Helix D elongation and allosteric activation of antithrombin.
about
The influence of hinge region residue Glu-381 on antithrombin allostery and metastabilityCorticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered releaseHeparin binds lamprey angiotensinogen and promotes thrombin inhibition through a template mechanismIncreased N-glycosylation efficiency by generation of an aromatic sequon on N135 of antithrombinThe critical role of hinge-region expulsion in the induced-fit heparin binding mechanism of antithrombin.Inhibitory properties of the P1 Tyr variant of antithrombin.Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor: both active site and exosite interactions are required for inhibition.Expression and Characterization of Gly-317 Variants of Factor IX Causing Variable Bleeding in Hemophilia B Patients.Characterization of the heparin-binding site of the protein z-dependent protease inhibitorSchistosome serine protease inhibitors: parasite defense or homeostasis?Mutagenesis studies toward understanding the intracellular signaling mechanism of antithrombin.The 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.Limitations of conventional anticoagulant therapy and the promises of non-heparin based conformational activators of antithrombin.Effects of glycosylation on heparin binding and antithrombin activation by heparin.Kinetic evidence that allosteric activation of antithrombin by heparin is mediated by two sequential conformational changes.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Activation 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.Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation.Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site.Expression and functional characterization of two natural heparin-binding site variants of antithrombin.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
Helix D elongation and allosteric activation of antithrombin.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
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2001年學術文章
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2001年學術文章
@zh-hant
name
Helix D elongation and allosteric activation of antithrombin.
@en
Helix D elongation and allosteric activation of antithrombin.
@nl
type
label
Helix D elongation and allosteric activation of antithrombin.
@en
Helix D elongation and allosteric activation of antithrombin.
@nl
prefLabel
Helix D elongation and allosteric activation of antithrombin.
@en
Helix D elongation and allosteric activation of antithrombin.
@nl
P2093
P2860
P356
P1476
Helix D elongation and allosteric activation of antithrombin
@en
P2093
James A Huntington
Klara J Belzar
Peter G W Gettins
Robin W Carrell
P2860
P304
P356
10.1074/JBC.M110807200
P407
P50
P577
2001-12-10T00:00:00Z