PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17489664-1 2007 Enoxaparin is a low-molecular-weight heparin (LMWH) derivative that exerts its anticoagulant activity through antithrombin III, an endogenous inhibitor of factor Xa and thrombin IIa. Heparin, Low-Molecular-Weight 46-50 serpin family C member 1 Homo sapiens 110-126 20229677-11 2010 One case (0.62%) of DVT propagation into the vena cava occurred in a woman with antithrombin deficiency treated with LMWH. Heparin, Low-Molecular-Weight 117-121 serpin family C member 1 Homo sapiens 80-92 17376263-5 2007 Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI. Heparin, Low-Molecular-Weight 84-88 serpin family C member 1 Homo sapiens 130-142 17600391-9 2007 In the case of pregnancy, antithrombin concentrate is often used around the time of birth when LMWH may increase the risk of post-partum haemorrhage. Heparin, Low-Molecular-Weight 95-99 serpin family C member 1 Homo sapiens 26-38 17966105-0 2007 [The insufficiency of low molecular weight heparin (LMWH) prophylaxis in patients with hereditary antithrombin (AT) deficiency]. Heparin, Low-Molecular-Weight 52-56 serpin family C member 1 Homo sapiens 98-110 15567452-0 2005 Pharmacokinetics of UH and LMWH are similar with respect to antithrombin activity. Heparin, Low-Molecular-Weight 27-31 serpin family C member 1 Homo sapiens 60-72 16344381-11 2005 These data suggest that LMWH should be the preferred antithrombin in this setting. Heparin, Low-Molecular-Weight 24-28 serpin family C member 1 Homo sapiens 53-65 15957976-5 2005 Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned. Heparin, Low-Molecular-Weight 26-30 serpin family C member 1 Homo sapiens 0-12 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 83-88 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 83-88 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 83-88 12871355-5 2003 RESULTS: The antithrombin activity and the effects on TG and APTT are primarily determined by the concentration of C-domain and independent of the source material (UFH or LMWH) or Mr. High Mr fractions (>15 000) are less active, probably through interaction with non-antithrombin plasma proteins. Heparin, Low-Molecular-Weight 171-175 serpin family C member 1 Homo sapiens 13-25 15199446-4 2003 Larger clinical studies are needed to confirm the safety and efficacy of LMWH as an antithrombin for the treatment across the spectrum of ACS. Heparin, Low-Molecular-Weight 73-77 serpin family C member 1 Homo sapiens 84-96 15339877-6 2004 These include fondaparinux and idraparinux, synthetic analogs of the pentasaccharide sequence that mediates the interaction of heparin and LMWH with antithrombin, and ximelagatran, an orally active inhibitor of thrombin. Heparin, Low-Molecular-Weight 139-143 serpin family C member 1 Homo sapiens 149-161 15116263-3 2004 Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH. Heparin, Low-Molecular-Weight 122-126 serpin family C member 1 Homo sapiens 20-32 15210403-13 2004 In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity. Heparin, Low-Molecular-Weight 18-22 serpin family C member 1 Homo sapiens 157-169 15168893-1 2004 Clinical practice over the past decade has evolved to include new agents, LMWH and synthetic polysaccharides, that bind to and enhance the activity of antithrombin similar to UFH. Heparin, Low-Molecular-Weight 74-78 serpin family C member 1 Homo sapiens 151-163 9736420-8 1998 The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis. Heparin, Low-Molecular-Weight 35-39 serpin family C member 1 Homo sapiens 43-55 11134031-2 2001 Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold. Heparin, Low-Molecular-Weight 34-38 serpin family C member 1 Homo sapiens 66-78 11134031-2 2001 Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold. Heparin, Low-Molecular-Weight 83-87 serpin family C member 1 Homo sapiens 66-78 11124600-7 2000 Serum anti-Xa activity is better than activated partial thromboplastin time and antithrombin in assessing the optimal dose of LMWH. Heparin, Low-Molecular-Weight 126-130 serpin family C member 1 Homo sapiens 80-92 11096650-7 2000 On the other hand, available data suggest that serious bleeding should not be problematic despite difficulties measuring that antithrombin effect among patients receiving LMWH, even when it is combined with potent platelet inhibitor therapy. Heparin, Low-Molecular-Weight 171-175 serpin family C member 1 Homo sapiens 126-138 9748565-3 1998 The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan. Heparin, Low-Molecular-Weight 255-259 serpin family C member 1 Homo sapiens 82-94 9748565-4 1998 Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol. Heparin, Low-Molecular-Weight 118-122 serpin family C member 1 Homo sapiens 53-65 9748565-4 1998 Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol. Heparin, Low-Molecular-Weight 118-122 serpin family C member 1 Homo sapiens 190-202 11668417-2 2001 To gain insight into structure-activity relationships, we investigated quantitatively the interactions of a series of sulfated LMW heparins of similar molecular weights (derived from statistical desulfation of a supersulfated heparin) with the target enzymes human antithrombin (AT) and thrombin (T). Heparin, Low-Molecular-Weight 127-139 serpin family C member 1 Homo sapiens 265-277 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin, Low-Molecular-Weight 66-70 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin, Low-Molecular-Weight 66-70 serpin family C member 1 Homo sapiens 248-260 11465877-1 2001 UNLABELLED: Reviparin (reviparin sodium) is a low molecular weight heparin (LMWH) that catalyses the inactivation of factors Xa and IIa by binding to antithrombin, which ultimately leads to the inhibition of the clotting cascade. Heparin, Low-Molecular-Weight 76-80 serpin family C member 1 Homo sapiens 150-162 9737475-2 1998 The favorable pharmacologic properties of LMWHs include a binding affinity for antithrombin III, anti-factor IIa activity, excellent bioavailability, minimal protein binding, predictable anticoagulant response, and clinical tolerance by patients. Heparin, Low-Molecular-Weight 42-47 serpin family C member 1 Homo sapiens 79-91 9684790-4 1998 The second order rate constant of the inactivation of FXIa by antithrombin was increased up to 6-fold by LMWH, whereas LMWdxs had no effect. Heparin, Low-Molecular-Weight 105-109 serpin family C member 1 Homo sapiens 62-74 9684790-7 1998 LMWH at maximal therapeutic plasma levels enhanced the contribution of antithrombin to the inactivation of FXIa in plasma up to 5-fold. Heparin, Low-Molecular-Weight 0-4 serpin family C member 1 Homo sapiens 71-83 9684790-9 1998 Furthermore, LMWH but not LMWdxs slightly enhanced FXIa inhibition by antithrombin. Heparin, Low-Molecular-Weight 13-17 serpin family C member 1 Homo sapiens 70-82 9736420-8 1998 The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis. Heparin, Low-Molecular-Weight 115-119 serpin family C member 1 Homo sapiens 43-55 8137606-3 1993 All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin. Heparin, Low-Molecular-Weight 4-16 serpin family C member 1 Homo sapiens 29-45 9868079-4 1997 Low molecular weight heparin (LMWH) prolonged significantly PT and APTT, and this effect ws weakened by an antibody against human AT III. Heparin, Low-Molecular-Weight 30-34 serpin family C member 1 Homo sapiens 130-136 7932105-3 1994 The procedures were based on the photometric determination of the inactivation of FXa and FIIa after incubation with LMWH in the presence of antithrombin III (AT III). Heparin, Low-Molecular-Weight 117-121 serpin family C member 1 Homo sapiens 159-165 8822125-3 1996 LMWH contains both high and low affinity fragments to antithrombin-III. Heparin, Low-Molecular-Weight 0-4 serpin family C member 1 Homo sapiens 54-70 8152901-1 1994 Some commercially available chronometric assays are influenced by the residual antithrombin activity of low molecular weight heparins (LMWH) and they underestimate the ex vivo anti Xa activity. Heparin, Low-Molecular-Weight 135-139 serpin family C member 1 Homo sapiens 79-91 8259546-6 1993 DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation. Heparin, Low-Molecular-Weight 101-105 serpin family C member 1 Homo sapiens 115-120 8259546-7 1993 Compared to plasma containing DS alone, the formation of ATIII-IIa complexes also is increased when the combination of DS and LMWH is added. Heparin, Low-Molecular-Weight 126-130 serpin family C member 1 Homo sapiens 57-62 2173168-6 1990 Antithrombin III levels were significantly higher at the end of the observation period in the LMW heparin group (p less than 0.005). Heparin, Low-Molecular-Weight 94-105 serpin family C member 1 Homo sapiens 0-16 1650391-3 1991 The interest raised by low molecular weight heparins (LMWH), prepared as early as 1970, was based on a concept that is currently called into question: their anti-Xa activity, accounting for the antithrombotic activity, is high, while the anti-IIa (antithrombin) activity, producing the hemorrhagic risks, is lower. Heparin, Low-Molecular-Weight 54-58 serpin family C member 1 Homo sapiens 248-260 1664095-5 1991 The clearance of the antithrombin activity of a LMWH is higher than that of the antifactor Xa activity. Heparin, Low-Molecular-Weight 48-52 serpin family C member 1 Homo sapiens 21-33 34955853-2 2021 Low molecular weight heparin (LMWH) is one of the most widely used anticoagulants although LMWHs differ in their anti-Xa, antithrombin, and anticoagulant activities. Heparin, Low-Molecular-Weight 0-28 serpin family C member 1 Homo sapiens 122-134 2196192-2 1990 In this study the ability of a low molecular weight heparin (LMWH) (Fluxum, Alfa-Wassermann S.p.A., Bologna, Italy), as well as unfractioned heparin, to preserve ATIII activity from glucose-induced alterations, both in vitro and in vivo, is reported. Heparin, Low-Molecular-Weight 61-65 serpin family C member 1 Homo sapiens 162-167 2196192-3 1990 The subcutaneous and intravenous LMWH and heparin administration increases basal depressed ATIII activity in diabetic patients. Heparin, Low-Molecular-Weight 33-37 serpin family C member 1 Homo sapiens 91-96 34955853-2 2021 Low molecular weight heparin (LMWH) is one of the most widely used anticoagulants although LMWHs differ in their anti-Xa, antithrombin, and anticoagulant activities. Heparin, Low-Molecular-Weight 30-34 serpin family C member 1 Homo sapiens 122-134 26686866-2 2016 The molecule is a recombinant protein analog of factor Xa that binds to Factor Xa inhibitors and antithrombin:LMWH complex but does not trigger prothrombotic activity. Heparin, Low-Molecular-Weight 110-114 serpin family C member 1 Homo sapiens 97-109 32841498-0 2020 Impact of exogenous antithrombin on low molecular weight heparin anti-Xa activity assays in a pediatric and young adult leukemia and lymphoma cohort with variable antithrombin levels. Heparin, Low-Molecular-Weight 36-64 serpin family C member 1 Homo sapiens 20-32 28667866-1 2017 Using an illustrative case of a patient with antithrombin (AT) deficiency who developed a recurrent venous thromboembolism (VTE) in pregnancy despite therapeutic low-molecular-weight heparin (LMWH), we highlight what is known in the literature and address areas of controversy through a series of questions around the case. Heparin, Low-Molecular-Weight 192-196 serpin family C member 1 Homo sapiens 45-57 28282887-1 2017 Low Molecular Weight Heparins (LMWH) are complex anticoagulant drugs that mainly inhibit the blood coagulation cascade through indirect interaction with antithrombin. Heparin, Low-Molecular-Weight 31-35 serpin family C member 1 Homo sapiens 153-165 2561387-3 1989 The definite mode of action remains unknown, but LMWH act at different steps like coagulation (by AT III), fibrinolysis, blood cells, endothelial cells. Heparin, Low-Molecular-Weight 49-53 serpin family C member 1 Homo sapiens 98-104 3196877-6 1988 The inhibition of thrombin generation by the LMWH was comparable with that of standard heparin on the basis of their respective antithrombin specific activities, but not on the basis of their antifactor Xa activities. Heparin, Low-Molecular-Weight 45-49 serpin family C member 1 Homo sapiens 128-140 2851191-7 1988 This concentration of the three LMW heparins increased, by approximately 70-fold, the rate of factor Xa inhibition by purified antithrombin III compared to the 50-fold increase seen with the two unfractionated heparins. Heparin, Low-Molecular-Weight 32-44 serpin family C member 1 Homo sapiens 127-143 30660948-9 2019 Antithrombin activity correlated with anti-Xa activity of UFH (R = 0.77) and LMWH (R = 0.66). Heparin, Low-Molecular-Weight 77-81 serpin family C member 1 Homo sapiens 0-12 27898513-1 2017 : The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH. Heparin, Low-Molecular-Weight 93-97 serpin family C member 1 Homo sapiens 128-140 28282887-3 2017 In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin). Heparin, Low-Molecular-Weight 165-169 serpin family C member 1 Homo sapiens 70-82 28168066-3 2017 We present a case of a woman with antithrombin (AT) deficiency who presented with a VTE despite therapeutic low molecular weight heparin (LMWH). Heparin, Low-Molecular-Weight 138-142 serpin family C member 1 Homo sapiens 34-46 24164039-2 2013 The methodology of an anti-factor Xa assay is that LMWH is added to a known amount of excess factor Xa and excess antithrombin. Heparin, Low-Molecular-Weight 51-55 serpin family C member 1 Homo sapiens 114-126 23010574-7 2012 Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding. Heparin, Low-Molecular-Weight 216-220 serpin family C member 1 Homo sapiens 178-183 22905983-9 2012 The molecular target for LMWH/ssLMWH was confirmed by supplementing FIX/antithrombin-depleted plasma with 90 nm recombinant FIX possessing mutations in the heparin-binding exosite. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 72-84 22905983-11 2012 CONCLUSIONS: Therapeutic LMWH concentrations inhibit plasma thrombin generation via antithrombin-independent interaction with the FIXa heparin-binding exosite. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 84-96