PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8037658-8	1994	Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin.	Cysteine	143-149	serpin family C member 1	Homo sapiens	200-216	
9521646-2	1998	We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa.	Cysteine	173-181	serpin family C member 1	Homo sapiens	18-30	
9521646-3	1998	By derivatization of this cysteine with a bulky group, fluorescein, the antithrombin became permanently and fully activated toward reaction with factor Xa in a manner analogous to heparin activation, albeit as a substrate.	Cysteine	26-34	serpin family C member 1	Homo sapiens	72-84	
8874869-0	1996	A novel nonsense mutation in the antithrombin III gene (Cys-4-->stop) causing recurrent venous thrombosis.	Cysteine	56-59	serpin family C member 1	Homo sapiens	33-49	
8176841-8	1994	The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine.	Cysteine	98-106	serpin family C member 1	Homo sapiens	4-20	
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Cysteine	109-112	serpin family C member 1	Homo sapiens	37-49	
8376590-7	1993	The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine.	Cysteine	103-111	serpin family C member 1	Homo sapiens	4-20	
1546950-11	1992	The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained.	Cysteine	45-48	serpin family C member 1	Homo sapiens	68-74	
8357789-3	1993	To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide.	Cysteine	169-177	serpin family C member 1	Homo sapiens	136-148	
1546950-11	1992	The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained.	Cysteine	57-60	serpin family C member 1	Homo sapiens	68-74	
1546950-12	1992	Mutations in full-length AT-III at Cys-430 had no effect on the ability of AT-III to bind heparin.	Cysteine	35-38	serpin family C member 1	Homo sapiens	25-31	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	68-71	serpin family C member 1	Homo sapiens	6-22	
2390061-2	1990	We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities.	Cysteine	76-79	serpin family C member 1	Homo sapiens	57-63	
2390061-2	1990	We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities.	Cysteine	76-79	serpin family C member 1	Homo sapiens	57-63	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	68-71	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	6-22	
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30	
2390061-2	1990	We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities.	Cysteine	70-73	serpin family C member 1	Homo sapiens	57-63	
2390061-2	1990	We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities.	Cysteine	76-79	serpin family C member 1	Homo sapiens	57-63	
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Cysteine	90-93	serpin family C member 1	Homo sapiens	57-73	
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Cysteine	90-93	serpin family C member 1	Homo sapiens	150-166	
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Cysteine	102-105	serpin family C member 1	Homo sapiens	57-73	
30431449-2	2019	We encountered a case of inherited type I AT deficiency and identified the causative mutation; a novel c.7430A>G missense mutation in the SERPINC1 gene in which tyrosine was substituted for cysteine at the 292nd amino acid.	Cysteine	193-201	serpin family C member 1	Homo sapiens	141-149	
18206177-0	2008	Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine.	Cysteine	55-63	serpin family C member 1	Homo sapiens	0-12	
18206177-7	2008	When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost.	Cysteine	53-61	serpin family C member 1	Homo sapiens	5-17	
18206177-7	2008	When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost.	Cysteine	53-61	serpin family C member 1	Homo sapiens	85-97