about
Crystal structure of an RNA aptamer bound to thrombinWhat we should know about portal vein thrombosis in cirrhotic patients: a changing perspectiveStructural basis of Na+ activation mimicry in murine thrombinCrystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4Structural identification of the pathway of long-range communication in an allosteric enzymeExosite-driven substrate specificity and function in coagulationTargeting recombinant thrombomodulin fusion protein to red blood cells provides multifaceted thromboprophylaxis.Identification and characterization of human archaemetzincin-1 and -2, two novel members of a family of metalloproteases widely distributed in Archaea.Biophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.Redesigning the monovalent cation specificity of an enzymeFibrinopeptides A and B release in the process of surface fibrin formation.Promotion of experimental thrombus formation by the procoagulant activity of breast cancer cells.Blood coagulation and its regulation by anticoagulant pathways: genetic pathogenesis of bleeding and thrombotic diseases.Emerging role of direct thrombin inhibitors in nonvalvular atrial fibrillation: potential and peril.P3-P3' residues flanking scissile bonds in factor VIII modulate rates of substrate cleavage and procofactor activation by thrombinThe anticoagulant protein C pathway.Meizothrombin is an unexpectedly zymogen-like variant of thrombin.Determinants of specificity in coagulation proteases.Thrombin.Detection of protein biomarkers using RNA aptamer microarrays and enzymatically amplified surface plasmon resonance imagingLooking at the proteases from a simple perspective.Viral cirrhosis: an overview of haemostatic alterations and clinical consequencesDesign of Potent and Controllable Anticoagulants Using DNA Aptamers and Nanostructures.HD1, a thrombin-directed aptamer, binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase.PDBSiteScan: a program for searching for active, binding and posttranslational modification sites in the 3D structures of proteins.Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics.Effect of Na+ binding on the conformation, stability and molecular recognition properties of thrombin.Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin.Active site-independent recognition of substrates and product by bovine prothrombinase: a fluorescence resonance energy transfer study.Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C.Crystal structure of thrombin bound to heparin.Thrombin functions through its RGD sequence in a non-canonical conformation.Non-Coded amino acids in protein engineering: structure-activity-relationship studies of hirudin-thrombin interaction.Molecular dissection of Na+ binding to thrombin.Phospholipid composition controls thromboplastin sensitivity to individual clotting factors.Effect of dalteparin administration on thrombin generation kinetics in healthy dogs.
P2860
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P2860
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Thrombin interactions.
@ast
Thrombin interactions.
@en
type
label
Thrombin interactions.
@ast
Thrombin interactions.
@en
prefLabel
Thrombin interactions.
@ast
Thrombin interactions.
@en
P1433
P1476
Thrombin interactions.
@en
P2093
Enrico Di Cera
P304
P356
10.1378/CHEST.124.3_SUPPL.11S
P407
P433
P577
2003-09-01T00:00:00Z