PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30724273-1 2019 The monovalent sodium ion (Na+) is a critical modulator of thrombin. Sodium 15-21 coagulation factor II, thrombin Homo sapiens 59-67 28849814-2 2017 Depending upon the binding of sodium ions, thrombin presents significantly different enzymatic activities. Sodium 30-36 coagulation factor II, thrombin Homo sapiens 43-51 28961453-1 2017 INTRODUCTION: Antithrombin resistance (ATR) prothrombinemia is an inherited thrombophilic disorder caused by missense mutations in prothrombin gene (F2) at Arg596 of the sodium-binding region. Sodium 170-176 coagulation factor II, thrombin Homo sapiens 44-55 28961453-11 2017 CONCLUSIONS: Mutation of prothrombin at the sodium-binding site caused ATR-phenotypes. Sodium 44-50 coagulation factor II, thrombin Homo sapiens 25-36 29573721-0 2018 Novel heparin mimetics reveal cooperativity between exosite 2 and sodium-binding site of thrombin. Sodium 66-72 coagulation factor II, thrombin Homo sapiens 89-97 29573721-8 2018 Label-free surface plasmon resonance was used to assess the role of sodium ion in LMWL binding to thrombin at a fixed ionic strength. Sodium 68-74 coagulation factor II, thrombin Homo sapiens 98-106 29573721-11 2018 Interestingly, LMWLs display preference for the sodium-bound form of thrombin, which supports the existence of an energetic coupling between exosite 2 and sodium-binding site of thrombin. Sodium 48-54 coagulation factor II, thrombin Homo sapiens 69-77 29573721-11 2018 Interestingly, LMWLs display preference for the sodium-bound form of thrombin, which supports the existence of an energetic coupling between exosite 2 and sodium-binding site of thrombin. Sodium 48-54 coagulation factor II, thrombin Homo sapiens 178-186 29573721-11 2018 Interestingly, LMWLs display preference for the sodium-bound form of thrombin, which supports the existence of an energetic coupling between exosite 2 and sodium-binding site of thrombin. Sodium 155-161 coagulation factor II, thrombin Homo sapiens 69-77 29573721-11 2018 Interestingly, LMWLs display preference for the sodium-bound form of thrombin, which supports the existence of an energetic coupling between exosite 2 and sodium-binding site of thrombin. Sodium 155-161 coagulation factor II, thrombin Homo sapiens 178-186 28849814-3 2017 In the environment with sodium ions, thrombin is highly active in cleaving the coagulated substrates and this is referred to as the "fast" form; in the environment without sodium ions, thrombin turns catalytically less active and is in the "slow" form. Sodium 24-30 coagulation factor II, thrombin Homo sapiens 37-45 28849814-3 2017 In the environment with sodium ions, thrombin is highly active in cleaving the coagulated substrates and this is referred to as the "fast" form; in the environment without sodium ions, thrombin turns catalytically less active and is in the "slow" form. Sodium 24-30 coagulation factor II, thrombin Homo sapiens 185-193 28849814-3 2017 In the environment with sodium ions, thrombin is highly active in cleaving the coagulated substrates and this is referred to as the "fast" form; in the environment without sodium ions, thrombin turns catalytically less active and is in the "slow" form. Sodium 172-178 coagulation factor II, thrombin Homo sapiens 37-45 28849814-3 2017 In the environment with sodium ions, thrombin is highly active in cleaving the coagulated substrates and this is referred to as the "fast" form; in the environment without sodium ions, thrombin turns catalytically less active and is in the "slow" form. Sodium 172-178 coagulation factor II, thrombin Homo sapiens 185-193 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. Sodium 41-47 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. Sodium 41-47 coagulation factor II, thrombin Homo sapiens 127-135 16732371-1 2006 Sodium plays an important role in modulating both the amidolytic and proteolytic activities of thrombin. Sodium 0-6 coagulation factor II, thrombin Homo sapiens 95-103 20535627-0 2010 Regulation of renal sodium handling through the interaction between serine proteases and serine protease inhibitors. Sodium 20-26 coagulation factor II, thrombin Homo sapiens 68-83 20535627-9 2010 These findings strongly suggest the possibility that coordinated regulation of serine protease, serpin, and ENaC expression plays a key role in sodium handling in the kidney. Sodium 144-150 coagulation factor II, thrombin Homo sapiens 79-94 17430903-0 2007 Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation. Sodium 45-51 coagulation factor II, thrombin Homo sapiens 86-94 17430903-0 2007 Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation. Sodium 45-51 coagulation factor II, thrombin Homo sapiens 102-113 18030731-0 2007 [Sodium ions as the effector of catalytic action of alpha-thrombin]. Sodium 1-7 coagulation factor II, thrombin Homo sapiens 58-66 18326052-0 2008 Protease-activated receptor-1 mediates thrombin-induced persistent sodium current in human cardiomyocytes. Sodium 67-73 coagulation factor II, thrombin Homo sapiens 39-47 18326052-2 2008 The role of PAR1 was investigated in the thrombin effect on sodium current (I(Na)). Sodium 60-66 coagulation factor II, thrombin Homo sapiens 41-49 18326052-5 2008 Thrombin-activated PAR1 induced a tetrodotoxin-blocked persistent sodium current, I(NaP), in a concentration-dependent manner with an apparent EC(50) of 28 U/ml. Sodium 66-72 coagulation factor II, thrombin Homo sapiens 0-8 18326052-8 2008 Thrombin, through PAR1 activation, increases persistent component of the Na(+) current resulting in an uncontrolled sodium influx into the cardiomyocyte, which can contribute to cellular injuries observed during cardiac ischemia. Sodium 116-122 coagulation factor II, thrombin Homo sapiens 0-8 17635698-3 2007 RESULTS: Residues around the active site (Tyr50 and Glu202) and the sodium-binding site (Glu229 and Arg233) were required for thrombin inhibition by PCI with and without cofactors. Sodium 68-74 coagulation factor II, thrombin Homo sapiens 126-134 16673263-5 2006 It cleaves fibrinogen, factors XI (FXI) and FXIII, cofactors V and VIII, and the thrombin receptors; uses thrombomodulin to activate protein C and thrombin-activatable-fibrinolysis inhibitor; is inhibited by heparin cofactor II and antithrombin III with the help of acidic carbohydrates; and its activity/specificity is modulated by sodium ions. Sodium 333-339 coagulation factor II, thrombin Homo sapiens 81-89 16673263-5 2006 It cleaves fibrinogen, factors XI (FXI) and FXIII, cofactors V and VIII, and the thrombin receptors; uses thrombomodulin to activate protein C and thrombin-activatable-fibrinolysis inhibitor; is inhibited by heparin cofactor II and antithrombin III with the help of acidic carbohydrates; and its activity/specificity is modulated by sodium ions. Sodium 333-339 coagulation factor II, thrombin Homo sapiens 147-155 1999477-2 1991 PMA or thrombin caused a cytoplasmic alkalinization that required extracellular sodium and was sensitive to 1 mM amiloride, suggesting that the rise in pH was mediated by the Na+/H+ exchanger. Sodium 80-86 coagulation factor II, thrombin Homo sapiens 7-15 16487178-4 2006 Amino acid 552 has been reported to be involved in the allosteric transition, which is induced by sodium binding to thrombin. Sodium 98-104 coagulation factor II, thrombin Homo sapiens 116-124 16288954-4 2006 We have characterized the structure, topography and lipophilicity of this channel in the ligand-free fast (sodium-bound) and slow (sodium-free) forms of thrombin, in the sole available structure of activated protein C and in several structures of the coagulation factors VIIa, IXa and Xa, differing in the nature of the bound inhibitor and in the occupancy of exosite-I as well as the Ca2+ and Na+ binding sites. Sodium 131-137 coagulation factor II, thrombin Homo sapiens 153-161 16288954-7 2006 We also disclosed major topographical changes on the thrombin"s surface upon sodium release and transition to the slow form that culminate in the narrowing of the S1 subsite entrance and, strikingly, in the loss of communication between the primary specificity pocket and the exosite-I. Sodium 77-83 coagulation factor II, thrombin Homo sapiens 53-61 15850610-11 2005 The increase of the decline in pHi elicited by preexposure to thrombin was still observed in the presence of an inhibitor of the Na+/H+ exchange or in sodium-free solutions. Sodium 151-157 coagulation factor II, thrombin Homo sapiens 62-70 12379580-0 2002 Thrombin facilitation of voltage-gated sodium channel activation in human cardiomyocytes: implications for ischemic sodium loading. Sodium 39-45 coagulation factor II, thrombin Homo sapiens 0-8 12379580-10 2002 CONCLUSIONS: Facilitation of VGSC activation causing large increases in window current is a major mechanism by which thrombin may promote ischemic sodium loading and injury. Sodium 147-153 coagulation factor II, thrombin Homo sapiens 117-125 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). Sodium 268-274 coagulation factor II, thrombin Homo sapiens 25-33 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. Sodium 75-81 coagulation factor II, thrombin Homo sapiens 35-43 8703074-2 1996 By means of mutant substrates, it was shown that LY254603 mediates the change in enzymatic substrate specificity through an alteration in thrombin"s S3 substrate recognition site, a mechanism that appeared to be independent of allosteric changes induced by either sodium ions or by thrombomodulin. Sodium 264-270 coagulation factor II, thrombin Homo sapiens 138-146 8613987-4 1996 The enthalpic contribution to the free energy of sodium binding is equal to -27 kcal/mol and -21 kcal/mol in the TM-free and TM-bound thrombin forms, respectively. Sodium 49-55 coagulation factor II, thrombin Homo sapiens 134-142 8613987-5 1996 Finally, the entropy change for sodium binding was also affected by TM, being equal to -83 cal/(mol deg) and -58 cal/(mol deg) in TM-free and TM-bound thrombin species, respectively. Sodium 32-38 coagulation factor II, thrombin Homo sapiens 151-159 8613987-10 1996 Therefore, the effect of sodium binding to thrombin on the hydrolysis of human Protein C was extensively investigated. Sodium 25-31 coagulation factor II, thrombin Homo sapiens 43-51 12679012-0 2003 Mechanism of thrombin"s enigmatic sodium switch revealed. Sodium 34-40 coagulation factor II, thrombin Homo sapiens 13-21 11891217-4 2002 When choline was substituted for sodium to transform thrombin to its slow form, the maximal levels of alpha-profibrin rose to those expected for independent release of the two FPA. Sodium 33-39 coagulation factor II, thrombin Homo sapiens 53-61 11676542-10 2001 For thrombin, smaller negative DeltaC(p) values are observed for ligand binding in the presence of sodium ions compared to the other alkali ions, probably due to stabilising effects on the protein or changes in the bound water structure. Sodium 99-105 coagulation factor II, thrombin Homo sapiens 4-12 11321677-3 2001 We pointed out the crucial role of the insertion loop 186a-d and the I16-D194 ion pair in the stabilization of sodium binding pocket in thrombin. Sodium 111-117 coagulation factor II, thrombin Homo sapiens 136-144 11043938-5 2000 This observation could be due to a simple ionic interaction between Asp189 and the sodium ion or a more complicated structural rearrangement of the thrombin S1 pocket. Sodium 83-89 coagulation factor II, thrombin Homo sapiens 148-156 10440258-0 1999 Thrombin inhibits active sodium-potassium transport in porcine lens. Sodium 25-31 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. Sodium 98-104 coagulation factor II, thrombin Homo sapiens 79-87 10091588-3 1999 Under low sodium concentration (5 mM Na+) the BPTI affinity for alpha-thrombin was roughly threefold lower than in the presence of 150 mM sodium (Ki = 320 microM vs. 100 microM). Sodium 10-16 coagulation factor II, thrombin Homo sapiens 70-78 9368669-4 1997 The procoagulant and anticoagulant functions of thrombin can be modulated by sodium binding, site-directed mutagenesis, and a small synthetic molecule. Sodium 77-83 coagulation factor II, thrombin Homo sapiens 48-56 8613987-0 1996 Effect of sodium on the energetics of thrombin-thrombomodulin interaction and its relevance for protein C hydrolysis. Sodium 10-16 coagulation factor II, thrombin Homo sapiens 38-46 8613987-3 1996 Namely, at 25 degrees C, the value of delta G of sodium binding was found equal to -2.4 kcal/mol in the absence of TM and -3.6 kcal/mol for the thrombin-TM complex. Sodium 49-55 coagulation factor II, thrombin Homo sapiens 144-152 35419655-0 2022 Simulations suggest double sodium binding induces unexpected conformational changes in thrombin. Sodium 27-33 coagulation factor II, thrombin Homo sapiens 87-95 35419655-6 2022 The correlation matrices for different binding modes suggest regions that may play an important role in thrombin"s allosteric response and provide us a possible allosteric pathway for the sodium binding. Sodium 188-194 coagulation factor II, thrombin Homo sapiens 104-112 35419655-8 2022 Principal component analysis (PCA) shows us how the different regions of thrombin change conformation together with sodium binding. Sodium 116-122 coagulation factor II, thrombin Homo sapiens 73-81 6404909-0 1983 Role of sodium in ADP- and thrombin-induced megakaryocyte spreading. Sodium 8-14 coagulation factor II, thrombin Homo sapiens 27-35 2730914-0 1989 Effects of sodium removal on calcium mobilization and dense granule secretion induced by thrombin in human platelets. Sodium 11-17 coagulation factor II, thrombin Homo sapiens 89-97 2730914-1 1989 Removal of extracellular sodium decreased calcium mobilization from intracellular stores induced by thrombin in aspirin-treated human platelets. Sodium 25-31 coagulation factor II, thrombin Homo sapiens 100-108 2730914-7 1989 These results suggest that the presence of external sodium is required for normal thrombin-induced calcium release from the intracellular stores and hence for dense granule secretion. Sodium 52-58 coagulation factor II, thrombin Homo sapiens 82-90 3027576-3 1987 The data we present here indicate that inhibition of this transport by ethylisopropyl-amiloride or by lowering extracellular sodium reduces or even completely suppresses the rise in cytoplasmic free Ca2+ concentration that is essential for platelet aggregation in response to thrombin. Sodium 125-131 coagulation factor II, thrombin Homo sapiens 276-284 6693420-2 1984 The dose-dependent depolarization of the platelet"s negative membrane potential by thrombin is in large part due to a rapid uptake of sodium. Sodium 134-140 coagulation factor II, thrombin Homo sapiens 83-91 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. Sodium 131-137 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. Sodium 131-137 coagulation factor II, thrombin Homo sapiens 231-239 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. Sodium 188-194 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. Sodium 188-194 coagulation factor II, thrombin Homo sapiens 231-239 6404909-1 1983 We investigated the role of sodium in megakaryocyte spreading induced by thrombin and ADP. Sodium 28-34 coagulation factor II, thrombin Homo sapiens 73-81 6404909-12 1983 These results indicate that megakaryocyte spreading induced by ADP and thrombin depends on an increase in sodium conductance. Sodium 106-112 coagulation factor II, thrombin Homo sapiens 71-79 31974511-0 2020 Sodium-induced population shift drives activation of thrombin. Sodium 0-6 coagulation factor II, thrombin Homo sapiens 53-61 33471524-8 2021 With respect to charge distribution, Glu192, together with the thrombin-specific sodium ion, helps in creating an electrostatic gradient across the S1 pocket. Sodium 81-87 coagulation factor II, thrombin Homo sapiens 63-71 31594586-2 2020 The thrombin aptamer1-functionalized magnetic sodium alginate (Malg-Apt1) hydrogel was synthesized by physical interaction between sodium alginate and Ca2+, and it was used in the biosensor for separating and enriching thrombin. Sodium 46-52 coagulation factor II, thrombin Homo sapiens 219-227 31594586-2 2020 The thrombin aptamer1-functionalized magnetic sodium alginate (Malg-Apt1) hydrogel was synthesized by physical interaction between sodium alginate and Ca2+, and it was used in the biosensor for separating and enriching thrombin. Sodium 131-137 coagulation factor II, thrombin Homo sapiens 4-12 31594586-0 2020 A "signal-on" chemiluminescence biosensor for thrombin detection based on DNA functionalized magnetic sodium alginate hydrogel and metalloporphyrinic metal-organic framework nanosheets. Sodium 102-108 coagulation factor II, thrombin Homo sapiens 46-54 31594586-2 2020 The thrombin aptamer1-functionalized magnetic sodium alginate (Malg-Apt1) hydrogel was synthesized by physical interaction between sodium alginate and Ca2+, and it was used in the biosensor for separating and enriching thrombin. Sodium 46-52 coagulation factor II, thrombin Homo sapiens 4-12