Alireza R. Rezaie, Ph.D.
Understanding the mechanism by which coagulation proteases interact with their target cofactors, substrates, and inhibitors, and how heparin enhances the inhibitory function of antithrombin in the regulation of the proteolytic activities of these proteases.
Office: DRC, Room 417
Voice: (314) 977-9240
Ph.D., 1989, Boston University
Our research is primarily focused on understanding the mechanism by which coagulation proteases interact with their target cofactors, substrates, and inhibitors, and how heparin enhances the inhibitory function of antithrombin in the regulation of the proteolytic activities of these proteases. Another project in the lab focuses on understanding the mechanism by which coagulation proteases interact with endothelial cell surface receptors to elicit diverse intracellular signaling responses. We employ biophysical, biochemical, and molecular biological approaches to study these questions.
- Thrombomodulin modulates cell migration in human melanoma cell lines.
de Oliveira Ada S, Yang L, et al. Melanoma Res. (2014) 24(1):11-9.
- Polyphosphate amplifies proinflammatory responses of nuclear proteins through interaction with receptor for advanced glycation end products and P2Y1 purinergic receptor.
Dinarvand P, Hassanian SM, et al. Blood. (2013) Nov 19 [Epub ahead of print].
- Thrombin inhibits HMGB1-mediated proinflammatory signaling responses when endothelial protein C receptor is occupied by its natural ligand.
Bae JS, Rezaie AR. BMB Rep. (2013) 46(11):544-9.
- The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
Ding Q, Shen Y, et al. Thromb Haemost. (2013) 110(1):53-61.
- Transmitting the allosteric signal in methylglyoxal synthase.
Falahati H, Pazhang M, et al. Protein Eng Des Sel. (2013) 26(7):445-52.
- Antithrombin is protective against myocardial ischemia and reperfusion injury.
Wang J, Wang Y, et al. J Thromb Haemost. (2013) 11(6):1020-8.
- Residues of the 39-loop restrict the plasma inhibitor specificity of factor IXa.
Yang L and Rezaie AR. J Biol Chem. (2013) 288(18):12692-8.
- Variable contributions of basic residues forming an APC exosite in the binding and inactivation of factor VIIIa.
Takeyama M, Wintermute JM, et al. Biochemistry. (2013) 52(13):2228-35.
- Expression and functional characterization of natural R147W and K150del variants of protein C in the Chinese population.
Ding Q, Yang L, et al. Thromb Haemost. (2013) 109(4):614-24.
- Phosphatidylserine-induced Factor Xa dimerization and binding to Factor Va are competing processes in solution.
Majumder R, Koklic T, et al. Biochemistry. (2013) 52(1):143-51.
- Contribution of the NH2-terminal EGF-domain of factor IXa to the specificity of intrinsic tenase.
Qureshi SH, Yang L, Rezaie AR. Thromb Haemost. (2012) 108(6):1154-64.
- Activated protein C modulates cardiac metabolism and augments autophagy in the ischemic heart.
Costa R, Morrison A, et al. J Thromb Haemost. (2012) 10(9):1736-445.
- Characterization of the heparin-binding site of the protein z-dependent protease inhibitor.
Yang L, Ding Q, et al. Biochemistry. (2012) 51(19):4078-85.
- Identification of exosite residues of factor Xa involved in recognition of PAR-2 on endothelial cells.
Manithody C, Yang L, et al. Biochemistry. (2012) 51(12):2551-7.
- Polyphosphate elicits pro-inflammatory responses that are counteracted by activated protein C in both cellular and animal models.
Bae JS, Lee W, et al. J Thromb Haemost. (2012) 10(6):1145-51.
- Determinants of the specificity of protease-activated receptors 1 and 2 signaling by factor Xa and thrombin.
Rana S, Yang L, et al. J Cell Biochem. (2012) 113(3):977-84.