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- W2266858638 endingPage "644" @default.
- W2266858638 startingPage "633" @default.
- W2266858638 abstract "Thrombin-activatable fibrinolysis inhibitor (TAFI) is an important regulator in the balance of coagulation and fibrinolysis. TAFI is a metallocarboxypeptidase that circulates in plasma as zymogen. Activated TAFI (TAFIa) cleaves C-terminal lysine or arginine residues from peptide substrates. The removal of C-terminal lysine residues from partially degraded fibrin leads to reduced plasmin formation and thus attenuation of fibrinolysis. TAFI also plays a role in inflammatory processes via the removal of C-terminal arginine or lysine residues from bradykinin, thrombin-cleaved osteopontin, C3a, C5a and chemerin. TAFI has been studied extensively over the past three decades and recent publications provide a wealth of information, including crystal structures, mutants and structural data obtained with antibodies and peptides. In this review, we combined and compared available data on structure/function relationships of TAFI." @default.
- W2266858638 created "2016-06-24" @default.
- W2266858638 creator A5018578667 @default.
- W2266858638 creator A5042624694 @default.
- W2266858638 date "2016-04-01" @default.
- W2266858638 modified "2023-10-10" @default.
- W2266858638 title "Structure‐function relationships in thrombin‐activatable fibrinolysis inhibitor" @default.
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- W2266858638 doi "https://doi.org/10.1111/jth.13261" @default.
- W2266858638 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26786060" @default.
- W2266858638 hasPublicationYear "2016" @default.
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