Rezaie, 2001 - Google Patents
Vitronectin functions as a cofactor for rapid inhibition of activated protein C by plasminogen activator inhibitor-1: implications for the mechanism of profibrinolytic action …Rezaie, 2001
View HTML- Document ID
- 12790433796561872043
- Author
- Rezaie A
- Publication year
- Publication venue
- Journal of Biological Chemistry
External Links
Snippet
Activated protein C (APC) is a natural anticoagulant in plasma that down-regulates the coagulation cascade by degrading factors Va and VIIIa. In addition to its anticoagulant function, APC is also known to possess a profibrinolytic property. This property of APC has …
- 108010022233 Plasminogen Activator Inhibitor 1 0 title abstract description 95
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Rezaie | Vitronectin functions as a cofactor for rapid inhibition of activated protein C by plasminogen activator inhibitor-1: implications for the mechanism of profibrinolytic action of activated protein C | |
| Simhadri et al. | Single synonymous mutation in factor IX alters protein properties and underlies haemophilia B | |
| Han et al. | Isolation of a protein Z-dependent plasma protease inhibitor | |
| Wilczynska et al. | The Inhibition Mechanism of Serpins: EVIDENCE THAT THE MOBILE REACTIVE CENTER LOOP IS CLEAVED IN THE NATIVE PROTEASE-INHIBITOR COMPLEX (∗) | |
| Kokame et al. | Activation of thrombin-activable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C | |
| Wang et al. | Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation | |
| Rezaie | Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding | |
| Zhou et al. | The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop | |
| Franzke et al. | Antileukoprotease inhibits stratum corneum chymotryptic enzyme: evidence for a regulative function in desquamation | |
| Rezaie | Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism: evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa | |
| Baglia et al. | Thrombin-mediated feedback activation of factor XI on the activated platelet surface is preferred over contact activation by factor XIIa or factor XIa | |
| Gould et al. | Unique in vivo modifications of coagulation factor V produce a physically and functionally distinct platelet-derived cofactor: characterization of purified platelet-derived factor V/Va | |
| Dickinson et al. | Active site modification of factor VIIa affects interactions of the protease domain with tissue factor | |
| Moraga et al. | Activation of primary human monocytes by the oxidized form of α1-antitrypsin | |
| Rezaie | Role of residue 99 at the S2 subsite of factor Xa and activated protein C in enzyme specificity | |
| Dang et al. | Selective loss of fibrinogen clotting in a loop-less thrombin | |
| Hopkins et al. | Development of a novel recombinant serpin with potential antithrombotic properties | |
| Geng et al. | A sequential mechanism for exosite-mediated factor IX activation by factor XIa | |
| Bijnens et al. | Importance of the hinge region between α-helix F and the main part of serpins, based upon identification of the epitope of plasminogen activator inhibitor type 1 neutralizing antibodies | |
| Gils et al. | Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1 | |
| Mundada et al. | Structure-function analysis of the streptokinase amino terminus (residues 1–59) | |
| Leipold et al. | Mathematical Model of Serine Protease Inhibition in the Tissue Factor Pathway to Thrombin (∗) | |
| Izaguirre et al. | Residues Tyr253 and Glu255 in strand 3 of β-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa | |
| Rezaie et al. | Contribution of residue 192 in factor Xa to enzyme specificity and function | |
| Soejima et al. | Factor VIIa modified in the 170 loop shows enhanced catalytic activity but does not change the zymogen-like property |