Conformational Activation of Antithrombin by Heparin Involves an Altered Exosite Interaction with Protease

Lignende værker

• Contribution of Exosite Occupancy by Heparin to the Regulation of Coagulation Proteases by Antithrombin
  af: Yang, Likui, et al.
  Udgivet: (2009)
• The Allosteric Mechanism of Activation of Antithrombin as an Inhibitor of Factor IXa and Factor Xa: HEPARIN-INDEPENDENT FULL ACTIVATION THROUGH MUTATIONS ADJACENT TO HELIX D
  af: Dementiev, Alexey, et al.
  Udgivet: (2013)
• Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States
  af: Roth, Ryan, et al.
  Udgivet: (2015)
• Engineering Functional Antithrombin Exosites in α(1)-Proteinase Inhibitor That Specifically Promote the Inhibition of Factor Xa and Factor IXa
  af: Izaguirre, Gonzalo, et al.
  Udgivet: (2009)
• Characterization of the Conformational Alterations, Reduced Anticoagulant Activity, and Enhanced Antiangiogenic Activity of Prelatent Antithrombin
  af: Richard, Benjamin, et al.
  Udgivet: (2008)