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Sriram Krishnaswamy, Ph.D.

Professor of Pediatrics
Department: Pediatrics

Contact information
Joseph Stokes Research Institute / CHOP
310 Abramson
3516 Civic Center Blvd.
Philadelphia, PA 19104
Office: (215) 590-3346
Fax: (215) 590-2320
BS (Biology)
Syracuse University, 1979.
Ph.D. (Biochemistry)
Syracuse University, 1984.
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> Perelman School of Medicine   > Faculty   > Details

Description of CVI Expertise

CVI Program Unit(s):
Thrombosis / Hemostasis

CVI Research Description:
The Krishnaswamy Lab focuses on the biochemistry, enzymology and physical biochemistry of the proteolytic reactions of blood coagulation. Our main interests lie in understanding how protein-protein interactions involved in the assembly of the coagulation complexes on membranes modulates enzymic function and how the coagulation enzymes achieve narrow and defined specificity.

Selected Publications

Krishnaswamy, S.: Exosite-Driven Substrate Specificity and Function in Coagulation. J. Thromb. Haemost. 3: 54-67, 2005.

Lu, G., Chhum, S. and Krishnaswamy, S.: The affinity of protein C for the thrombin-thrombomodulin complex is determined in a primary way by active site-dependent interactions. J. Biol. Chem. 280: 15471-15478, 2005.

Bianchini, E.P., Orcutt, S.J., Panizzi, P., Bock, P.E. and Krishnaswamy, S.: Ratcheting of the Substrate from the Zymogen to Proteinase Conformations Directs Sequential Cleavage of Prothrombin by Prothrombinase. Proc. Natl. Acad. Sci. U.S.A. 102: 10099-10104, 2005.

Cao, W., Krishnaswamy, S., Camire, R.M., Lenting, P.J. and Zheng, X.L.: Factor VIII accelerates proteolytic cleavage of von Willebrand factor by ADAMTS13. Proc. Natl. Acad. Sci. U.S.A. 105: 7416-7421, 2008.

Hacisalihoglu, A., Panizzi, P., Bock, P.E., Camire, R.M. and Krishnaswamy, S.: Restricted Active Site Docking by Enzyme-Bound Substrate Enforces the Ordered Cleavage of Prothrombin by Prothrombinase. J. Biol. Chem. 282: 32974 – 32982, 2007.

Kamath, P. and Krishnaswamy, S.: Fate of Membrane-Bound Reactants and Products during the Activation of Human Prothrombin by Prothrombinase. J. Biol. Chem. 283: 30164-30173, 2008.

Bradford, H.N., Miccuci, J.A. and Krishnaswamy, S.: Regulated Cleavage of Prothrombin by Prothrombinase. Repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrate. J. Biol. Chem. 285: 328-338, 2010.

Buddai, S.K., Lu, G., Layzer, J., Rusconi, C.P., Sullenger, B.A., Monroe, D. and Krishnaswamy, S.: An anticoagulant RNA aptamer that inhibits proteinase-cofactor interactions within prothrombinase. J. Biol. Chem. 285: 5212-5223, 2010.

Kamath, P., Huntington, J.A. and Krishnaswamy, S.: Ligand binding shuttles thrombin along a continuum of zymogen-like and proteinase-like states. J. Biol. Chem. 285: 28651-28658, 2010.

Kroh, H.K., Panizzi, P., Tchaikovski, S., Wei, N., Krishnaswamy, S. , Tans, G., Rosing, J., Furie, B., Furie, B.C. and Bock, P.E.: Active site-labeled prothrombin inhibits prothrombinase in vitro and thrombosis in vivo. J. Biol. Chem. 286: 23345-23356, 2011.

Bradford, H.N. and Krishnaswamy, S.: Meizothrombin is an Unexpectedly Zymogen-Like Variant of Thrombin. J. Biol.Chem. 287: 30914-30925, 2012.

Vadivel, K., Agah, S., Messer, A.S., Cascio, D., Bajaj, M.S., Krishnaswamy, S., Esmon, C.T., Padmanabhan, K. and Bajaj, S.P.: Structural and Functional Studies of -Carboxyglutamic Acid Domains of Factor VIIa and Activated Protein C: Role of Magnesium at Physiological Calcium. J. Mol. Biol. 425: 1961-1981, 2013.

Krishnaswamy, S.: The Transition of Prothrombin to Thrombin. J. Thromb. Hemostas. 11: 265-276, 2013.

Bradford, H.N., Orcutt, S.J. and Krishnaswamy, S.: Membrane Binding by Prothrombin Mediates its Constrained Presentation to Prothrombinase For Cleavage. J. Biol.Chem. in press, 2013.

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Last updated: 02/19/2019
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