about
Nucleic Acid Aptamers: An Emerging Tool for Biotechnology and Biomedical SensingMechanism of the Anticoagulant Activity of Thrombin Mutant W215A/E217ANa+ binding to meizothrombin desF1Stabilization of the E* Form Turns Thrombin into an AnticoagulantMolecular basis of thrombomodulin activation of slow thrombinMutant N143P Reveals How Na+ Activates ThrombinCrystal Structure of Thrombin Bound to the Uncleaved Extracellular Fragment of PAR1Crystal structure of prethrombin-1Rigidification of the autolysis loop enhances Na+ binding to thrombinCrystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseInteraction of Thrombin with Sucrose OctasulfateCrystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationExposure of R169 controls protein C activation and autoactivationLoop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in ThrombinDynamics Govern Specificity of a Protein-Protein Interface: Substrate Recognition by ThrombinDesigning Allosteric Regulators of Thrombin. Exosite 2 Features Multiple Subsites That Can Be Targeted by Sulfated Small Molecules for Inducing InhibitionCorrelated motions and residual frustration in thrombin.Proton bridging in the interactions of thrombin with hirudin and its mimics.Glycosaminoglycan-binding properties and kinetic characterization of human heparin cofactor II expressed in Escherichia coliSucrose octasulfate selectively accelerates thrombin inactivation by heparin cofactor IIEngineering thrombin for selective specificity toward protein C and PAR1.Severe bleeding in a woman heterozygous for the fibrinogen gammaR275C mutation.NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.Ligand binding shuttles thrombin along a continuum of zymogen- and proteinase-like states.Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities.Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).On scaffold hopping: challenges in the discovery of sulfated small molecules as mimetics of glycosaminoglycans.Thrombomodulin Binding Selects the Catalytically Active Form of ThrombinEvidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.Redesigning allosteric activation in an enzyme.Switching cation-binding loops paves the way for redesigning allosteric activationUpdate on the Serum Biomarkers and Genetic Factors Associated with Safety and Efficacy of rt-PA Treatment in Acute Stroke Patients.Why Ser and not Thr brokers catalysis in the trypsin foldAntithrombin nanoparticles improve kidney reperfusion and protect kidney function after ischemia-reperfusion injury.Allostery in trypsin-like proteases suggests new therapeutic strategies.Aptamer-functionalized nano-biosensors.Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.Allosteric Inhibition of Factor XIIIa. Non-Saccharide Glycosaminoglycan Mimetics, but Not Glycosaminoglycans, Exhibit Promising Inhibition Profile.Designing allosteric regulators of thrombin. Monosulfated benzofuran dimers selectively interact with Arg173 of exosite 2 to induce inhibition.Highly selective and rapidly activatable fluorogenic Thrombin sensors and application in human lung tissue.
P2860
Q26825644-E9D73D3E-D1C8-47D9-ABCB-8F1A86C0BDB5Q27646504-024C2925-08DE-4FB0-A609-092948CDD2C4Q27652506-B7DB025E-1854-47A3-855D-3E7DFFC4A027Q27655637-57E5838B-0EFE-4022-9F22-ADAB851F8E66Q27656902-AAF6CCF9-2C9D-4D0F-BFD6-284C1CA746A4Q27657884-664C4593-20A0-46F1-9420-D8717647A269Q27660263-A773122A-DD46-49AB-A346-EB3A1D1A4966Q27665368-BA0FEBDC-BDEF-4D48-9461-AB6AA4472B1FQ27667649-FC1FE416-E18C-4DD3-B679-75E410D8C993Q27670579-73E8B18C-1A1B-4821-A388-CDE3F971186CQ27670722-B86E25EE-2B11-458B-83EA-F8FAC6F98953Q27675359-05A72D10-468C-44C8-AA8A-3542E14BA94BQ27678741-0225F11C-0422-42BF-AC28-43DA9C0590B6Q27714094-604D3D0F-BD18-48CD-80E0-DE5050CC4200Q28550480-B99A1D4D-815A-4FC7-A023-BA3ED6C0734DQ29040782-CBA0D483-7DE3-47A8-8F40-25958E39A391Q30155107-B8D753FD-78CC-47E7-B298-BF419350F023Q30604793-B680EDF6-0D37-4BB0-B1DA-7E179864B1EEQ33645142-799577BC-82FC-4490-A28B-E8A399E928A0Q33707130-5EF58D9C-3FCB-4133-B753-4B110AAA46B4Q33911257-9F9B4CE1-81A7-4DC1-AF7B-48F3B456512FQ33959050-AF17FECA-6C52-444E-9FEE-A090E9329F67Q34069668-FF626D98-6F64-420D-B510-CD7E3F370A2BQ34121251-0B84C7F3-ADE1-4160-9A7A-C3A0369B9C39Q34314615-15808010-2A30-4259-A642-FE4876FC16B3Q34457491-EDB82885-AC15-49A2-8FFE-98730F7A5E7FQ34481378-AB442708-5C4F-4330-B7F6-1A03DFA85DC8Q34498065-C6F8DE5E-D141-44BB-81F3-305929AF5279Q34630229-8BDAC267-5B85-49B3-ABE8-2323811F78FEQ34750145-3C197787-EBF7-4AB9-A5C3-8A54DF260BF4Q34750443-1B9C8529-71A4-46F1-8945-C6B22DFB1EB6Q35109940-30829C8B-ADA9-4C43-B860-E0F656FF13C6Q35127936-CB51F8FD-C3E5-4C98-89C6-8982556E9500Q35274033-AC2E6C12-B0FB-4492-90D8-6F98844BE509Q35317139-615B8F22-A69A-4980-BA7C-79EDCF45DE1FQ35701619-7D3FD8A0-2D4C-46CA-816F-8A1110D533ACQ36049897-E5FA74BB-F71C-4BA8-BDAA-AE173EBDC3CFQ36088633-549DBE94-47AF-4DC3-8C85-7D2508729509Q36157083-80CAD194-376C-4652-A99E-D459BC91884FQ36363953-DD112B18-615D-4640-8B16-3DDB70308C69
P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Thrombin.
@ast
Thrombin.
@en
type
label
Thrombin.
@ast
Thrombin.
@en
prefLabel
Thrombin.
@ast
Thrombin.
@en
P2860
P1476
Thrombin.
@en
P2093
Enrico Di Cera
P2860
P304
P356
10.1016/J.MAM.2008.01.001
P577
2008-02-01T00:00:00Z