Proline Substitutions and Threonine Pseudophosphorylation of the SH3 Ligand of 18.5-kDa Myelin Basic Protein Decrease Its Affinity for the Fyn-SH3 Domain and Alter Process Development and Protein Localization in Oligodendrocytes

Lignende værker

• The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro
  af: De Avila, Miguel, et al.
  Udgivet: (2014)
• Myelin management by the 18.5–kDa and 21.5–kDa classic myelin basic protein isoforms
  af: Harauz, George, et al.
  Udgivet: (2013)
• Classical 18.5-and 21.5-kDa Isoforms of Myelin Basic Protein Inhibit Calcium Influx Into Oligodendroglial Cells, in Contrast to Golli Isoforms
  af: Smith, Graham S.T., et al.
  Udgivet: (2011)
• Classic 18.5- and 21.5-kDa Myelin Basic Protein Isoforms Associate with Cytoskeletal and SH3-Domain Proteins in the Immortalized N19-Oligodendroglial Cell Line Stimulated by Phorbol Ester and IGF-1
  af: Smith, Graham S. T., et al.
  Udgivet: (2012)
• The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein
  af: Vassall, Kenrick A., et al.
  Udgivet: (2013)