Functional mapping of the surface residues of human thrombin.
about
Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexesA novel method of screening thrombin-inhibiting DNA aptamers using an evolution-mimicking algorithm.Mechanism of the Anticoagulant Activity of Thrombin Mutant W215A/E217ACrystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4Molecular basis of thrombomodulin activation of slow thrombinCrystal Structure of Thrombin Bound to the Uncleaved Extracellular Fragment of PAR1Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin FoldStructural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junctionThrombin-aptamer recognition: a revealed ambiguityUnique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vectorStructure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bugMolecular mapping of the thrombin-heparin cofactor II complexAptamers as a sensitive tool to detect subtle modifications in therapeutic proteinsRole of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.Molecular recognition mechanisms of thrombin.Thrombin hydrolysis of human osteopontin is dependent on thrombin anion-binding exosites.Thrombin mutant W215A/E217A treatment improves neurological outcome and reduces cerebral infarct size in a mouse model of ischemic stroke.Engineering thrombin for selective specificity toward protein C and PAR1.Identification and characterization of novel salivary thrombin inhibitors from the ixodidae tick, Haemaphysalis longicornis.Switching cation-binding loops paves the way for redesigning allosteric activationA guided mode resonance aptasensor for thrombin detection.The Importance of Exosite Interactions for Substrate Cleavage by Human Thrombin.Relative antithrombotic and antihemostatic effects of protein C activator versus low-molecular-weight heparin in primates.Determinants of specificity in coagulation proteases.Thrombomodulin allosterically modulates the activity of the anticoagulant thrombin.The role of thrombin exosites I and II in the activation of human coagulation factor V.Role of Na+ and K+ in enzyme function.Selection of a suppressor mutation that restores affinity of an oligonucleotide inhibitor for thrombin using in vitro genetics.Thrombin.Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants.Crystal structure of the complex between thrombin and the central "E" region of fibrin.Exosites in the substrate specificity of blood coagulation reactions.Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa.Human Norovirus Aptamer Exhibits High Degree of Target Conformation-Dependent Binding Similar to That of Receptors and Discriminates Particle FunctionalityStructural basis of thrombin-protease-activated receptor interactions.Stability and binding properties of a modified thrombin binding aptamer.Towards maintenance-free biosensors for hundreds of bind/release cycles.HD1, a thrombin-directed aptamer, binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase.Thrombin a-chain: activation remnant or allosteric effector?Transition step during assembly of HIV Tat:P-TEFb transcription complexes and transfer to TAR RNA.
P2860
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P2860
Functional mapping of the surface residues of human thrombin.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Functional mapping of the surface residues of human thrombin.
@en
Functional mapping of the surface residues of human thrombin.
@nl
type
label
Functional mapping of the surface residues of human thrombin.
@en
Functional mapping of the surface residues of human thrombin.
@nl
prefLabel
Functional mapping of the surface residues of human thrombin.
@en
Functional mapping of the surface residues of human thrombin.
@nl
P2093
P2860
P356
P1476
Functional mapping of the surface residues of human thrombin.
@en
P2093
P2860
P304
16854-16863
P356
10.1074/JBC.270.28.16854
P407
P577
1995-07-01T00:00:00Z