Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain.

Lignende værker

• Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
  af: Mateu, Mauricio G., et al.
  Udgivet: (1999)
• Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.
  af: McCoy, M, et al.
  Udgivet: (1997)
• Change in oligomerization specificity of the p53 tetramerization domain by hydrophobic amino acid substitutions.
  af: Stavridi, E. S., et al.
  Udgivet: (1999)
• Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor
  af: Fernandez-Fernandez, Maria Rosario, et al.
  Udgivet: (2005)
• Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53
  af: Rajagopalan, Sridharan, et al.
  Udgivet: (2011)