PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7666362-0 1995 Thrombin-induced inhibition of potassium currents in human retinal glial (Muller) cells. Potassium 31-40 coagulation factor II, thrombin Homo sapiens 0-8 9511103-5 1998 The thrombin-fibrinogen dissociation constant Ks served as the single adjustable parameter in a least-squares fitting of the model to experimental anticoagulation data. Potassium 46-48 coagulation factor II, thrombin Homo sapiens 4-12 15650548-6 2005 When 0.4 IU/ml thrombin was used in samples provided by 10 healthy individuals treated with acetysalicylic acid, Ks levels were increased during versus before therapy. Potassium 113-115 coagulation factor II, thrombin Homo sapiens 15-23 10440258-0 1999 Thrombin inhibits active sodium-potassium transport in porcine lens. Potassium 32-41 coagulation factor II, thrombin Homo sapiens 0-8 10440258-2 1999 In the present study, experiments were conducted to determine the influence of thrombin on active sodium-potassium transport in porcine lenses. Potassium 105-114 coagulation factor II, thrombin Homo sapiens 79-87 10440258-5 1999 RESULTS: In the presence of thrombin (1 unit/ml) the rate of ouabain-sensitive potassium (86Rb) uptake was reduced by 40% to 60%, but ouabain-insensitive potassium (86Rb) uptake was unchanged. Potassium 79-88 coagulation factor II, thrombin Homo sapiens 28-36 10440258-5 1999 RESULTS: In the presence of thrombin (1 unit/ml) the rate of ouabain-sensitive potassium (86Rb) uptake was reduced by 40% to 60%, but ouabain-insensitive potassium (86Rb) uptake was unchanged. Potassium 154-163 coagulation factor II, thrombin Homo sapiens 28-36 10440258-6 1999 The inhibitory effect of thrombin on ouabain-sensitive potassium (86Rb) uptake was suppressed in the presence of hirudin (an antagonist for thrombin receptors) but persisted in the presence of amphotericin B (a pseudo ionophore that effectively clamps plasma membrane sodium permeability at a high value). Potassium 55-64 coagulation factor II, thrombin Homo sapiens 25-33 10440258-6 1999 The inhibitory effect of thrombin on ouabain-sensitive potassium (86Rb) uptake was suppressed in the presence of hirudin (an antagonist for thrombin receptors) but persisted in the presence of amphotericin B (a pseudo ionophore that effectively clamps plasma membrane sodium permeability at a high value). Potassium 55-64 coagulation factor II, thrombin Homo sapiens 140-148 10440258-13 1999 The functional significance of the thrombin-mediated change of lens active sodium-potassium transport is unclear since appreciable amounts of thrombin may only be presented to the lens during instances of blood-aqueous-barrier breakdown. Potassium 82-91 coagulation factor II, thrombin Homo sapiens 35-43 7642616-4 1995 In contrast, aptamers selected against R70E thrombin were able to bind and inhibit both wild-type and R70E thrombins, and displayed potassium-independent inhibition. Potassium 132-141 coagulation factor II, thrombin Homo sapiens 44-52 8373370-5 1993 In addition, the values of Km for thrombin-fibrinogen reaction were measured at different solution viscosities in order to derive the equilibrium dissociation constant, Ks, of this interaction. Potassium 169-171 coagulation factor II, thrombin Homo sapiens 34-42 8373370-6 1993 These experiments showed that the Ks values for thrombin-fibrinogen binding was equal to 1.8 microM at 25 degrees C. Altogether these results indicated that fibrinogen, though interacting with both the catalytic pocket and the fibrinogen recognition site on the thrombin molecule, dissociates from Michaelis complex with a rate comparable with that shown by amide substrates, which interact only with the catalytic site. Potassium 34-36 coagulation factor II, thrombin Homo sapiens 48-56 8373370-6 1993 These experiments showed that the Ks values for thrombin-fibrinogen binding was equal to 1.8 microM at 25 degrees C. Altogether these results indicated that fibrinogen, though interacting with both the catalytic pocket and the fibrinogen recognition site on the thrombin molecule, dissociates from Michaelis complex with a rate comparable with that shown by amide substrates, which interact only with the catalytic site. Potassium 34-36 coagulation factor II, thrombin Homo sapiens 262-270 34001444-4 2021 RESULTS: Endometriosis was associated with increased thrombin generation, reflected by both higher F1+2 (+96.1%, P = 0.005) and ETP (+14.2%, P = 0.014) along with unfavourably altered fibrin clot properties represented by lower Ks (-31%, P < 0.001) and prolonged CLT (+13.5%, P = 0.02), compared with the non-endometriosis group. Potassium 228-230 coagulation factor II, thrombin Homo sapiens 53-61 2752057-8 1989 Permeation analysis showed that gel porosity (measured as Ks) decreased in gels formed at higher fibrin and thrombin concentrations in agreement with the porosity observed by microscopy. Potassium 58-60 coagulation factor II, thrombin Homo sapiens 108-116 6693420-5 1984 It is thus apparent that: 1) the change in the membrane potential induced by thrombin is directly dependent upon the transmembrane sodium gradient and is primarily due to a dose-dependent sodium uptake by the platelets; and 2) the thrombin-induced secretory processes are dependent upon maintenance of the transmembrane potassium gradients. Potassium 320-329 coagulation factor II, thrombin Homo sapiens 77-85 6693420-5 1984 It is thus apparent that: 1) the change in the membrane potential induced by thrombin is directly dependent upon the transmembrane sodium gradient and is primarily due to a dose-dependent sodium uptake by the platelets; and 2) the thrombin-induced secretory processes are dependent upon maintenance of the transmembrane potassium gradients. Potassium 320-329 coagulation factor II, thrombin Homo sapiens 231-239 32810596-7 2020 Ks correlated inversely with FIX and FV, thrombin-activatable fibrinolysis inhibitor, complement C1s, C7, C8, and apolipoprotein A-I. Potassium 0-2 coagulation factor II, thrombin Homo sapiens 41-49 26540111-7 2015 Multivariate analysis adjusted for fibrinogen showed that Ks was predicted by eosinophil count, peak thrombin generation, factor VIII, and soluble CD40 ligand, whereas eosinophil count, peak thrombin generation and antiplasmin predicted t50%. Potassium 58-60 coagulation factor II, thrombin Homo sapiens 101-109 28849814-5 2017 In this work, we employ microsecond-scale all-atom molecular dynamics simulations to investigate the differences in the structural ensembles in sodium-bound/unbound and potassium-bound/unbound thrombin. Potassium 169-178 coagulation factor II, thrombin Homo sapiens 193-201 28849814-10 2017 Our study of thrombin in the presence of sodium/potassium ions suggests Na+-mediated generalized allostery is the mechanism of thrombin"s functional switch between the "fast" and "slow" forms. Potassium 48-57 coagulation factor II, thrombin Homo sapiens 13-21 28849814-10 2017 Our study of thrombin in the presence of sodium/potassium ions suggests Na+-mediated generalized allostery is the mechanism of thrombin"s functional switch between the "fast" and "slow" forms. Potassium 48-57 coagulation factor II, thrombin Homo sapiens 127-135 28771277-4 2017 At baseline, the prothrombin mutation group formed denser clots (Ks -12 %, p=0.0006) and had impaired fibrinolysis (CLT +14 %, p=0.004, and CLT-TAFI +13 %, p=0.03) compared with the no mutation group and were similar to those observed in 15 healthy unrelated prothrombin mutation carriers. Potassium 65-67 coagulation factor II, thrombin Homo sapiens 17-28 25714986-1 2015 The repair ligation-mediated light-producing DNA machine can produce light through transforming the repetitive DNA cleavage/ligation motions into optical energy without the requirement of either external reporting reagents or excitation light, and it can be applied for sensitive and selective detection of DNA, thrombin, adenosine, potassium ions (K(+)) and endonuclease even in human serum. Potassium 333-342 coagulation factor II, thrombin Homo sapiens 312-320 25352996-4 2014 Here, we report the rational design of structure-switching DNA aptamers, based on the thrombin binding aptamer (TBA), that bind potassium with affinities that bridge the gap between previously reported weak-binding and strong-binding aptamers. Potassium 128-137 coagulation factor II, thrombin Homo sapiens 86-94 24738991-8 2014 Multivariate analysis adjusted for age and fibrinogen showed that in MM patients elevated peak thrombin levels determine Ks and D-Dmax , while thrombin-activatable fibrinolysis inhibitor (TAFI) activity predicts Ks , t50% , D-Drate and lag phase. Potassium 121-123 coagulation factor II, thrombin Homo sapiens 95-103 22475983-0 2012 Fluorescence imaging of potassium ions in living cells using a fluorescent probe based on a thrombin binding aptamer-peptide conjugate. Potassium 24-33 coagulation factor II, thrombin Homo sapiens 92-100 21396765-5 2011 Both FF and FH aptamer dimers exhibited a potassium-dependent inhibitory effect on thrombin-mediated fibrin gel formation, which was on average two-fold higher than those of canonical single stranded Fibri aptamers. Potassium 42-51 coagulation factor II, thrombin Homo sapiens 83-91