Phe-Gly motifs drive fibrillization of TDP-43’s prion-like domain condensates

Samankaltaisia teoksia

• Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions
  Tekijä: Mompeán, Miguel, et al.
  Julkaistu: (2017)
• Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation
  Tekijä: Mompeán, Miguel, et al.
  Julkaistu: (2016)
• An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds
  Tekijä: Mompeán, Miguel, et al.
  Julkaistu: (2016)
• Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43
  Tekijä: Mompeán, Miguel, et al.
  Julkaistu: (2015)
• Dysregulation of TDP‐43 intracellular localization and early onset ALS are associated with a TARDBP S375G variant
  Tekijä: Newell, Kathy, et al.
  Julkaistu: (2018)