D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Biology and Biochemistry D-index 57 Citations 10,024 120 World Ranking 9491 National Ranking 723

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Biochemistry

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.

His most cited work include:

  • Structure of a serpin–protease complex shows inhibition by deformation (920 citations)
  • Structure of the antithrombin–thrombin–heparin ternary complex reveals the antithrombotic mechanism of heparin (289 citations)
  • Serpins in thrombosis, hemostasis and fibrinolysis (243 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Biochemistry (49.15%)
  • Serpin (40.68%)
  • Thrombin (38.14%)

What were the highlights of his more recent work (between 2010-2021)?

  • Biochemistry (49.15%)
  • Thrombin (38.14%)
  • Serpin (40.68%)

In recent papers he was focusing on the following fields of study:

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.

Between 2010 and 2021, his most popular works were:

  • Serpin structure, function and dysfunction. (195 citations)
  • Molecular basis of α1‐antitrypsin deficiency revealed by the structure of a domain‐swapped trimer (117 citations)
  • Design and characterization of an APC-specific serpin for the treatment of hemophilia (74 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Gene
  • Amino acid

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.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Structure of a serpin–protease complex shows inhibition by deformation

James A. Huntington;Randy J. Read;Robin W. Carrell.
Nature (2000)

1300 Citations

Serpins in thrombosis, hemostasis and fibrinolysis

J. C. Rau;L. M. Beaulieu;J. A. Huntington;Frank C. Church.
Journal of Thrombosis and Haemostasis (2007)

407 Citations

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)

404 Citations

Structure and properties of ovalbumin.

James A. Huntington;Penelope E. Stein.
Journal of Chromatography B: Biomedical Sciences and Applications (2001)

374 Citations

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)

319 Citations

Molecular recognition mechanisms of thrombin

J. A. Huntington.
Journal of Thrombosis and Haemostasis (2005)

279 Citations

Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization

Masayuki Yamasaki;Wei Li;Daniel J. D. Johnson;James A. Huntington.
Nature (2008)

274 Citations

Serpin structure, function and dysfunction.

J. A. Huntington.
Journal of Thrombosis and Haemostasis (2011)

248 Citations

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)

241 Citations

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)

203 Citations

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