F
Frank C. Church
Researcher at University of North Carolina at Chapel Hill
Publications - 138
Citations - 8308
Frank C. Church is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Thrombin & Heparin cofactor II. The author has an hindex of 44, co-authored 137 publications receiving 7743 citations. Previous affiliations of Frank C. Church include North Carolina State University & University of Western Ontario.
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Spectrophotometric Assay Using o-Phthaldialdehyde for Determination of Proteolysis in Milk and Isolated Milk Proteins
TL;DR: The o-phthaldialdehyde Spectrophotometric (OPS) as discussed by the authors was developed and characterized for measurement of proteolysis of milk proteins in buffered solutions or in milk.
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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,Paul Bernard Coughlin,Peter G.W. Gettins,James A. Irving,David A. Lomas,Cliff J. Luke,Richard W. Moyer,Philip A. Pemberton,Eileen Remold-O'Donnell,Guy S. Salvesen,James Travis,James C. Whisstock +14 more
TL;DR: This work aims to provide a systematic literature review and meta-analyses of the determinants of blood clotting disorders and their Kessler’s disease progression as well as some of the mechanisms behind these reactions.
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Serpins in thrombosis, hemostasis and fibrinolysis
TL;DR: This review describes key serpins important in the regulation of these pathways: antithrombin, heparin cofactor II, protein Z‐dependent protease inhibitors, α1‐protease inhibitor, protein C inhibitor, α2‐antiplasmin and plasminogen activator inhibitor‐1.
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Antithrombin activity of fucoidan. The interaction of fucoidan with heparin cofactor II, antithrombin III, and thrombin.
TL;DR: The results indicate that heparin cofactor II is activated by fucoidan in vitro and in an ex vivo plasma system and suggest that the major antithrombin activity of fucoidin in vivo is mediated by hepar in co Factor II and not by antithromabin III.
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Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
TL;DR: The native structure of HCII resembles that of native antithrombin and suggests an alternative mechanism of allosteric activation, whereas the structure of the S195A thrombin–HCII complex defines the molecular basis of allostery.