The molecular weights, mass distribution, chain composition, and structure of soluble fibrin degradation products released from a fibrin clot perfused with plasmin.
about
Staphylococcus aureus secretes coagulase and von Willebrand factor binding protein to modify the coagulation cascade and establish host infectionsA Dormant Microbial Component in the Development of PreeclampsiaTwo naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme.MRI evaluation of BBB disruption after adjuvant AcSDKP treatment of stroke with tPA in rat.Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation.The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies.Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sitesThrombin activatable fibrinolysis inhibitor activation and bleeding in haemophilia A.Solulin increases clot stability in whole blood from humans and dogs with hemophilia.Thrombin-thrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon.Point of care D-dimer testing in the emergency department: a bioequivalence studyFibrinogen decreases cardiomyocyte contractility through an ICAM-1-dependent mechanism.A CCR2 macrophage endocytic pathway mediates extravascular fibrin clearance in vivo.The plasmin-antiplasmin system: structural and functional aspects.Novel aspects of fibrin(ogen) fragments during inflammation.Biomarkers of endothelial dysfunction: can they help us deciphering systemic inflammation and sepsis?Basic mechanisms and regulation of fibrinolysis.The roles of selected arginine and lysine residues of TAFI (Pro-CPU) in its activation to TAFIa by the thrombin-thrombomodulin complexFurther evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages.A high affinity interaction of plasminogen with fibrin is not essential for efficient activation by tissue-type plasminogen activatorThrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis.Reduced plasminogen binding and delayed activation render γ'-fibrin more resistant to lysis than γA-fibrin.The use of prothrombin(S525C) labeled with fluorescein to directly study the inhibition of prothrombinase by antithrombin during prothrombin activation.Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process.Factor Xa is highly protected from antithrombin-fondaparinux and antithrombin-enoxaparin when incorporated into the prothrombinase complex.Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin.A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis.Proteolytic cleavage of carboxypeptidase N markedly increases its antifibrinolytic activity.A kinetic analysis of the tissue plasminogen activator and DSPAalpha1 cofactor activities of untreated and TAFIa-treated soluble fibrin degradation products of varying size.The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability.Measuring fibrinolysis: from research to routine diagnostic assays.Anti-tumor necrosis factor alpha therapy (adalimumab) in Rasmussen's encephalitis: An open pilot study.[Inventive activity of the Departments of Protein Structure and Function, and Molecular Immunology of the Palladin Institute of Biochemistry of NAS of Ukraine. Part II. National breakthrough in the study and diagnostics of human hemostasis system].
P2860
Q26858947-B7EB50B7-722D-4778-9E63-2438481D4A73Q28069689-65A12A87-5F6F-4EAE-B2FD-0144CA31968FQ30757818-110F409B-C1BA-4104-8C6D-5428B3BFC989Q33709032-6F5DB257-4933-4A4B-BCBD-408532C94A3DQ34109013-0C73A07C-920B-4111-A0E4-54F887ACCBECQ34542145-64E963EC-43BD-4AED-ADFE-2106AA062B65Q35010889-0DFCD9F4-C8EC-4519-8137-617F4FCB7B3DQ35788435-497BCEC5-4BEF-42E9-B557-4D4F43051FC0Q35885322-62548BCE-320C-4FB4-9DF8-CBE39BEED92DQ36384872-FC84A641-CC47-49D7-AA25-3EC09A9BE0D8Q36502678-019A643F-1003-4127-9152-FEA344C50898Q36642140-70431778-6982-4492-9B17-240370048497Q36651337-F44DDED0-B73F-4D8B-BB89-8C1E13AFC99DQ37817023-C35B3D6C-8EE3-4BA1-823A-DB59E83FA28DQ37826365-F4FBD894-77BD-443F-95DF-9FA44F626042Q37894728-9C27E240-15CB-40D1-8853-5C512D8B24EDQ38543323-C35953C3-D1F0-4012-B77F-2676034B232EQ39906372-355F521D-5C05-444D-B926-CB1B2CE49EA8Q40088315-0CE3B0A2-E926-4B98-A997-ED8DDC5DC09EQ41223914-5FB9F629-9A95-434A-A8E0-566BF4516D09Q41763565-04497DEA-F57D-4B2F-8830-081A50AC8FAAQ42137305-80C65344-0D87-40D9-8947-2B44F3D82C41Q43560091-67AEB947-1C8F-48DC-8597-F6330D38DFB7Q44258994-928D1EB8-922D-428B-874C-E121B4BB3E5CQ44518771-B1261D61-B771-4B60-8A52-FC429B8DFC8EQ44722857-2EB30AFC-0C78-4B9A-88E2-97164D2A8480Q44722862-748F098E-058B-4BBA-8DB1-F21A2EF7FCC5Q46790423-3C5B54EC-B0E3-4E9B-A187-DD43AE671BEEQ47225991-36B5D27C-73CC-4989-A39B-2EF113FE52A8Q47644869-2CA292AD-F2B9-402A-BD29-1867EE72A1D8Q47715508-5F23BBC3-89F6-4178-8DDA-1F6EAE328773Q48799486-85904930-3DE2-4D28-854E-1B9EF65ED2B9Q49863792-5F8B9654-963B-499F-8743-926AE7A73D58
P2860
The molecular weights, mass distribution, chain composition, and structure of soluble fibrin degradation products released from a fibrin clot perfused with plasmin.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The molecular weights, mass di ...... in clot perfused with plasmin.
@ast
The molecular weights, mass di ...... in clot perfused with plasmin.
@en
type
label
The molecular weights, mass di ...... in clot perfused with plasmin.
@ast
The molecular weights, mass di ...... in clot perfused with plasmin.
@en
prefLabel
The molecular weights, mass di ...... in clot perfused with plasmin.
@ast
The molecular weights, mass di ...... in clot perfused with plasmin.
@en
P2860
P356
P1476
The molecular weights, mass di ...... in clot perfused with plasmin.
@en
P2093
P2860
P304
P356
10.1074/JBC.274.8.5201
P407
P577
1999-02-01T00:00:00Z