J
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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Journal ArticleDOI
S-ovalbumin, an ovalbumin conformer with properties analogous to those of loop-inserted serpins
TL;DR: It is concluded that the limited native‐to‐S conformational change specifically affected the reactive center region of each protein to proteolysis by porcine pancreatic elastase and by subtilisin Carlsberg, and this alone is sufficient to account for the absence of detectable inhibitory properties in ovalbumin.
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Natural inhibitors of thrombin.
TL;DR: This review examines how the special features of thrombin have been exploited by evolution to achieve inhibition of the ultimate coagulation protease.
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Ligand Binding Shuttles Thrombin along a Continuum of Zymogen- and Proteinase-like States
TL;DR: Thrombin mutants, with deformed x-ray structures, previously considered to be emblematic of specific regulated states of the enzyme, are instead shown to be variously zymogen-like and can be made proteinase-like by active-site ligation.
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Whole-exome sequencing in evaluation of patients with venous thromboembolism
Eun-Ju Lee,Daniel J. Dykas,Andrew D. Leavitt,Rodney M. Camire,Eduard H T M Ebberink,Pablo García de Frutos,Kavitha Gnanasambandan,Sean X. Gu,James A. Huntington,Steven R. Lentz,Koen Mertens,Christopher R. Parish,Alireza R. Rezaie,Peter P. Sayeski,Caroline Cromwell,Noffar Bar,Stephanie Halene,Natalia Neparidze,Terri L. Parker,Adrienne J Burns,Anne Dumont,Xiaopan Yao,Cassius Iyad Ochoa Chaar,Jean M. Connors,Allen E. Bale,Alfred Ian Lee +25 more
TL;DR: In this paper, the authors performed whole-exome sequencing (WES) in 64 patients with venous thromboembolism (VTE), focusing their analysis on a novel 55-gene extended thrombophilia panel that they compiled.
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Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation
TL;DR: A striking feature of the structure is a two-turn N-terminal shortening of helix A, which creates a large hydrophobic pocket that docking studies indicate to be the retinoid binding site, and a novel mechanism for heparin activation is proposed.