acidic Protein Filaments Can Tolerate the Incorporation of Assembly-compromised GFAP-δ, but with Consequences for Filament Organization and αB-Crystallin Association
  per: Perng, Ming-Der, et al.
  Publicat: (2008)
• Oligomers of Mutant Glial Fibrillary Acidic Protein (GFAP) Inhibit the Proteasome System in Alexander Disease Astrocytes, and the Small Heat Shock Protein αB-Crystallin Reverses the Inhibition
  per: Tang, Guomei, et al.
  Publicat: (2010)
• Rosenthal fibers share epitopes with alpha B-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold.
  per: Tomokane, N., et al.
  Publicat: (1991)
• Alexander Disease-Associated Glial Fibrillary Acidic Protein Mutations in Mice Induce Rosenthal Fiber Formation and a White Matter Stress Response
  per: Hagemann, Tracy L., et al.
  Publicat: (2006)
• Relative stabilities of wild-type and mutant glial fibrillary acidic protein in patients with Alexander disease
  per: Heaven, Michael R., et al.
  Publicat: (2019)