Tissue factor mutated at the allosteric Cys186-Cys209 disulfide bond is severely impaired in decrypted procoagulant activity

Blood. 2010 Jul 22;116(3):500-1; author reply 502-3. doi: 10.1182/blood-2010-04-281287.
No abstract available

Publication types

  • Comment
  • Letter
  • Research Support, N.I.H., Extramural

MeSH terms

  • Allosteric Site / genetics
  • Amino Acid Substitution
  • Cystine / chemistry
  • Disulfides / chemistry
  • Endothelial Cells / metabolism
  • Factor VIIa / metabolism
  • Humans
  • In Vitro Techniques
  • Mutagenesis, Site-Directed
  • Mutant Proteins / chemistry
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Thromboplastin / chemistry
  • Thromboplastin / genetics*
  • Thromboplastin / metabolism*
  • Transduction, Genetic

Substances

  • Disulfides
  • Mutant Proteins
  • Recombinant Proteins
  • Cystine
  • Thromboplastin
  • Factor VIIa