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Susan Bock

Affiliations: 
University of Utah, Salt Lake City, UT 
Area:
Pharmaceutical Chemistry, Biochemistry
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"Susan Bock"
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Richard G. dela Cruz grad student 2006 University of Utah

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Roth R, Swanson R, Izaguirre G, et al. (2015) Saturation mutagenesis of the antithrombin reactive center loop P14 residue supports a 3-step mechanism of heparin allosteric activation involving intermediate and fully-activated states. The Journal of Biological Chemistry
Boucher L, de la Cruz R, Bock S, et al. (2009) Conformational Dynamics of Antithrombin III With its Allosteric Activator Heparin Biophysical Journal. 96: 69a
Schedin-Weiss S, Desai UR, Bock SC, et al. (2004) Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change. Biochemistry. 43: 675-83
Jairajpuri MA, Lu A, Desai U, et al. (2003) Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation. The Journal of Biological Chemistry. 278: 15941-50
Schedin-Weiss S, Arocas V, Bock SC, et al. (2002) Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding. Biochemistry. 41: 12369-76
Olson ST, Björk I, Bock SC. (2002) Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants. Trends in Cardiovascular Medicine. 12: 198-205
Jairajpuri MA, Lu A, Bock SC. (2002) Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition. The Journal of Biological Chemistry. 277: 24460-5
Schedin-Weiss S, Desai UR, Bock SC, et al. (2002) Importance of lysine 125 for heparin binding and activation of antithrombin. Biochemistry. 41: 4779-88
Arocas V, Bock SC, Raja S, et al. (2001) Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding. The Journal of Biological Chemistry. 276: 43809-17
Chuang YJ, Swanson R, Raja SM, et al. (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 activation. Biochemistry. 40: 6670-9
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