Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement

Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement

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http://www.wikidata.org/entity/Q28274243

Q28274243

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Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells The anticoagulant activation of antithrombin by heparin New anticoagulants for the prevention and treatment of venous thromboembolism Engineering the substrate and inhibitor specificities of human coagulation Factor VIIa Structural and Functional Characterization of a Highly Specific Serpin in the Insect Innate Immunity Computationally derived points of fragility of a human cascade are consistent with current therapeutic strategies Anticoagulants and the propagation phase of thrombin generation Interaction of heparin with internally quenched fluorogenic peptides derived from heparin-binding consensus sequences, kallistatin and anti-thrombin III Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function.Designing nonsaccharide, allosteric activators of antithrombin for accelerated inhibition of factor Xa.Probing the impact of GFP tagging on Robo1-heparin interaction.Chemical Sulfation of Small Molecules - Advances and Challenges.Probing the coagulation pathway with aptamers identifies combinations that synergistically inhibit blood clot formation.Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor: both active site and exosite interactions are required for inhibition.Anticoagulation by factor Xa inhibitors.Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).Hormonal contraception and thrombotic risk: a multidisciplinary approach.Sulodexide: a renewed interest in this glycosaminoglycan.Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Heparin is a major activator of the anticoagulant serpin, protein Z-dependent protease inhibitor.Mechanisms of glycosaminoglycan activation of the serpins in hemostasis.Molecular mapping of the heparin-binding exosite of thrombin.Heparin modulates the 99-loop of factor IXa: effects on reactivity with isolated Kunitz-type inhibitor domains.Anti-thrombin is expressed in the benign prostatic epithelium and in prostate cancer and is capable of forming complexes with prostate-specific antigen and human glandular kallikrein 2.Heparin-binding domains in vascular biology.Specificity and selectivity profile of EP217609: a new neutralizable dual-action anticoagulant that targets thrombin and factor Xa Pentosan polysulfate increases affinity between ADAMTS-5 and TIMP-3 through formation of an electrostatically driven trimolecular complex.Initial experience with recombinant antithrombin to treat antithrombin deficiency in patients on extracorporeal membrane oxygenation Heparin reduces neuroinflammation and transsynaptic neuronal apoptosis in a model of subarachnoid hemorrhage.Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin-induced conformers of antithrombin Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States Clinical review: molecular mechanisms underlying the role of antithrombin in sepsis.The High Affinity Binding Site on Plasminogen Activator Inhibitor-1 (PAI-1) for the Low Density Lipoprotein Receptor-related Protein (LRP1) Is Composed of Four Basic Residues.Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases.Pentasaccharide enhances the inactivation of factor Xa by antithrombin by promoting the assembly of a Michaelis-type intermediate complex. Demonstration by rapid kinetic, surface plasmon resonance, and competitive binding studies.The design and synthesis of new synthetic low-molecular-weight heparins.Prevention and treatment of venous thromboembolism in the elderly patient Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor Antithrombin concentrate use in children: a multicenter cohort study.Pathophysiology, management and treatment of smoke inhalation injury.

P2860

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P2860

Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement

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http://www.wikidata.org/entity/Q28274243

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1992 nî lūn-bûn

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1992 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1992 թվականի հունիսին հրատարակված գիտական հոդված

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1992年の論文

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年學術文章

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