Frank C. Church mostly deals with Biochemistry, Thrombin, Antithrombin, Heparin cofactor II and Heparin. His study in Biochemistry is interdisciplinary in nature, drawing from both Molecular biology, Chromatography and Protein C inhibitor. Frank C. Church studies Thrombin, focusing on Thrombomodulin in particular.
The concepts of his Antithrombin study are interwoven with issues in Serine Proteinase Inhibitors and Immunology. His Heparin cofactor II research incorporates themes from Dermatan sulfate, Protease and Cell biology. His work is dedicated to discovering how Heparin, Cofactor are connected with Peptide and other disciplines.
His main research concerns Biochemistry, Thrombin, Heparin cofactor II, Molecular biology and Serpin. His research investigates the connection between Biochemistry and topics such as Protein C inhibitor that intersect with problems in Protein C. His research in Thrombin intersects with topics in Glycosaminoglycan, Stereochemistry, Coagulation and Active site.
His Heparin cofactor II research focuses on Dermatan sulfate and how it connects with Proteoglycan. His studies in Molecular biology integrate themes in fields like Plasminogen activator, Plasminogen activator inhibitor-1, Proteolysis, Chymotrypsin and Protease-activated receptor. His Heparin research includes themes of Cofactor and Pharmacology.
His primary areas of study are Plasminogen activator, Cancer research, Thrombin, Plasminogen activator inhibitor-1 and Internal medicine. His work deals with themes such as Cell, Cell type, Molecular biology, Receptor and Motility, which intersect with Plasminogen activator. His Cancer research research integrates issues from Fibrinolysis, Plasmin, Urokinase and Tissue factor.
Frank C. Church is interested in Heparin cofactor II, which is a branch of Thrombin. His work in Internal medicine tackles topics such as Endocrinology which are related to areas like Peroxisome proliferator-activated receptor, Breast cancer, Cancer and Protease-Activated Receptor 1. As a member of one scientific family, Frank C. Church mostly works in the field of Protease, focusing on Proteases and, on occasion, Heparan sulfate.
Internal medicine, Plasminogen activator inhibitor-1, Plasminogen activator, Endocrinology and Fibrinolysis are his primary areas of study. The concepts of his Plasminogen activator inhibitor-1 study are interwoven with issues in Cell signaling, Tissue factor, Molecular biology and Protease-activated receptor, Thrombin. His work in Plasminogen activator is not limited to one particular discipline; it also encompasses Angiogenesis.
His research integrates issues of Cancer, Breast cancer and Protease-Activated Receptor 1 in his study of Endocrinology. The study incorporates disciplines such as Thrombosis, Cancer research and Cardiology in addition to Fibrinolysis. His Cancer research research is multidisciplinary, incorporating elements of Urokinase receptor, Urokinase, Immunology, Tissue plasminogen activator and Vitronectin.
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The serpins are an expanding superfamily of structurally similar but functionally diverse proteins - Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
Gary A. Silverman;Phillip I. Bird;Robin W. Carrell;Frank C. Church.
Journal of Biological Chemistry (2001)
Serpins in thrombosis, hemostasis and fibrinolysis
J. C. Rau;L. M. Beaulieu;J. A. Huntington;Frank C. Church.
Journal of Thrombosis and Haemostasis (2007)
Antithrombin activity of fucoidan. The interaction of fucoidan with heparin cofactor II, antithrombin III, and thrombin.
F C Church;J B Meade;R E Treanor;H C Whinna.
Journal of Biological Chemistry (1989)
Protein C Inhibitor Is a Potent Inhibitor of the Thrombin-Thrombomodulin Complex
Alireza R. Rezaie;Scott T. Cooper;Frank C. Church;Charles T. Esmon;Charles T. Esmon;Charles T. Esmon.
Journal of Biological Chemistry (1995)
Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
Trevor P. Baglin;Robin W. Carrell;Frank C. Church;Charles T. Esmon.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Cellular Internalization and Degradation of Antithrombin III-Thrombin, Heparin Cofactor II-Thrombin, and α1-Antitrypsin-Trypsin Complexes Is Mediated by the Low Density Lipoprotein Receptor-related Protein
Maria Z. Kounnas;Frank C. Church;W. Scott Argraves;Dudley K. Strickland.
Journal of Biological Chemistry (1996)
An o-phthalaldehyde spectrophotometric assay for proteinases☆
Frank C. Church;David H. Porter;George L. Catignani;Harold E. Swaisgood.
Analytical Biochemistry (1985)
Reactive site peptide structural similarity between heparin cofactor II and antithrombin III.
M J Griffith;C M Noyes;F C Church.
Journal of Biological Chemistry (1985)
Tumor-derived tissue factor activates coagulation and enhances thrombosis in a mouse xenograft model of human pancreatic cancer.
Jian Guo Wang;Julia E. Geddings;Maria M. Aleman;Jessica C. Cardenas.
Blood (2012)
Effect of oligodeoxynucleotide thrombin aptamer on thrombin inhibition by heparin cofactor II and antithrombin
Carrie A Holland;Alexis T Henry;Herbert C Whinna;Frank C Church.
FEBS Letters (2000)
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