A Kinetic Analysis of the Tissue Plasminogen Activator and DSPAα1 Cofactor Activities of Untreated and TAFIa-treated Soluble Fibrin Degradation Products of Varying Size-Reference-Cited by-同舟云学术

A Kinetic Analysis of the Tissue Plasminogen Activator and DSPAα1 Cofactor Activities of Untreated and TAFIa-treated Soluble Fibrin Degradation Products of Varying Size

Published:2001-02 Issue:5 Volume:276 Page:3138-3148
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Walker John B.,Nesheim Michael E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference18 articles.

1. Structural Features Mediating Fibrin Selectivity of Vampire Bat Plasminogen Activators

2. Characterization of the Interactions of Plasminogen and Tissue and Vampire Bat Plasminogen Activators with Fibrinogen, Fibrin, and the Complex of d-Dimer Noncovalently Linked to Fragment E

3. A Steady-state Template Model That Describes the Kinetics of Fibrin-stimulated [Glu1]- and [Lys78]Plasminogen Activation by Native tissue-type Plasminogen Activator and Variants That Lack Either the Finger or Kringle-2 Domain

4. The dissociation constants and stoichiometries of the interactions of Lys-plasminogen and chloromethyl ketone derivatives of tissue plasminogen activator and the variant delta FEIX with intact fibrin.

5. Characterization of the binding of plasminogen to fibrin surfaces: The role of carboxy-terminal lysines

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