James A. Huntington spends much of his time researching Biochemistry, Serpin, Protease, Antithrombin and Conformational change. His work carried out in the field of Biochemistry brings together such families of science as Antibody, Thrombin and Cell biology. The various areas that James A. Huntington examines in his Serpin study include Peptide sequence and Stereochemistry.
Protease is often connected to Protein structure in his work. As a member of one scientific family, James A. Huntington mostly works in the field of Antithrombin, focusing on Proteases and, on occasion, Allosteric regulation. Conformational change is a subfield of Biophysics that James A. Huntington explores.
Biochemistry, Serpin, Thrombin, Antithrombin and Protein structure are his primary areas of study. His Biochemistry research is multidisciplinary, incorporating perspectives in alpha-2-Macroglobulin and Biophysics. His biological study spans a wide range of topics, including Proteases, Peptide sequence, Protein C inhibitor and Cell biology.
His research in Thrombin intersects with topics in Coagulation, Zymogen and Allosteric regulation. James A. Huntington interconnects Conformational change and Stereochemistry in the investigation of issues within Antithrombin. His study looks at the intersection of Protein structure and topics like Binding site with Plasma protein binding and Cofactor binding.
His primary scientific interests are in Biochemistry, Thrombin, Serpin, Protease and Prothrombinase. His Peptide sequence, Conformational change and Antithrombin deficiency study in the realm of Biochemistry interacts with subjects such as Frame. His Thrombin research integrates issues from Biophysics and Fibrin.
His study in Serpin focuses on Reactive center in particular. James A. Huntington has included themes like Antithrombin and Classical complement pathway in his Protease study. The study incorporates disciplines such as Genetics, Gene and Molecular biology in addition to Antithrombin.
His primary areas of study are Thrombin, Biochemistry, Protease, Serpin and Prothrombinase. The Thrombin study combines topics in areas such as Protein C, Coagulation and Fibrin. Many of his research projects under Biochemistry are closely connected to Porphyromonas gingivalis and Gingipain K with Porphyromonas gingivalis and Gingipain K, tying the diverse disciplines of science together.
His studies deal with areas such as Biophysics, Antithrombin and Cell biology as well as Protease. His work deals with themes such as Protein superfamily, Conformational change and Function, which intersect with Antithrombin. His work on Serpin is being expanded to include thematically relevant topics such as In vivo.
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Structure of a serpin–protease complex shows inhibition by deformation
James A. Huntington;Randy J. Read;Robin W. Carrell.
Serpins in thrombosis, hemostasis and fibrinolysis
J. C. Rau;L. M. Beaulieu;J. A. Huntington;Frank C. Church.
Journal of Thrombosis and Haemostasis (2007)
Structure of the antithrombin–thrombin–heparin ternary complex reveals the antithrombotic mechanism of heparin
Wei Li;Daniel J D Johnson;Charles T Esmon;James A Huntington.
Nature Structural & Molecular Biology (2004)
Structure and properties of ovalbumin.
James A. Huntington;Penelope E. Stein.
Journal of Chromatography B: Biomedical Sciences and Applications (2001)
How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration
Aiwu Zhou;James A Huntington;Navraj S Pannu;Navraj S Pannu;Robin W Carrell.
Nature Structural & Molecular Biology (2003)
Molecular recognition mechanisms of thrombin
J. A. Huntington.
Journal of Thrombosis and Haemostasis (2005)
Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
Masayuki Yamasaki;Wei Li;Daniel J. D. Johnson;James A. Huntington.
Serpin structure, function and dysfunction.
J. A. Huntington.
Journal of Thrombosis and Haemostasis (2011)
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)
Antithrombin–S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation
Daniel J D Johnson;Wei Li;Ty E Adams;James A Huntington.
The EMBO Journal (2006)
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