Hotspot Mutations in KIT Receptor Differentially Modulate Its Allosterically Coupled Conformational Dynamics: Impact on Activation and Drug Sensitivity

Podobne zapisy

• Hotspot mutations in KIT receptor differentially modulate its allosterically coupled conformational dynamics: impact on activation and drug sensitivity.
  od: Isaure Chauvot de Beauchêne, i wsp.
  Wydane: (2014-07-01)
• Mutation D816V alters the internal structure and dynamics of c-KIT receptor cytoplasmic region: implications for dimerization and activation mechanisms.
  od: Elodie Laine, i wsp.
  Wydane: (2011-06-01)
• Mutation D816V Alters the Internal Structure and Dynamics of c-KIT Receptor Cytoplasmic Region: Implications for Dimerization and Activation Mechanisms
  od: Laine, Elodie, i wsp.
  Wydane: (2011)
• Allosteric Communication across the Native and Mutated KIT Receptor Tyrosine Kinase
  od: Laine, Elodie, i wsp.
  Wydane: (2012)
• The First 3D Model of the Full-Length KIT Cytoplasmic Domain Reveals a New Look for an Old Receptor
  od: Inizan, François, i wsp.
  Wydane: (2020)