Elimination of P1 Arginine 393 Interaction with Underlying Glutamic Acid 255 Partially Activates Antithrombin III for Thrombin Inhibition but Not Factor Xa Inhibition

This publication has 26 references indexed in Scilit:

• Implications for function and therapy of a 2.9 å structure of binary-complexed antithrombin
  Journal of Molecular Biology, 1998
• Conformational Conversion of Antithrombin to a Fully Activated Substrate of Factor Xa without Need for Heparin
  Biochemistry, 1998
• The Oligosaccharide Side Chain on Asn-135 of α-Antithrombin, Absent in β-Antithrombin, Decreases the Heparin Affinity of the Inhibitor by Affecting the Heparin-Induced Conformational Change
  Biochemistry, 1997
• The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site 1 1Edited by R. Huber
  Journal of Molecular Biology, 1997
• Mechanism of Heparin Activation of Antithrombin. Evidence for Reactive Center Loop Preinsertion with Expulsion upon Heparin Binding
  Biochemistry, 1996
• Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the .beta.-antithrombin III isoform with enhanced heparin affinity
  Biochemistry, 1995
• Biological implications of a 3 å structure of dimeric antithrombin
  Structure, 1994
• P1 variant antithrombins Glasgow (393 Arg to His) and Pescara (393 Arg to Pro) have increased heparin affinity and are resistant to catalytic cleavage by elastase Implications for the heparin activation mechanism
  FEBS Letters, 1991
• Determination of Heparin and Related Sulfated Mucopolysaccharides
  Published by Wiley ,1977