PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3191114-7 1988 Proline-407 is located 14 amino acids C-terminal to the reactive site arginine of ATIII in a core region of the molecule that has been highly conserved during evolution of the serine protease inhibitor (serpin) gene family. Arginine 70-78 serpin family C member 1 Homo sapiens 82-87 3305015-9 1987 259, 939-941], the heparin-binding site of antithrombin III has been suggested to be in the region of Pro-41, Arg-47 and Trp-49. Arginine 110-113 serpin family C member 1 Homo sapiens 43-59 3260695-1 1988 Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction. Arginine 51-59 serpin family C member 1 Homo sapiens 0-16 3260695-1 1988 Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction. Arginine 51-59 serpin family C member 1 Homo sapiens 18-24 3080419-6 1986 This substitution is close to an Arg (residue 47) and a Trp (residue 49) which have previously been shown to be critical for heparin binding by antithrombin III. Arginine 33-36 serpin family C member 1 Homo sapiens 144-160 3603738-0 1987 [Antithrombin activity of methyl esters of arginine-containing peptides]. Arginine 43-51 serpin family C member 1 Homo sapiens 1-13 3754413-3 1986 Both antithrombin and heparin cofactor activities of heparin cofactor II are inactivated by the arginine-specific reagent, 2,3-butanedione. Arginine 96-104 serpin family C member 1 Homo sapiens 5-17 6977539-9 1982 The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin. Arginine 168-171 serpin family C member 1 Homo sapiens 72-84 3863104-4 1985 Arginine-modified heparin cofactor II showed a comparable percentage loss of both antichymotrypsin and antithrombin activities. Arginine 0-8 serpin family C member 1 Homo sapiens 103-115 6338832-1 1983 The inhibition of thrombin by antithrombin-III involves formation of a 1:1 covalent complex between protease and inhibitor and concomitant cleavage of the antithrombin-III peptide chain after Arg-385. Arginine 192-195 serpin family C member 1 Homo sapiens 30-46 6338832-1 1983 The inhibition of thrombin by antithrombin-III involves formation of a 1:1 covalent complex between protease and inhibitor and concomitant cleavage of the antithrombin-III peptide chain after Arg-385. Arginine 192-195 serpin family C member 1 Homo sapiens 155-171 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Arginine 56-59 serpin family C member 1 Homo sapiens 66-72 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Arginine 124-132 serpin family C member 1 Homo sapiens 66-72 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Arginine 134-137 serpin family C member 1 Homo sapiens 66-72 6582486-6 1984 Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama. Arginine 72-80 serpin family C member 1 Homo sapiens 94-110 6582486-6 1984 Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama. Arginine 72-80 serpin family C member 1 Homo sapiens 94-106 6977539-9 1982 The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin. Arginine 168-171 serpin family C member 1 Homo sapiens 212-224 32194638-10 2020 This novel mutation resulted in a substitution of arginine by tryptophan, leading to antithrombin resistance (ATR). Arginine 50-58 serpin family C member 1 Homo sapiens 85-97 6790279-1 1981 Previous studies have shown that a modified form of antithrombin, cleaved at a single Arg-Ser bond near the carboxy-terminal end of the chain, is formed during the reaction with thrombin concurrent with the formation of the inactive enzyme-inhibitor complex. Arginine 86-89 serpin family C member 1 Homo sapiens 52-64 7213342-11 1980 The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s). Arginine 117-125 serpin family C member 1 Homo sapiens 50-66 7213342-11 1980 The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s). Arginine 140-148 serpin family C member 1 Homo sapiens 50-66 6966584-1 1980 The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively. Arginine 105-108 serpin family C member 1 Homo sapiens 60-76 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Arginine 147-150 serpin family C member 1 Homo sapiens 45-51 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Arginine 147-150 serpin family C member 1 Homo sapiens 57-63 26797521-2 2016 Although another plasma serpin with an Arg-Ser reactive centre, antithrombin (AT), has been shown to inhibit factor VIIa (FVIIa), no published data are available with respect to FVIIa inhibition by API M358R. Arginine 39-42 serpin family C member 1 Homo sapiens 64-76 27010094-7 2016 Genetic analysis revealed a single-base substitution (C>T) at the codon 359 (Arg to STOP) in the 5th exon portion of the antithrombin gene, heterozygote. Arginine 80-83 serpin family C member 1 Homo sapiens 124-136 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Arginine 131-134 serpin family C member 1 Homo sapiens 54-59 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 41-43 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 41-43 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 120-122 25307422-10 2014 Results from LC-MS/MS experiments revealed that MGO covalently adducts the active site Arg 393 of ATIII through two distinct glyoxalation mechanisms. Arginine 87-90 serpin family C member 1 Homo sapiens 98-103 23581397-6 2013 METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain. Arginine 121-129 serpin family C member 1 Homo sapiens 24-26 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Arginine 142-145 serpin family C member 1 Homo sapiens 54-59 19172319-5 2009 However, detailed comparison of our modeled structure of ZPI/FXa with that of AT3/FXa points to differences in interaction specificity at the reactive center and in the stability of the inhibitory complex, due to the presence of a tyrosine residue at the P1 position in ZPI, instead of the P1 arginine residue in AT3. Arginine 293-301 serpin family C member 1 Homo sapiens 78-81 19818773-2 2009 The currently-accepted mechanism involves removal of a constraint on the antithrombin reactive center loop (RCL) so that the proteinase can simultaneously engage both the P1 arginine and an exosite at Y253. Arginine 174-182 serpin family C member 1 Homo sapiens 73-85 19843180-3 2009 We have evaluated the functional and conformational effects on antithrombin of citrullination, a post-translational modification catalyzed by peptidylarginine deiminase (PAD), which changes arginine to citrulline. Arginine 150-158 serpin family C member 1 Homo sapiens 63-75 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. Arginine 15-23 serpin family C member 1 Homo sapiens 35-47 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Arginine 113-121 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Arginine 113-121 serpin family C member 1 Homo sapiens 107-112 12939144-10 2003 We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions. Arginine 137-145 serpin family C member 1 Homo sapiens 101-113 12939144-10 2003 We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions. Arginine 137-145 serpin family C member 1 Homo sapiens 195-207 12846563-4 2003 Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity. Arginine 162-165 serpin family C member 1 Homo sapiens 48-60 19010776-5 2009 Mutation of Arg-150 in factor Xa, which interacts with the exosite residues in heparin-activated antithrombin, abrogated the ability of the engineered exosites in alpha1PI to promote factor Xa inhibition. Arginine 12-15 serpin family C member 1 Homo sapiens 97-109 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Arginine 113-121 serpin family C member 1 Homo sapiens 107-112 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. Arginine 15-23 serpin family C member 1 Homo sapiens 57-69 12591924-2 2003 Sequencing of the antithrombin genes of the patient revealed that one of the two alleles was abnormal due to an in-frame deletion of the codon for the P1 arginine residue. Arginine 154-162 serpin family C member 1 Homo sapiens 18-30 12369826-5 2002 However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114. Arginine 70-73 serpin family C member 1 Homo sapiens 151-163 12369826-10 2002 This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor. Arginine 54-57 serpin family C member 1 Homo sapiens 93-105 12369826-10 2002 This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor. Arginine 181-184 serpin family C member 1 Homo sapiens 93-105 11380262-2 2001 Heparin has been proposed to conformationally activate the serpin, antithrombin, by making the reactive center loop P1 arginine residue accessible to proteinases. Arginine 119-127 serpin family C member 1 Homo sapiens 67-79 11971909-0 2002 Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition. Arginine 18-26 serpin family C member 1 Homo sapiens 97-113 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. Arginine 32-35 serpin family C member 1 Homo sapiens 203-215 12022882-6 2002 The reactivities of Arg(143) and Lys(147) mutants were improved approximately 2-fold with antithrombin in the absence but not in the presence of heparin cofactors. Arginine 20-23 serpin family C member 1 Homo sapiens 90-102 12022882-7 2002 On the other hand, the pentasaccharide-catalyzed reactivity of antithrombin with the Arg(150) mutant was impaired by an order of magnitude. Arginine 85-88 serpin family C member 1 Homo sapiens 63-75 12022882-8 2002 These results suggest that Arg(150) of the autolysis loop may specifically interact with the activated conformation of antithrombin. Arginine 27-30 serpin family C member 1 Homo sapiens 119-131 11389017-4 2001 The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond. Arginine 179-182 serpin family C member 1 Homo sapiens 75-91 11389017-4 2001 The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond. Arginine 179-182 serpin family C member 1 Homo sapiens 133-149 11380262-3 2001 To evaluate this proposal, we determined the effect of mutating the P1 arginine on antithrombin"s specificity for target and nontarget proteinases in both native and heparin-activated states of the serpin. Arginine 71-79 serpin family C member 1 Homo sapiens 83-95 11380262-4 2001 As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)). Arginine 32-40 serpin family C member 1 Homo sapiens 120-132 11380262-6 2001 Mutation of the P1 arginine greatly reduced k(assoc) for antithrombin inhibition of thrombin and factor Xa from 40- to 5000-fold, but heparin normally accelerated the reactions of the variant antithrombins with these enzymes to make them reasonably efficient inhibitors (k(assoc) = 10(3)-10(4) M(-1) s(-1)). Arginine 19-27 serpin family C member 1 Homo sapiens 57-69 11380262-10 2001 Together, these findings suggest that the P1 arginine residue is similarly accessible to proteinases in both native and heparin-activated states of the serpin and contributes similarly to the specificity of antithrombin for thrombin and factor Xa in the two serpin conformational states. Arginine 45-53 serpin family C member 1 Homo sapiens 207-219 10764763-0 2000 Role of arginine 129 in heparin binding and activation of antithrombin. Arginine 8-16 serpin family C member 1 Homo sapiens 58-70 10764763-1 2000 The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln. Arginine 20-23 serpin family C member 1 Homo sapiens 44-56 10764763-6 2000 These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state. Arginine 44-47 serpin family C member 1 Homo sapiens 106-118 10764763-6 2000 These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state. Arginine 177-180 serpin family C member 1 Homo sapiens 106-118 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. Arginine 35-38 serpin family C member 1 Homo sapiens 48-60 8900394-6 1996 In one case, the Arg residue of the reference peptide corresponding to R129 of ATIII has been replaced by Gln (R129deltaQ peptide), thus mimicking the naturally occurring mutant protein, ATIII Geneva. Arginine 17-20 serpin family C member 1 Homo sapiens 79-84 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 42-45 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9242619-0 1997 Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity. Arginine 54-62 serpin family C member 1 Homo sapiens 66-78 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. Arginine 43-46 serpin family C member 1 Homo sapiens 56-68 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. Arginine 43-46 serpin family C member 1 Homo sapiens 261-273 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. Arginine 326-329 serpin family C member 1 Homo sapiens 56-68 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. Arginine 35-38 serpin family C member 1 Homo sapiens 238-250 9242619-5 1997 The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1 Arg. Arginine 165-168 serpin family C member 1 Homo sapiens 38-50 9242619-5 1997 The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1 Arg. Arginine 298-301 serpin family C member 1 Homo sapiens 38-50 8910598-0 1996 Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. Arginine 8-16 serpin family C member 1 Homo sapiens 76-88 7893664-2 1995 The serpins antithrombin, protease nexin 1, and alpha 1-antitrypsin with a reactive-center arginine (Arg-alpha 1-antitrypsin) were found to inhibit the sperm protease acrosin with varying efficiency. Arginine 91-99 serpin family C member 1 Homo sapiens 12-24 8392392-4 1993 Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser). Arginine 156-159 serpin family C member 1 Homo sapiens 111-123 7981186-1 1994 We have identified three novel mutations of the antithrombin (AT) gene in patients with thrombotic complications: a Cys 128 --> Tyr mutations, a G --> A mutation in the intervening sequence 4 (IVS4) 14 nucleotide 5" to exon 5, and a 9 bp deletion in the 3" end of exon 6 resulting in a short aberrant sequence after Arg 425. Arginine 316-319 serpin family C member 1 Homo sapiens 48-60 7981186-1 1994 We have identified three novel mutations of the antithrombin (AT) gene in patients with thrombotic complications: a Cys 128 --> Tyr mutations, a G --> A mutation in the intervening sequence 4 (IVS4) 14 nucleotide 5" to exon 5, and a 9 bp deletion in the 3" end of exon 6 resulting in a short aberrant sequence after Arg 425. Arginine 316-319 serpin family C member 1 Homo sapiens 62-64 8280781-0 1994 Arg-129 plays a specific role in the conformation of antithrombin and in the enhancement of factor Xa inhibition by the pentasaccharide sequence of heparin. Arginine 0-3 serpin family C member 1 Homo sapiens 53-65 8186357-5 1994 This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule. Arginine 117-125 serpin family C member 1 Homo sapiens 153-165 8331659-9 1993 Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein. Arginine 137-145 serpin family C member 1 Homo sapiens 101-106 1331047-6 1992 The two peptides, particularly IIFMGRVANP, directly enhanced the amidolytic activity of thrombin and Factor Xa on the synthetic substrate Boc-Ala-Gly-Arg-MCA (where Boc is t-butoxycarbonyl and MCA is 4-methylcoumarin), which corresponds to residues P3-P1 of the reactive site of antithrombin III, and also on other substrates due to increased Vmax. Arginine 150-153 serpin family C member 1 Homo sapiens 279-295 1569192-4 1992 A G to T transition at nucleotide 10038 results in the substitution of Met to an Arg, converting alpha 1-AT into an Arg-Ser protease inhibitor (serpin) that inhibited thrombin and Factor Xa more effectively than antithrombin III. Arginine 81-84 serpin family C member 1 Homo sapiens 212-228 1870264-5 1991 Nucleotide sequencing of exon 6 of AT III gene showed a G to T transitional mutation resulting in the conversion of arginine-406 to methionine coexisted with normal allele which encodes arginine. Arginine 116-124 serpin family C member 1 Homo sapiens 35-41 1776135-3 1991 Arginine-406 is located at the 12th amino acid residue from the reactive site on the C-terminal side of AT-III in a core region of the molecule which has been highly conserved during evolution of serine protease inhibitor (serpin) family. Arginine 0-8 serpin family C member 1 Homo sapiens 104-110 2394749-10 1990 The predicted reactive site (P1-P1") of this J6 protein is Arg-Ser, which is the same as that of antithrombin III. Arginine 59-62 serpin family C member 1 Homo sapiens 97-113 2229057-0 1990 Important role of arginine 129 in heparin-binding site of antithrombin III. Arginine 18-26 serpin family C member 1 Homo sapiens 58-74 2229057-4 1990 This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding. Arginine 130-133 serpin family C member 1 Homo sapiens 31-36 2229057-7 1990 Taken together, these results demonstrate an important role for Arg-129 in the binding and interaction of ATIII with heparin of high affinity. Arginine 64-67 serpin family C member 1 Homo sapiens 106-111 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Arginine 47-50 serpin family C member 1 Homo sapiens 212-217 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Arginine 69-72 serpin family C member 1 Homo sapiens 212-217