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Dipali Sinha, PhD

Associate Professor, Sol Sherry Thrombosis Research Center

Telephone:  215-707-4458

Fax:  215-707-3005

Email: dipali@temple.edu

Sol Sherry Thrombosis Research Center

Presidency College, India  

1960-1962, B.S., Chemistry

 

Calcutta University, India

1962-1964, M.S., Chemistry

 

Calcutta University, India 

1971, Ph.D., Chemistry

 

Miami University, Oxford, OH

1970-1971, Postdoctoral Fellow

 

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The focus of my research is in the area of blood coagulation and fibrinolysis. Deficiency in blood coagulation factor IX (FIX) underlies the  hemophilia syndrome known as hemophilia B, which produces a severe hemorrhagic state.  Activation of FIX is essential for the formation of clot at the site of tissue injury.   FIX can be activated by factor VIIa/tissue factor complex in the extrinsic pathway or by factor XIa (FXIa) in the intrinsic pathway.   My research focuses on the mechanism of activation of FIX by FXIa and identifying inhibitors and promoters for this important activation process.  Deficiency of FXI may also cause bleeding and it is essential in the consolidation phase of blood coagulation.  A major part of my investigation involves elucidation of structure/function relationship of FXI and its activated form FXIa.

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Recent Medically Related Publications, Obtained from PubMed (Click on PubMed ID to view abstract)

18441012. Wu W, Sinha D, Shikov S, Yip CK, Walz T, Billings PC, Lear JD, Walsh PN, Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa. J Biol Chem 283:27(18655-64)2008 Jul 4

18020374. Miller TN, Sinha D, Baird TR, Walsh PN, A catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets. Biochemistry 46:50(14450-60)2007 Dec 18

17676929. Sinha D, Marcinkiewicz M, Navaneetham D, Walsh PN, Macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation. Biochemistry 46:34(9830-9)2007 Aug 28

16042419. Sinha D, Marcinkiewicz M, Lear JD, Walsh PN, Factor XIa dimer in the activation of factor IX. Biochemistry 44:30(10416-22)2005 Aug 2

15182201. Sinha D, Badellino KO, Marcinkiewicz M, Walsh PN, Allosteric modification of factor XIa functional activity upon binding to polyanions. Biochemistry 43:23(7593-600)2004 Jun 15

12084014. Sinha D, Marcinkiewicz M, Gailani D, Walsh PN, Molecular cloning and biochemical characterization of rabbit factor XI. Biochem J 367:Pt 1(49-56)2002 Oct 1

8660613. Sinha D, Bakhshi MR, Vora RK, Kirby EP, Budzynski AZ, Engineering DNA and protein chimeras utilizing coding sequences of restriction sites. Anal Biochem 238:2(205-8)1996 Jul 1

8713801. Bakhshi MR, Sinha D, Vora RK, Budzynski AZ, Kirby EP, Primary binding domain of bovine von Willebrand factor fragment expressed in E. coli. Thromb Haemost 75:1(196-202)1996 Jan

8093071. Sinha D, Bakhshi M, Kunapuli S, Vora R, Gabriel JL, Kirby EP, Budzynski AZ, ASP514 within the A1 domain of bovine von Willebrand factor is required for interaction with platelet glycoprotein Ib. Biochem Biophys Res Commun 203:2(881-8)1994 Sep 15

7818905. Sinha D, Bakhshi M, Vora R, Ligand binding assays with recombinant proteins refolded on an affinity matrix. Biotechniques 17:3(509-12, 514)1994 Sep

8056747. Sinha D, Yang X, Emig F, Kirby EP, Isolation and characterization of two protease inhibitors from bovine plasma. J Biochem 115:3(387-91)1994 Mar

8409210. Sinha D, Bakhshi MR, Yang X, Kirby EP, PCR to identify specific clones of interest for DNA sequencing. J Biochem Biophys Methods 27:1(49-55)1993 Aug

1562597. Sinha D, Bakhshi MR, Kirby EP, Complete cDNA sequence of bovine alpha 1-antitrypsin. Biochim Biophys Acta 1130:2(209-12)1992 Mar 24

1331709. Sinha D, Walsh PN, Binding of coagulation factor XIa to receptor on human platelets. Methods Enzymol 215:(361-9)1992

2665835. Baglia FA, Sinha D, Walsh PN, Functional domains in the heavy-chain region of factor XI: a high molecular weight kininogen-binding site and a substrate-binding site for factor IX. Blood 74:1(244-51)1989 Jul

3500185. Walsh PN, Sinha D, Kueppers F, Seaman FS, Blankstein KB, Regulation of factor XIa activity by platelets and alpha 1-protease inhibitor. J Clin Invest 80:6(1578-86)1987 Dec

3498513. Sinha D, Seaman FS, Walsh PN, Role of calcium ions and the heavy chain of factor XIa in the activation of human coagulation factor IX. Biochemistry 26:13(3768-75)1987 Jun 30

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