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S T Olson

Showing results (61-70 of 77) with videos related to

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The Journal of Biological Chemistry|April 28, 1995
Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formationS T Olson, A W Stephens, C H Hirs, et al.
Biochemistry|May 31, 2001
The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activationY J Chuang, R Swanson, S M Raja, et al.
Biochemistry|September 26, 2001
Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsinS T Olson, R Swanson, D Day, et al.
The Biochemical Journal|September 15, 1992
Decreased affinity of recombinant antithrombin for heparin due to increased glycosylationI Björk, K Ylinenjärvi, S T Olson, et al.
Biochemistry|September 23, 1986
Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonateD D Roberts, S D Lewis, D P Ballou, et al.
The Journal of Biological Chemistry|June 25, 1992
Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancementS T Olson, I Björk, R Sheffer, et al.
The Journal of Biological Chemistry|August 15, 1990
The COOH-terminal domain of hirudin. An exosite-directed competitive inhibitor of the action of alpha-thrombin on fibrinogenM C Naski, J W Fenton, J M Maraganore, et al.
The Journal of Biological Chemistry|June 15, 1993
Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studiesM M Bernardo, D E Day, H R Halvorson, et al.
Biochemistry|August 24, 1993
Transmission of conformational change from the heparin binding site to the reactive center of antithrombinP G Gettins, B Fan, B C Crews, et al.
The Journal of Biological Chemistry|January 12, 1996
Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinaseP E Bock, D E Day, I M Verhamme, et al.
Pageof 8

Showing results (61-70 of 77) with videos related to

Sort By:
Pageof 8
The Journal of Biological Chemistry|April 28, 1995
Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formationS T Olson, A W Stephens, C H Hirs, et al.
Biochemistry|May 31, 2001
The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activationY J Chuang, R Swanson, S M Raja, et al.
Biochemistry|September 26, 2001
Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsinS T Olson, R Swanson, D Day, et al.
The Biochemical Journal|September 15, 1992
Decreased affinity of recombinant antithrombin for heparin due to increased glycosylationI Björk, K Ylinenjärvi, S T Olson, et al.
Biochemistry|September 23, 1986
Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonateD D Roberts, S D Lewis, D P Ballou, et al.
The Journal of Biological Chemistry|June 25, 1992
Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancementS T Olson, I Björk, R Sheffer, et al.
The Journal of Biological Chemistry|August 15, 1990
The COOH-terminal domain of hirudin. An exosite-directed competitive inhibitor of the action of alpha-thrombin on fibrinogenM C Naski, J W Fenton, J M Maraganore, et al.
The Journal of Biological Chemistry|June 15, 1993
Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studiesM M Bernardo, D E Day, H R Halvorson, et al.
Biochemistry|August 24, 1993
Transmission of conformational change from the heparin binding site to the reactive center of antithrombinP G Gettins, B Fan, B C Crews, et al.
The Journal of Biological Chemistry|January 12, 1996
Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinaseP E Bock, D E Day, I M Verhamme, et al.
Pageof 8