Critical role of the linker region between helix D and strand 2A in heparin activation of antithrombin.
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Structure of native protein C inhibitor provides insight into its multiple functionsHeparin binds lamprey angiotensinogen and promotes thrombin inhibition through a template mechanismGlycosaminoglycan-binding properties and kinetic characterization of human heparin cofactor II expressed in Escherichia coliSucrose octasulfate selectively accelerates thrombin inactivation by heparin cofactor IISaturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated StatesThe allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.Probing serpin conformational change using mass spectrometry and related methods.Limitations of conventional anticoagulant therapy and the promises of non-heparin based conformational activators of antithrombin.Synthetic heparin pentasaccharide depolymerization by heparinase I: molecular and biological implications.Effects of glycosylation on heparin binding and antithrombin activation by heparin.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.The heparin-binding site of antithrombin is crucial for antiangiogenic activityActivation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement.Antiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence.Helix D elongation and allosteric activation of antithrombin.The heparin binding properties of heparin cofactor II suggest an antithrombin-like activation mechanism.Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site.Inhibitory activity of the Drosophila melanogaster serpin Necrotic is dependent on lysine residues in the D-helix.Engineering D-helix of antithrombin in alpha-1-proteinase inhibitor confers antiinflammatory properties on the chimeric serpin.
P2860
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P2860
Critical role of the linker region between helix D and strand 2A in heparin activation of antithrombin.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Critical role of the linker re ...... in activation of antithrombin.
@en
type
label
Critical role of the linker re ...... in activation of antithrombin.
@en
prefLabel
Critical role of the linker re ...... in activation of antithrombin.
@en
P2093
P2860
P356
P1476
Critical role of the linker re ...... in activation of antithrombin.
@en
P2093
P2860
P304
P356
10.1074/JBC.275.4.2698
P407
P577
2000-01-01T00:00:00Z