PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22498748-4 2012 These mutations do not modify the folding or secretion of the protein, but abolish the glycosaminoglycan-induced activation of antithrombin by affecting the heparin-binding domain. Glycosaminoglycans 87-104 serpin family C member 1 Homo sapiens 127-139 22315264-3 2012 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 66-78 21866614-20 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 87-103 23152789-4 2012 The availability of multiple co-crystal structures facilitates a structural analysis that challenges the long-held belief that the GAG binding sites in antithrombin and thrombin are essentially similar with high solvent exposure and shallow surface characteristics. Glycosaminoglycans 131-134 serpin family C member 1 Homo sapiens 152-164 12010802-8 2002 The observation that chemically modified AT III that lacks heparin-binding capacity had no effect on NF-kappaB activation supports the current understanding that the inhibitory potency of AT III depends on the interaction of AT III with heparinlike cell surface glycosaminoglycans. Glycosaminoglycans 262-280 serpin family C member 1 Homo sapiens 188-194 15383472-2 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 66-78 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Glycosaminoglycans 43-61 serpin family C member 1 Homo sapiens 214-230 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Glycosaminoglycans 63-66 serpin family C member 1 Homo sapiens 214-230 12907439-5 2003 The stoichiometries were not affected by pentasaccharides, indicating that the inhibitory mechanism of antithrombin Cambridge II is perturbed only in the presence of a bridging glycosaminoglycan. Glycosaminoglycans 177-194 serpin family C member 1 Homo sapiens 103-115 12865952-5 2003 Antithrombin binds to endothelial glycosaminoglycans and then significantly increases anticoagulant activity. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 0-12 12768169-7 2003 The most important mechanism responsible of the anti-inflammatory properties of AT is the binding to the glycosaminoglycans of the endothelial cells and the consequent release of prostacyclin. Glycosaminoglycans 105-123 serpin family C member 1 Homo sapiens 80-82 12413592-1 2002 Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans. Glycosaminoglycans 235-253 serpin family C member 1 Homo sapiens 0-12 12413592-1 2002 Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans. Glycosaminoglycans 235-253 serpin family C member 1 Homo sapiens 14-19 18574264-2 2008 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 66-78 15957976-2 2005 It is one of a group of glycosaminoglycan compounds that accelerate the inactivation of factor Xa by inducing a conformational change in antithrombin. Glycosaminoglycans 24-41 serpin family C member 1 Homo sapiens 137-149 15743473-5 2005 Various glycosaminoglycans, including HA, chondroitin sulfate, keratan sulfate, heparin, and heparan, were incubated with human antithrombin III in vitro. Glycosaminoglycans 8-26 serpin family C member 1 Homo sapiens 128-144 15311269-2 2004 Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans. Glycosaminoglycans 146-164 serpin family C member 1 Homo sapiens 0-12 12010802-8 2002 The observation that chemically modified AT III that lacks heparin-binding capacity had no effect on NF-kappaB activation supports the current understanding that the inhibitory potency of AT III depends on the interaction of AT III with heparinlike cell surface glycosaminoglycans. Glycosaminoglycans 262-280 serpin family C member 1 Homo sapiens 188-194 12010802-9 2002 This hypothesis was underscored by the finding that the AT III beta-isoform, known to have higher affinity for glycosaminoglycans, is more effective in preventing NF-kappaB transactivation than alpha-AT III. Glycosaminoglycans 111-129 serpin family C member 1 Homo sapiens 56-62 11006120-4 2000 The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII. Glycosaminoglycans 115-132 serpin family C member 1 Homo sapiens 220-225 12004255-7 2002 Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces. Glycosaminoglycans 70-88 serpin family C member 1 Homo sapiens 0-12 11323006-1 2001 In the presence of glycosaminoglycans, thrombin is rapidly inactivated by two natural inhibitors secreted from liver: antithrombin (AT) is presumed to be the principal thrombin inhibitor in circulating blood, while for heparin cofactor II (HCII), a role outside circulation has been proposed. Glycosaminoglycans 19-37 serpin family C member 1 Homo sapiens 118-130 9169007-1 1997 Two major glycoforms of recombinant antithrombin which differ 10-fold in their affinity for the effector glycosaminoglycan, heparin, were previously shown to be expressed in BHK or CHO mammalian cell lines (I. Bjork, et al., 1992, Biochem. Glycosaminoglycans 105-122 serpin family C member 1 Homo sapiens 36-48 10766996-4 2000 The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N). Glycosaminoglycans 126-129 serpin family C member 1 Homo sapiens 62-65 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. Glycosaminoglycans 51-69 serpin family C member 1 Homo sapiens 24-36 9692954-11 1998 Homology modeling of PEDF based on the X-ray crystal structures of antithrombin III and ovalbumin shows a region at the center of beta-sheet A-strands 2 and 3- and helix F that has a basic electrostatic surface potential and is densely populated with lysines exposed to the surface (K134, K137, K189, K191, H212, and K214) that are available to interact with various glycosaminoglycans/polyanions. Glycosaminoglycans 367-385 serpin family C member 1 Homo sapiens 67-83 9662467-8 1998 An interaction between antithrombin and heparin-like glycosaminoglycans on the endothelial cell surface appears to be important for this effect. Glycosaminoglycans 53-71 serpin family C member 1 Homo sapiens 23-35 9662467-9 1998 Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans. Glycosaminoglycans 127-145 serpin family C member 1 Homo sapiens 45-57 11776053-3 2000 The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system. Glycosaminoglycans 30-33 serpin family C member 1 Homo sapiens 4-16 11776053-3 2000 The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system. Glycosaminoglycans 30-33 serpin family C member 1 Homo sapiens 172-184 11776053-16 2000 GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin. Glycosaminoglycans 0-3 serpin family C member 1 Homo sapiens 83-95 9713170-1 1998 We investigated the effect of cell surface glycosaminoglycans (GAGs) on the inactivation of factor VIIa-tissue factor activity by antithrombin III (ATIII) on a human bladder carcinoma (J82) cell line and an ovarian carcinoma (OC-2008) cell line, two tumor cell lines which constitutively synthesize and express high levels of cell surface tissue factor. Glycosaminoglycans 43-61 serpin family C member 1 Homo sapiens 148-153 9515777-7 1998 Interaction of AT III with heparin-like glycosaminoglycans (GAGs) on the endothelial cell surface appears to be important for this effect. Glycosaminoglycans 40-58 serpin family C member 1 Homo sapiens 15-21 7806495-3 1994 Thrombin is inhibited by the serpins antithrombin and heparin cofactor II (HCiI) in reactions that are accelerated markedly by specific glycosaminoglycans. Glycosaminoglycans 136-154 serpin family C member 1 Homo sapiens 37-49 8951806-6 1996 Numerous studies indicate that in the case of thinning of the anionic glycosaminoglycan film on the endothelial surface, the lipoprotein-lipase and antithrombin III activity induced by heparin is reduced, as result of which hyperlipoproteinaemia and increased tendency to thrombosis can only by compensated for to an inadequate extent. Glycosaminoglycans 70-87 serpin family C member 1 Homo sapiens 148-164 8662679-4 1996 The rate constants of the inactivation of FXIa by C1 inhibitor and by antithrombin III increased up to 117-fold in the presence of glycosaminoglycans. Glycosaminoglycans 131-149 serpin family C member 1 Homo sapiens 70-86 7841596-18 1994 Whether AT-III in the presence of glycosaminoglycans on cell surfaces expressing TF can function as an auxiliary second physiological regulator is not known. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 8-14 7757423-1 1994 In this paper, we report the synthesis of "non-glycosamino" glycan analogues 5-10 of the antithrombin III binding pentasaccharide 1. Glycosaminoglycans 47-66 serpin family C member 1 Homo sapiens 89-105 8186357-2 1994 In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans. Glycosaminoglycans 111-129 serpin family C member 1 Homo sapiens 40-52 8167338-2 1994 Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan. Glycosaminoglycans 236-253 serpin family C member 1 Homo sapiens 158-174 8331144-5 1993 The second approach consisted of using heparin, a mucopolysaccharide with a strong affinity towards ATIII, coupled to amine-modified or epoxy-activated membranes by reductive amination, for the purification of rATIII. Glycosaminoglycans 50-68 serpin family C member 1 Homo sapiens 100-105 7692967-9 1993 These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans. Glycosaminoglycans 165-183 serpin family C member 1 Homo sapiens 27-39 8429040-3 1993 Thrombin is inhibited by the serpins antithrombin III and heparin cofactor II in a reaction that is dramatically accelerated by glycosaminoglycans. Glycosaminoglycans 128-146 serpin family C member 1 Homo sapiens 37-53 8429008-1 1993 Heparin cofactor II and antithrombin are plasma serine proteinase inhibitors whose ability to inhibit alpha-thrombin is accelerated by glycosaminoglycans. Glycosaminoglycans 135-153 serpin family C member 1 Homo sapiens 24-36 1872461-1 1991 The identification of a specific required carbohydrate structure for the antithrombin III binding site on heparin suggests that there may be specific structures in glycosaminoglycan chains which are necessary for other vascular functions of these carbohydrates. Glycosaminoglycans 164-181 serpin family C member 1 Homo sapiens 73-89 1566349-4 1992 Displacement studies were done with glycosaminoglycans to show that the antithrombin III was bound to its glycosaminoglycan anchor via a heparinlike binding site, and replacement studies showed that antithrombin III could be returned to the same endothelial cells from which it was displaced. Glycosaminoglycans 36-54 serpin family C member 1 Homo sapiens 72-88 1566349-4 1992 Displacement studies were done with glycosaminoglycans to show that the antithrombin III was bound to its glycosaminoglycan anchor via a heparinlike binding site, and replacement studies showed that antithrombin III could be returned to the same endothelial cells from which it was displaced. Glycosaminoglycans 36-53 serpin family C member 1 Homo sapiens 72-88 3218731-0 1988 Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin. Glycosaminoglycans 63-81 serpin family C member 1 Homo sapiens 115-131 2175954-6 1990 These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production. Glycosaminoglycans 109-127 serpin family C member 1 Homo sapiens 81-86 2851191-6 1988 This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma. Glycosaminoglycans 27-44 serpin family C member 1 Homo sapiens 193-209 2851191-6 1988 This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma. Glycosaminoglycans 27-44 serpin family C member 1 Homo sapiens 283-299 2083865-8 1990 The activities of thrombin and other serine proteases are modulated by the serine protease inhibitors (serpins), including antithrombin III and heparin cofactor II which are important in regulating the physiological anticoagulant action of glycosaminoglycans at the endothelium and the pharmacological action of heparin. Glycosaminoglycans 240-258 serpin family C member 1 Homo sapiens 123-139 3218731-3 1988 This has been used to compare the binding of a range of glycosaminoglycans and other sulfated polymers to antithrombin III and thrombin, a major inhibitor of and a central protease in the coagulation system, respectively. Glycosaminoglycans 56-74 serpin family C member 1 Homo sapiens 106-122 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. Glycosaminoglycans 67-85 serpin family C member 1 Homo sapiens 89-105 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. Glycosaminoglycans 67-85 serpin family C member 1 Homo sapiens 138-154 3581111-2 1987 experiments conducted on synthetic fragments of glycosaminoglycans, one of them representing the pentasaccharidic sequence present in heparin and responsible for the binding to antithrombin III, and the others being related to this sequence. Glycosaminoglycans 48-66 serpin family C member 1 Homo sapiens 177-193 3400080-4 1988 Our results suggested that heparin-like glycosaminoglycans on endothelial cells play as important a role as heparin does in the regulation of antithrombin activity. Glycosaminoglycans 40-58 serpin family C member 1 Homo sapiens 142-154 3988937-1 1985 Clinical grade heparin is a very heterogeneous mucopolysaccharide, containing molecules with Mr ranging from 6,000 to 30,000 that have either a high affinity or a low affinity for antithrombin III (AT). Glycosaminoglycans 47-65 serpin family C member 1 Homo sapiens 180-196 6084876-0 1984 Purification and biological property of heparin cofactor II: activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans. Glycosaminoglycans 147-165 serpin family C member 1 Homo sapiens 99-115 6084876-3 1984 Chem., 257, 2162, 1982) and abilities of dextran sulfate and various glycosaminoglycans to activate the antithrombin activities of HC II and antithrombin III (AT III) were studied. Glycosaminoglycans 69-87 serpin family C member 1 Homo sapiens 104-116 6486808-2 1984 This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease inhibitor for mucopolysaccharide. Glycosaminoglycans 214-232 serpin family C member 1 Homo sapiens 103-115 6486808-5 1984 Based upon these data, it was proposed that the loss of "heparin cofactor" activity of antithrombin must be predominantly due to an inability of the modified protease inhibitor to undergo a conformational transition required for mucopolysaccharide-dependent "activation" of the macromolecule. Glycosaminoglycans 229-247 serpin family C member 1 Homo sapiens 87-99 6961402-1 1982 We have utilized circular dichroism spectroscopy to examine the interaction of antithrombin with heparin-derived oligosaccharides and mucopolysaccharides of various sizes. Glycosaminoglycans 134-153 serpin family C member 1 Homo sapiens 79-91 6746897-6 1984 The above mucopolysaccharides function in a manner similar to commercial heparin, since modification of antithrombin at a site critical for heparin-dependent acceleration of the protease inhibitor resulted in a level of interaction product identical to the uncatalyzed amount. Glycosaminoglycans 10-29 serpin family C member 1 Homo sapiens 104-116 6687888-1 1983 We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Glycosaminoglycans 38-56 serpin family C member 1 Homo sapiens 141-157 6687888-1 1983 We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Glycosaminoglycans 38-56 serpin family C member 1 Homo sapiens 159-164 6687802-5 1983 The results suggest that heparin cofactor II differs from antithrombin III with respect to the mucopolysaccharide binding site. Glycosaminoglycans 95-113 serpin family C member 1 Homo sapiens 58-74 7164033-9 1982 The antithrombin III independent effect of heparin is unlikely to be important therapeutically, however, if this property of heparin is shared by other naturally occurring glycosaminoglycans, it could be important in maintaining the fluidity of blood under physiological conditions. Glycosaminoglycans 172-190 serpin family C member 1 Homo sapiens 4-20 6961402-15 1982 Given our method for generating the above data, these spectral alterations must be associated with the binding of a second critical domain of the mucopolysaccharide to antithrombin that is required for rapid complex formation with thrombin or the activation of the protease inhibitor with respect to the neutralization of the latter enzyme. Glycosaminoglycans 146-164 serpin family C member 1 Homo sapiens 168-180 7059522-10 1982 It is concluded that this new sulphated mucopolysaccharide acts as a pure antithrombin with a potency corresponding to 40--50 iu heparin/mg S-Lim. Glycosaminoglycans 40-58 serpin family C member 1 Homo sapiens 74-86 7053378-2 1982 This methodology is able to subdivide the active mucopolysaccharide pools of molecular weight 6,000 to 8,000 (LMW) or 18,000 to 22,000 (HMW) into various species with descending affinities for antithrombin as well as decreasing anticoagulant potencies. Glycosaminoglycans 49-67 serpin family C member 1 Homo sapiens 193-205 7053378-6 1982 The stoichiometries of interaction of antithrombin and platelet factor 4 with HMW highly active heparin as determined by fluorescence spectroscopy indicated that 2 molecules of either protein are able to bind to 1 molecule of the mucopolysaccharide. Glycosaminoglycans 230-248 serpin family C member 1 Homo sapiens 38-50 7053378-8 1982 The avidity of platelet factor 4 for HMW highly active heparin could not be quantitated but appears to be at least 10 to 100 times greater than that of antithrombin for mucopolysaccharide. Glycosaminoglycans 169-187 serpin family C member 1 Homo sapiens 152-164 570737-0 1978 Inhibition of thrombin by antithrombin III in the presence of certain glycosaminoglycans found in the mammalian aorta. Glycosaminoglycans 70-88 serpin family C member 1 Homo sapiens 26-42 6448845-1 1980 A low molecular weight preparation of porcine heparin (specific anticoagulation activity = 125 units/mg) was fractionated to obtain a mucopolysaccharide product of 6500 daltons (specific anticoagulant activity = 373 units/mg) that is homogeneous with respect to its interaction with antithrombin. Glycosaminoglycans 134-152 serpin family C member 1 Homo sapiens 283-295 6448845-3 1980 Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion. Glycosaminoglycans 80-98 serpin family C member 1 Homo sapiens 115-127 6448846-17 1980 Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor. Glycosaminoglycans 87-105 serpin family C member 1 Homo sapiens 54-66 6448846-18 1980 Furthermore, a careful comparison of the various constants suggests that the direct interaction between heparin and antithrombin may be largely responsible for the kinetic effect of this mucopolysaccharide. Glycosaminoglycans 187-205 serpin family C member 1 Homo sapiens 116-128 7368150-1 1980 The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides. Glycosaminoglycans 141-160 serpin family C member 1 Homo sapiens 94-110 7368150-1 1980 The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides. Glycosaminoglycans 141-160 serpin family C member 1 Homo sapiens 112-118 33176060-9 2021 In addition to the chain length, the type and extent of sulfation of glycosaminoglycans influenced the ability of skeletal muscle myosin to neutralize the polysaccharide"s ability to enhance antithrombin"s activity. Glycosaminoglycans 69-87 serpin family C member 1 Homo sapiens 191-203 30845788-4 2019 Possible inter-species differences in the GAG-binding sites on antithrombin III, heparanase, and chemokines of the CCL and CXCL families were examined by sequence alignments, molecular modelling and assessment of surface electrostatic potentials to determine if one species of laboratory animal is likely to result in more clinically relevant data than another. Glycosaminoglycans 42-45 serpin family C member 1 Homo sapiens 63-79 30774881-4 2019 Through an experimental and computational approach using fluorescence polarization, ITC, docking and molecular dynamics simulations we investigate the binding of these functionalized GAG derivatives to ten representative regulatory proteins including IL-8, IL-10, BMP-2, sclerostin, TIMP-3, CXCL-12, TGF-beta, FGF-1, FGF-2, and AT-III, and we establish structure-activity relationships for GAG recognition. Glycosaminoglycans 183-186 serpin family C member 1 Homo sapiens 328-334 29173042-1 2018 Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate. Glycosaminoglycans 104-122 serpin family C member 1 Homo sapiens 0-12 25325940-2 2015 One example, the extensively studied heparin pentasaccharide sequence-which binds antithrombin-III, inducing a conformational change that increases its serpin protease activity by 1,000-fold-is unique in that no other specific GAG-protein structure-function relations have been described to the same degree. Glycosaminoglycans 227-230 serpin family C member 1 Homo sapiens 82-98