PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16884719-1	2006	We investigate the hypothesis that heparin activates antithrombin (AT) by relieving electrostatic strain within helix D. Mutation of residues K125 and R129 to either Ala or Glu abrogated heparin binding, but did not activate AT towards inhibition of factors IXa or Xa.	Alanine	166-169	serpin family C member 1	Homo sapiens	53-65	
10037709-3	1999	Protection from inhibition by antithrombin and heparin cofactor II requires ligation of both exosites 1 and 2 because minimal protection is seen when exosite 1 variants (gamma-thrombin and thrombin Quick 1) or an exosite 2 variant (Arg93 --> Ala, Arg97 --> Ala, and Arg101 --> Ala thrombin) is substituted for thrombin.	Alanine	245-248	serpin family C member 1	Homo sapiens	30-42	
12578831-4	2003	Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH.	Alanine	62-69	serpin family C member 1	Homo sapiens	157-169	
10037709-3	1999	Protection from inhibition by antithrombin and heparin cofactor II requires ligation of both exosites 1 and 2 because minimal protection is seen when exosite 1 variants (gamma-thrombin and thrombin Quick 1) or an exosite 2 variant (Arg93 --> Ala, Arg97 --> Ala, and Arg101 --> Ala thrombin) is substituted for thrombin.	Alanine	263-266	serpin family C member 1	Homo sapiens	30-42	
8026575-5	1994	We have measured the stability to denaturation of one of these non-inhibitor substrate mutants, antithrombin-Hamilton, which has an Ala-->Thr change at position P12 in strand s4A.	Alanine	132-135	serpin family C member 1	Homo sapiens	96-108	
9493570-1	1998	Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution.	Alanine	188-195	serpin family C member 1	Homo sapiens	55-67	
8026575-6	1994	We find that it undergoes the transformation to the more stable form which is observed for inhibitor serpins, from which we conclude that the Ala-->Thr change in antithrombin-Hamilton does not prevent insertion of s4A into beta-sheet A in the cleaved form.	Alanine	142-145	serpin family C member 1	Homo sapiens	165-177	
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.	Alanine	254-261	serpin family C member 1	Homo sapiens	4-20	
1604438-0	1992	A useful restriction analysis for the determination of human antithrombin III variants with mutations from Ala 382 to Ala 384.	Alanine	107-110	serpin family C member 1	Homo sapiens	61-77	
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.	Alanine	254-261	serpin family C member 1	Homo sapiens	4-20	
1604438-0	1992	A useful restriction analysis for the determination of human antithrombin III variants with mutations from Ala 382 to Ala 384.	Alanine	118-121	serpin family C member 1	Homo sapiens	61-77	
1911389-13	1991	The present results with antithrombin Glasgow II suggest that all the alanine residues at the base of the reactive site loop in positions P12-10 may be important for the formation of a stabilized inhibitor-thrombin complex.	Alanine	70-77	serpin family C member 1	Homo sapiens	25-37	
3305015-14	1987	The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin.	Alanine	54-57	serpin family C member 1	Homo sapiens	255-271	
3305015-14	1987	The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin.	Alanine	197-200	serpin family C member 1	Homo sapiens	255-271	
1690736-5	1990	By analyzing a CNBr fragment of the thrombin-antithrombin III complex that reacts with the antibody we localized the epitope for the antibody to a strongly hydrophobic residue 382-386 peptide segment, Ala-Ala-Ala-Ser-Thr, of the inhibitor, which is also contiguous with a hydrophobic amino acid Ala at its carboxyl terminus.	Alanine	201-204	serpin family C member 1	Homo sapiens	45-61	
3179438-9	1988	Codon 382 codes for alanine in the normal allele and for threonine in the antithrombin-III-Hamilton allele.	Alanine	20-27	serpin family C member 1	Homo sapiens	74-90	
3179438-11	1988	We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases.	Alanine	68-75	serpin family C member 1	Homo sapiens	79-95	
3179438-11	1988	We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases.	Alanine	68-75	serpin family C member 1	Homo sapiens	316-332	
24068708-7	2013	These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role.	Alanine	201-204	serpin family C member 1	Homo sapiens	34-46	
24068708-7	2013	These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role.	Alanine	201-204	serpin family C member 1	Homo sapiens	121-133