Representative Publications (updated January 2008):

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Beaulieu, L.M., M.W. Gramling, and F.C. Church. Activated protein C has both intracellular and extracellular effects on breast cancer and endothelial cells.  Exp. Cell Res. Submitted for publication.

Henry, A.T., G.Q. Daley, M. Cargill, E.S. Lander, A.R. Rezaie and F.C. Church.  Effect of single nucleotide polymorphisms in protein C inhibitor on protease inhibition and heparin binding.  Manuscript in preparation for submission.

Mitchell, J.W., A.C. Schaap, J.C. Rau and F.C. Church.  Interdependence of the heparin cofactor II reactive center Leu444 for its acidic domain during thrombin inhibition.  Manuscript in preparation for submission.

Beaulieu, L.M., B.R. Whitley, T.F. Wiesner, D. Palmieri, S.M. Rehault, A. Elkahloun, and F.C. Church (2007) Breast cancer and metabolic syndrome linked through the plasminogen activator inhibitor-1 cycle. BioEssays. Oct;29(10):1029-38.

Rau, J.C., L.M. Beaulieu, J.A. Huntington, and F.C. Church (2007) Serpins in thrombosis, hemostasis and fibrinolysis. J. Thromb. Haemost. Jul;5 Suppl 1:102-15.

Gonzales, P.R., T.D. Walston, L.O. Camacho, D.M. Kielar, F.C. Church, A.R. Rezaie, and S.T. Cooper (2007) Mutation of the H-helix in antithrombin decreases heparin stimulation of protease inhibition. Biochim Biophys Acta, Nov;1774(11):1431-7.

Fortenberry, Y.M., H.C. Whinna, S.T. Cooper, T. Myles, L.L.K. Leung, and F.C. Church (2007) Essential thrombin residues for inhibition by protein C inhibitor with the cofactors heparin and thrombomodulin.  J. Thromb. Haemost. 5(7):1486-92.

Beaulieu, L.M. and F.C. Church (2007) Activated protein C promotes breast cancer cell migration through interactions with EPCR and PAR-1. Exp. Cell Res. Feb 15;313(4):677-87.

Whitley, B.R., L.M. Beaulieu, J.C. Carter, and F.C. Church (2007) Phosphatidylinositol 3-kinase/Akt regulates the balance between plasminogen activator inhibitor-1 and urokinase to promote migration of SKOV-3 ovarian cancer cells.  Gynecol. Oncol. Feb;104(2):470-9.

Church, F.C., R.N. Pike, D.M. Tollefsen, A.M. Buckle, A.V. Ciaccia, and S.T. Olson (2007) Regulation of hemostasis by heparin-binding Serpins. In “Molecular and cellular aspects of the serpinopathies and disorders of serpin activity”, World Scientific Publishing Co.  Chapter 22, 509-554.
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Beaulieu, L.M. and F.C. Church (2006) Is protein C inhibitor antithrombotic and protective in pulmonary hypertension?  J. Thromb. Haemost. 4: 2327-2330.

Pike, R.N., Buckle, A.M., le Bonniec, B.F., and F.C. Church (2005) Control of the coagulation system by serpins: getting by with a little help from glycosaminoglycans. FEBS J. 272(19):4842-51.

Glasscock, L.N., S.M. Rehault, C.W. Gregory, Cooper, S.T., Jackson, T.P., Hoffman, M., and F.C. Church (2005) Protein C inhibitor (Plasminogen Activator Inhibitor-3) expression in the CWR22 prostate cancer xenograft. Exp. Molec. Pathol. 79:23-32.

Whitley, B.R. and F.C. Church (2005) Regulation of wound-induced migration of MDA-MB-435 and SKOV-3 cancer cells by plasminogen activator inhibitor-1. Int J Oncol. 27(3):749-57.

Réhault, S.M., Zechmeister-Machhart, M.,, Binz, N.M., Fortenberry, Y.M., Cooper, S.T., Geiger, M., and F.C. Church (2005).  Characterization of recombinant human protein C inhibitor expressed in Escherichia coli. Biochimica Biophysica Acta. 1748: 57-65.

Hobson, J.P., S. Netzel-Arnett, R. Szabo, S.M. Réhault, F.C. Church, D.K. Strickland, D.A. Lawrence, T.M. Antalis, and T.H. Bugge (2004)  Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes.  J. Biol. Chem. 279(45): 46981-94.

Fortenberry, Y.M., H.C. Whinna, H.R. Gentry, T. Myles, L.L.K. Leung, and F.C. Church (2004) Molecular mapping of the thrombin-heparin cofactor II complex.  J. Biol. Chem. 279(41):43237-44.

Whinna, H.C., E.B. Lesesky, D.M. Monroe, K.A. High, P.J. Larson, and F.C. Church (2004)  Role of the g-carboxyglutamic acid domain of factor Xa in heparin-catalyzed inhibition by antithrombin.  J Thromb Haemost. 2: 1127-1134.

Jeter, M.L, L.V. Ly, Y.M. Fortenberry, , H.C. Whinna, R.R. White, C.P. Rusconi, B.A. Sullenger, and F.C. Church (2004) RNA aptamer to thrombin protects thrombin in inhibition by heparin-binding serpins.  FEBS Letts. 568: 10-14.

Whitley, B.R., Palmieri, D., Twerdi, C.D., and F.C. Church (2004) Expression of active plasminogen activator inhibitor-1 reduces cell migration and invasion in breast and gynecological cancer cells.  Exp Cell Res. 2004 Jun: 296(2):151-62.

Patston, P.A., F.C. Church, and S.T. Olson (2004) Serpin-ligand interactions. Methods. Feb.: 32(2):93-109.  

Hoffman, M., K.L.M. Loh, V.K. Bond, D. Palmieri and F.C. Church (2003) Localization of heparin cofactor II in injured human skin: A potential role in wound healing. Exp. Molec. Pathol. 75: 109-118.

Glasscock, L.N., B. Gerlitz, S.T. Cooper, B.W. Grinnell, and F.C. Church (2003) Basic residues in the 37-loop of activated protein C modulate inhibition by protein C inhibitor but not by alpha1-antitrypsin Biochimica Biophysica Acta. 1649:106-117.

Palmieri, D., J.-W. Lee, R.L. Juliano and F.C. Church (2002) Plasminogen activator inhibitor-1 and -3 increase cell adhesion and motility of MDA-MB-435 breast cancer cells. J. Biol. Chem. 277: 40950-40957.

Baglin, T., R.W. Carrell, F.C. Church, C.T. Esmon and J.A. Huntington (2002) Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc Natl Acad Sci U S A. 99: 11079-11084.

Mitchell, J.W. and F.C. Church (2002) Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.  J. Biol. Chem. 277(22):19823-19830.  

Wu, H.-F. and F.C. Church (2003) Arginine 25 and arginine 28 of lactoferrin are critical for effective heparin neutralization in blood.  Arch. Biochem. Biophys.  412:121-125.

Oliver, J.A., D.M. Monroe, F.C. Church, H.R. Roberts, and M. Hoffman (2002) Activated protein C cleaves factor Va more efficiently on endothelium than on platelet surfaces.  Blood. 100:539-546.
Cooper, S.T., A.R. Rezaie, C.T. Esmon, and F.C. Church (2002) Inhibition of a thrombin anion-binding exosite-2 mutant by the glycosaminoglycan-dependent serpins protein C inhibitor and heparin cofactor II. Thromb. Res. 107: 67-73.

Silverman, G.A., Bird, P.I., Carrell, R.W., Church, F.C., Coughlin, P.B., Gettins, P.G., Irving, J.A., Lomas, D.A., Luke, C.J., Moyer, R.W., Pemberton, P.A., Remold-O'Donnell, E., Salvesen, G.S., Travis. J., Whisstock., J.C. (2001)  The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature.  J. Biol. Chem. 276(36):33293-33296.

Bauman, S.J., H.C. Whinna and F.C. Church (2001) Serpins (Serine Protease Inhibitors) In “Current Protocols in Protein Science”.  Unit 21.10.1-7.

Holland, C.A., A.T. Henry, H.C. Whinna and F.C. Church (2000) Effect of oligodeoxynucleotide thrombin aptamer on thrombin inhibition by heparin cofactor II and antithrombin.  FEBS Letts. 484: 87-91.

Bushman, J.E., D. Palmieri, H.C. Whinna, and F.C. Church (2000) Insight into the mechanism of asparaginase-induced depletion of antithrombin III in treatment of childhood acute lymphoblastic leukemia.  Leukemia Res. 27 (7): 559-565.

Shirk, R.A., N. Parthasarathy, J.D. San Antonio, F.C. Church, and W.D. Wagner (2000) Altered dermatan sulfate structure and reduced heparin cofactor II activity of biglycan and decorin from human atherosclerotic plaque.  J. Biol. Chem. 275: 18085-18092. 

Bauman, S.J. and F.C. Church (1999) Enhancement of heparin cofactor II anticoagulant activity.  J. Biol. Chem.  274: 34556-334565.  

Bauman, S.J. and F. C. Church (1999) Heparin cofactor II.  In "Laboratory Assays in Thrombosis- A Manual", (J. Jespersen, R.M. Bertina, and F. Havertake, Eds.), Kluwer Academic Publ. , Chpt. 20, pp. 189-196.

Myles, T. , F.C. Church, H.C. Whinna, D. Monard, and S.R. Stone (1998) Role of thrombin anion-binding exosite-I in the formation of thrombin-serpin complexes.  J. Biol. Chem. 273: 31203-31208. 

Elisen, M.G.L.M., B.N. Bouma, F.C. Church, and J.C.M. Meijers (1998) Inhibition of serine proteases by reactive site mutants of protein C inhibitor. Fibrinol. Proteol. 12: 283-291.

Neese, L.L., C.A. Wolfe, and F.C. Church (1998) Contribution of basic residues of the D and H helices in heparin binding to protein C inhibitor. Arch. Biochem. Biophys. 355: 101-108.

Cooper, S.T. and F.C. Church (1997) PCI: Protein C Inhibitor?  In "Chemistry and Biology of Serpins" . (Church, F.C., Editor, and D.D. Cunningham, D. Ginsburg, M. Hoffman, D.M. Tollefsen, and S.R. Stone, Assoc. Eds.)  Plenum Press, New York.   pp. 45-54.

Ciaccia, A.V., D.M. Monroe, and F.C. Church (1997) Arginine 200 of heparin cofactor II promotes intramolecular interactions of the acidic domain: Implications for thrombin inhibition.  J. Biol. Chem. 272: 14074-14079. 
 
Jackson, T.P., S.T. Cooper and F.C. Church (1997) Assessment of the interaction between urokinase and reactive site mutants of protein C inhibitor.  J. Protein Chem. 16: 819-828.

Ciaccia, A. V., Willemze, A.J., and Church, F. C. (1997) Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II.  J. Biol. Chem. 272: 888-893. 

Kounnase, M.Z., F.C. Church, W.S. Argraves and D.K. Strickland (1996) Cellular internalization and degradation of antithrombin III:thrombin, heparin cofactor II:thrombin, and a 1-antitrypsin: trypsin complexes is mediated by the low density lipoprotein receptor-related protein.  J. Biol. Chem. 271: 6523-6529. 

Cooper, S.T., L.L. Neese, M.N. DiCuccio, D.K. Liles, M. Hoffman and F.C. Church (1996)  Vascular localization of the heparin-binding serpins antithrombin, heparin cofactor II and protein C inhibitor.  Clin. Appl. Thromb./Hemost.  2: 185-191.

Elisen, M.G.L.M., M.H.H. Maseland, F.C. Church, B.N. Bouma and J.C.M. Meijers (1996) Role of the A+ helix in heparin binding to protein C inhibitor.  Thromb. Haemost.  75: 760-766 .

Shirk, R.A, F. C. Church and W.D. Wagner (1996) Arterial smooth muscle cell heparan sulfate proteoglycans accelerate thrombin inhibition by heparin cofactor II.  Arterioscl. Thromb. Vasc. Biol. 16: 1138-1146 .

Cooper, S.T., H.C. Whinna, T.P. Jackson, J.M. Boyd and F.C. Church (1995) Intermolecular interactions between protein C inhibitor and coagulation proteases.  Biochemistry 34: 12991-12997 .

Rezaie, A.R., S.T. Cooper, F.C. Church and C.T. Esmon (1995) Protein C inhibitor is a potent inhibitor of the thrombin-thrombomodulin complex.  J. Biol. Chem.  270: 25336-25339.  

Ciaccia, A.V., E.L. Cunningham and F.C. Church (1995) Characterization of recombinant heparin cofactor II expressed in insect cells.  Prot. Express. Purif. 6: 806-812.

Crago, A.M., H.-F. Wu, M. Hoffman and F.C. Church (1995) Monocyte chemoattractant activity of Ser 195 to Ala active site mutant recombinant a -thrombin.  Exp. Cell. Res. 219: 650-656 .

Wu, H.-F., R.L. Lundblad, and F.C. Church (1995) Neutralization of heparin by neutrophil lactoferrin. Blood 85: 421-428 .

Cooper, S.T. and F.C. Church (1995) Reactive site mutants of recombinant protein C inhibitor. Biochim. Biophys. Acta.  1246: 29-33 .

Melton, L.G., F.C. Church and B.W. Erickson (1995) Designed polyanionic coiled-coil proteins: Acceleration of heparin cofactor II inhibition of thrombin.  Int. J. Prot. Pept. Res.  45: 44-52 .

Wu, H.-F., Monroe, D.M., and F.C. Church (1995)  Characterization of the glycosaminoglycan-binding region in lactoferrin.  Arch. Biochem. Biophys. 317: 85-92 .

Slate, C.A., S.C. Weninger, F.C. Church and B.W. Erickson (1995) Engineering of five 88-residue receptor-adhesive modular proteins containing a parallel a-helical coiled coil and two RGD ligand sites.  Int. J. Prot. Pept. Res.  45: 290-298 .

Shirk, R.A, Elisen, M.G.L.M., Meijers, J.C.M. and F.C. Church (1994) Role of the H helix in heparin binding to protein C inhibitor.  J. Biol. Chem. 269: 28690-28695 .

Phillips, J.E., S.T. Cooper, E.E. Potter and F.C. Church (1994) Mutagenesis of recombinant protein C inhibitor reactive site residues alters target proteinase specificity.  J. Biol. Chem. 269: 16696-16700 .