Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex - Wikidata - awgldk - TriplyDB

Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

http://www.wikidata.org/entity/Q27622194

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Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors Thrombin inhibition by the serpins Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1 Crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4 Structural identification of the pathway of long-range communication in an allosteric enzyme Isolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle Tick Molecular basis of thrombomodulin activation of slow thrombin Crystal Structure of Thrombin Bound to the Uncleaved Extracellular Fragment of PAR1 Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junction Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector Exposure of R169 controls protein C activation and autoactivation GpIbα Interacts Exclusively with Exosite II of Thrombin Exosite-driven substrate specificity and function in coagulation The normal role of Activated Protein C in maintaining homeostasis and its relevance to critical illness Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.Molecular recognition mechanisms of thrombin.Placental thrombomodulin expression in recurrent miscarriage.Regulation of the protein C anticoagulant and antiinflammatory pathways.NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation.Acquired antithrombin deficiency in sepsis.Modeling zymogen protein C.Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin.Activation of protein C by the thrombin-thrombomodulin complex: cooperative roles of Arg-35 of thrombin and Arg-67 of protein C Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities.Allosteric inhibition of the neuropeptidase neurolysin.Thrombomodulin Binding Selects the Catalytically Active Form of Thrombin Thrombomodulin as an intravascular safeguard against inflammatory and thrombotic diseases.Why Ser and not Thr brokers catalysis in the trypsin fold Thrombomodulin.Molecular recognition in the protein C anticoagulant pathway.Receptors of the protein C activation and activated protein C signaling pathways are colocalized in lipid rafts of endothelial cells.The Importance of Exosite Interactions for Substrate Cleavage by Human Thrombin.End-point immobilization of recombinant thrombomodulin via sortase-mediated ligation.Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.

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P2860

Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

http://www.wikidata.org/entity/Q27622194

description

2000 nî lūn-bûn

@nan

2000 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մարտին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex

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D R Light

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G Rumennik

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J Morser

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M Seto

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P Fuentes-Prior

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R Huber

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R Pagila

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W Bode

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Y Iwanaga

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P2860

Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin

The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin

Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin

Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders

Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug

Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern

New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK

The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action

The CCP4 suite: programs for protein crystallography

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518-25

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4278617

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10.1038/35006683

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404

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10761923

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anticoagulation