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James A. Huntington

Researcher at University of Cambridge

Publications -  119
Citations -  8495

James A. Huntington is an academic researcher from University of Cambridge. The author has contributed to research in topics: Serpin & Thrombin. The author has an hindex of 50, co-authored 114 publications receiving 7920 citations. Previous affiliations of James A. Huntington include Wellcome Trust & University of Illinois at Chicago.

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Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin.

TL;DR: It is concluded that neither arginine 132 nor lysine 133 plays an important role in the binding of heparin pentasaccharide or in the mechanism of heParin activation, suggesting that D-helix extension through charge neutralization is not the mechanism for transmission of conformational change from the heparIn binding site to the reactive center region.
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Heparin-induced substrate behavior of antithrombin Cambridge II

TL;DR: The high occurrence of this mutation and its possible propagation from a few founders suggests an evolutionary advantage, perhaps in decreasing postpartum bleeding.
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Immunologic and structural analysis of eight novel domain-deletion beta3 integrin peptides designed for detection of HPA-1 antibodies.

TL;DR: Soluble recombinant β3 peptides can be used for detection of clinical HPA‐1a antibodies, and testing of FMAIT samples indicated that ΔβA‐Leu33 is the superior peptide for HPA-1a antibody detection, with 96% sensitivity and 95% specificity.
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GpIbα interacts exclusively with exosite II of thrombin.

TL;DR: The results indicate that the peptide corresponding to the C-terminal portion of GpIbα and the entire extracellular domain bind exclusively to thrombin's exosite II, which serves to recruitThrombin activity to the platelet surface while leaving exosite I free for PAR-1 recognition.
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SERPINC1 gene mutations in antithrombin deficiency

TL;DR: Several novel SERPINC1 mutations are reported, thereby adding to the knowledge of the molecular background of antithrombin deficiency, and the results point out the importance of future research outside the conventional SERPinc1 gene approach.