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Query author contributions in Reactome

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Details on Person Olson, ST

Class:IdPerson:211153
_displayNameOlson, ST
_timestamp2008-01-28 22:58:55
created[InstanceEdit:211152] D'Eustachio, P, 2008-01-28 22:58:31
firstnameSteven T
initialST
modified[InstanceEdit:211180] D'Eustachio, P, 2008-01-28 22:59:10
surnameOlson
(author)[LiteratureReference:211151] Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms. Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding
[LiteratureReference:9823303] Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease
[LiteratureReference:9823476] Mechanism by which exosites promote the inhibition of blood coagulation proteases by heparin-activated antithrombin
[LiteratureReference:9920992] The heparin-binding site of antithrombin is crucial for antiangiogenic activity
[LiteratureReference:9932946] Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa
[LiteratureReference:9932962] Kinetic characterization of the protein Z-dependent protease inhibitor reaction with blood coagulation factor Xa
[LiteratureReference:9932963] Thermodynamic and kinetic characterization of the protein Z-dependent protease inhibitor (ZPI)-protein Z interaction reveals an unexpected role for ZPI Lys-239
[LiteratureReference:9932973] Structural basis for catalytic activation of protein Z-dependent protease inhibitor (ZPI) by protein Z
[LiteratureReference:9932974] Heparin activation of protein Z-dependent protease inhibitor (ZPI) allosterically blocks protein Z activation through an extended heparin-binding site
[LiteratureReference:9935173] Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors
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No pathways have been reviewed or authored by Olson, ST (211153)