W. Church

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Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity

M. Ziman, D. I. Johnson, J. O'Brien, 1991, Molecular and cellular biology.

The humoral response to human factor VIII in hemophilia A mice

P. Lollar, E. Parker, W. Church, 2007, Journal of thrombosis and haemostasis : JTH.

Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.

K. Mann, R. Jernigan, R. Hewick, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Factor VII Antigen Levels in a Healthy Blood Donor Population

R. Tracy, E. Bovill, W. Church, 1994, Thrombosis and Haemostasis.

Vitamin K1 metabolism and the production of des-carboxy prothrombin and protein C in the term and premature neonate.

R. Soll, T. McAuliffe, E. Bovill, 1993, Blood.

A conserved epitope on several human vitamin K-dependent proteins. Location of the antigenic site and influence of metal ions on antibody binding.

K. Mann, J. Amiral, T. Messier, 1988, The Journal of biological chemistry.

Discrimination of normal and abnormal prothrombin and protein C in plasma using a calcium ion-inhibited monoclonal antibody to a common epitope on several vitamin K-dependent proteins.

K. Mann, E. Bovill, W. Church, 1989, Blood.

Association of human and bovine beta 2-microglobulins with detergent solubilized HLA-A,B antigens.

R. Reisfeld, W. Church, M. D. Poulik, 1982, Journal of immunological methods.

The fluorescein-mediated interaction of bovine serum albumin with fluorescent derivatives of prolactin and other polypeptides in polarization of fluorescence based assays.

W. Church, A. Rawitch, K. Ebner, 1981, Archives of biochemistry and biophysics.

A simple purification of human factor X using a high affinity monoclonal antibody immunoadsorbant.

K. Mann, W. Church, 1985, Thrombosis Research.

Anti-HLA antibodies of predetermined specificity: a chemically synthesized peptide induces antibodies specific for HLA-A,B heavy chain.

R. Houghten, R. Reisfeld, W. Church, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Inhibiting GPIb&agr; Shedding Preserves Post-Transfusion Recovery and Hemostatic Function of Platelets After Prolonged Storage

Renhao Li, J. Ware, C. Josephson, 2016, Arteriosclerosis, thrombosis, and vascular biology.

Purification of six human vitamin K-dependent proteins in a single chromatographic step using immunoaffinity columns.

K. Mann, W. Church, R. Litwiller, 1986, Preparative biochemistry.

Surface-dependent reactions of the vitamin K-dependent enzyme complexes

Kenneth G. Mann, Sriram Krishnaswamy, K. Mann, 1990 .

Surface-dependent reactions of the vitamin K-dependent enzyme complexes.

K. Mann, M. Nesheim, K G Mann, 1990, Blood.

The comparative immunogenicity of human and porcine factor VIII in haemophilia A mice

J. Healey, P. Lollar, E. Parker, 2009, Thrombosis and Haemostasis.

Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism.

K. Mann, M. Nesheim, W. Church, 1987, The Journal of biological chemistry.

Antithrombotic efficacy of a novel murine antihuman factor IX antibody in rats.

G. Feuerstein, A. Patel, P. Bugelski, 1999, Arteriosclerosis, thrombosis, and vascular biology.

A kringle-specific monoclonal antibody.

T. Messier, L. Ouellette, W. Church, 1994, Hybridoma.

Active site-specific immunoassays.

K. Mann, E. Williams, R. Tracy, 1990, Blood.

Domain-specific monoclonal antibodies to ovotransferrin indicate conservation of determinants involved in avian transferrin receptor recognition.

A. Mason, W. Church, S. Brown, 1988, Comparative biochemistry and physiology. B, Comparative biochemistry.

alpha-Thrombin-induced human platelet activation results solely from formation of a specific enzyme-substrate complex.

L. Leong, R. Henriksen, L. Ouellette, 1994, The Journal of biological chemistry.

"Thrombin" receptor-directed ligand accounts for activation by thrombin of platelet phospholipase C and accumulation of 3-phosphorylated phosphoinositides.

A. Sorisky, E. Simons, W. Church, 1991, The Journal of biological chemistry.

An inhibitory monoclonal antibody to factor X that blocks prothrombin activation but not prothrombinase enzyme assembly.

K. Mann, T. Messier, M. Tucker, 1988, Blood.

Inhibition of plasminogen activation by monoclonal antibodies to the kringle 5-B chain segment of human plasminogen.

T. Messier, W. Church, 1991, Hybridoma.

Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X.

T. Messier, G. Long, R. Kaufman, 1991, Gene.

Design of constructs for the expression of biologically active recombinant human factors X and Xa. Kinetic analysis of the expressed proteins.

C. Esmon, D. Wolf, T. Messier, 1991, The Journal of biological chemistry.

Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X

C. Y. Wong, T. Messier, G. Long, 1996, Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis.

Evidence for a common metal ion-dependent transition in the 4-carboxyglutamic acid domains of several vitamin K-dependent proteins.

K. Mann, T. Messier, W. Church, 1989, The Journal of biological chemistry.

Monoclonal antibodies to either domain of ovotransferrin block binding to transferrin receptors on chick reticulocytes.

A. Mason, W. Church, S. Brown, 1987, The Journal of biological chemistry.

Modulation of human prothrombin activation on phospholipid vesicles and platelets using monoclonal antibodies to prothrombin fragment 2.

T. Messier, L. Ouellette, W. Church, 1991, Journal of Biological Chemistry.

Immunochemical techniques for studying coagulation proteins.

T. Messier, L. Ouellette, W. Church, 1993, Methods in enzymology.

Solubilization of prolactin receptor by a Zwitterionic detergent

W. Church, K. Ebner, 1982, Experientia.

Monoclonal antibodies to the amino- and carboxyl-terminal domains of ovotransferrin.

A. Mason, W. Church, S. Brown, 1988, Hybridoma.