Ettelaie, C; Adam, JM; James, NJ; Oke, AO; Harrison, JA; Bunce, TD; Bruckdorfer, KR; (1999) The role of the C-terminal domain in the inhibitory functions of tissue factor pathway inhibitor. Federation of European Biochemical Societies Letters , 463 (3) 341 - 344.
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Tissue factor pathway inhibitor (TFPI) inhibits the activity of coagulation factors VIIa and Xa through Kunitz domains, thereby inhibiting the activity of tissue factor. However, it has been shown that the C-terminal of this inhibitor is essential for the maximal anticoagulant activity of TFPI. We have investigated the endogenous ability of the C-terminal of TFPI to influence coagulation. A synthetic peptide corresponding to residues 254-265 within the C-terminal of TFPI was prepared and shown to be capable of inhibiting tissue factor pathway by preventing the activation of factor VII. Mutational analysis of the peptide revealed the identity of the key lysine residues
|Title:||The role of the C-terminal domain in the inhibitory functions of tissue factor pathway inhibitor|
|Additional information:||UI - 20074928 LA - Eng RN - EC 220.127.116.11 (Factor VIIa) RN - EC 18.104.22.168 (Factor Xa) RN - 0 (lipoprotein-associated coagulation inhibitor) RN - 0 (Anticoagulants) RN - 0 (Lipoproteins) RN - 0 (Peptide Fragments) RN - 9035-58-9 (Thromboplastin) PT - JOURNAL ARTICLE DA - 20000119 IS - 0014-5793 SB - M SB - X CY -NETHERLANDS JC - EUH AA - Author EM - 200003|
|Keywords:||function, Lipoproteins, peptides, Amino Acid Sequence, analysis, antagonists & inhibitors, Anticoagulants, Biochemistry, Blood Coagulation, Cell Line, chemistry, drug effects, Factor VIIa, Factor Xa, lipoprotein associated coagulation inhibitor, Lysine, Mutation, Peptide Fragments, pharmacology, Support, Non-U.S.Gov't, Thromboplastin|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)|
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