PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8679610-8 1996 To test this hypothesis, we have characterized a P14 serine --> tryptophan antithrombin variant. Tryptophan 67-77 serpin family C member 1 Homo sapiens 78-90 8679610-9 1996 From changes in tryptophan fluorescence upon heparin binding, increased affinity for heparin, and partial activation of the variant against factor Xa, we conclude that the proposed mechanism of heparin activation is correct with respect to loop expulsion and that it may consequently be possible to create more highly activated antithrombin variants through suitable hinge region substitutions. Tryptophan 16-26 serpin family C member 1 Homo sapiens 328-340 1412223-7 1992 These findings, together with our previous report upon tryptophan modification of antithrombin III [1] suggest that the nature of the molecule is such that considerable care must be taken in interpretation of results when investigating the structure/function relationships of this protein by chemical modification. Tryptophan 55-65 serpin family C member 1 Homo sapiens 82-98 2019613-2 1991 The conformational change of antithrombin III was investigated in terms of the intrinsic fluorescence of tryptophan residue, the extrinsic fluorescence using 1,6-diphenyl-1,3,5-hexatriene as fluorescent probe, and Fourier-transform infrared spectroscopy. Tryptophan 105-115 serpin family C member 1 Homo sapiens 29-45 2057915-0 1991 Influence of tryptophan modification upon digestion of antithrombin III by elastase. Tryptophan 13-23 serpin family C member 1 Homo sapiens 55-71 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Tryptophan 25-35 serpin family C member 1 Homo sapiens 48-64 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. Tryptophan 121-124 serpin family C member 1 Homo sapiens 43-59 2315891-0 1990 Influence of chemical modification of tryptophan residues on the properties of human antithrombin III. Tryptophan 38-48 serpin family C member 1 Homo sapiens 85-101 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. Tryptophan 72-82 serpin family C member 1 Homo sapiens 95-111 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. Tryptophan 72-82 serpin family C member 1 Homo sapiens 306-322 2315891-5 1990 A recovery of heparin cofactor activity towards coagulation factor Xa was observed upon prolonged storage of low affinity forms at -70 degrees C. It is considered that the loss of high affinity for heparin upon modification of antithrombin III arises from change or stabilization of conformation associated with tryptophan modification and is not a singular property of modification of Trp 49. Tryptophan 312-322 serpin family C member 1 Homo sapiens 227-243 2315891-5 1990 A recovery of heparin cofactor activity towards coagulation factor Xa was observed upon prolonged storage of low affinity forms at -70 degrees C. It is considered that the loss of high affinity for heparin upon modification of antithrombin III arises from change or stabilization of conformation associated with tryptophan modification and is not a singular property of modification of Trp 49. Tryptophan 386-389 serpin family C member 1 Homo sapiens 227-243 3743657-2 1986 Only 15% of the biologic activity of the complex carbohydrates derived from human skin fibroblasts was expressed when the heparin-binding domain an antithrombin was chemically modified at the Trp 49 residue. Tryptophan 192-195 serpin family C member 1 Homo sapiens 148-160 3584126-7 1987 The hydroxy-nitrobenzyl (HNB) group attached to a unique tryptophan has been used in the present study as an extrinsic probe for localization of conformational changes to the heparin-binding region within antithrombin III using immunochemical and spectral techniques. Tryptophan 57-67 serpin family C member 1 Homo sapiens 205-221 3584126-8 1987 Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol. Tryptophan 30-40 serpin family C member 1 Homo sapiens 47-59 3584126-11 1987 Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin. Tryptophan 73-83 serpin family C member 1 Homo sapiens 90-102 3584126-11 1987 Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin. Tryptophan 73-83 serpin family C member 1 Homo sapiens 218-230 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. Tryptophan 56-59 serpin family C member 1 Homo sapiens 144-160 6693405-2 1984 Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol. Tryptophan 34-44 serpin family C member 1 Homo sapiens 56-72 6486808-0 1984 The role of tryptophan residues in heparin-antithrombin interactions. Tryptophan 12-22 serpin family C member 1 Homo sapiens 43-55 6486808-1 1984 A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide. Tryptophan 9-19 serpin family C member 1 Homo sapiens 31-43 6486808-3 1984 Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor. Tryptophan 207-217 serpin family C member 1 Homo sapiens 17-29 6486808-4 1984 Fluorescence quenching experiments indicated that the modifiable tryptophan groups of antithrombin were exposed to the solvent environment. Tryptophan 65-75 serpin family C member 1 Homo sapiens 86-98 6643466-11 1983 However, the tryptophan-ascribed fluorescence enhancement and absorption difference spectrum which occur when heparin binds to antithrombin III are reduced by 70%. Tryptophan 13-23 serpin family C member 1 Homo sapiens 127-143 6420409-10 1984 Fluorescence emission spectra of the phosphopyridoxyl-antithrombin derivative that does not bind to heparin-agarose indicated fluorescence energy transfer from tryptophan to the bound phosphopyridoxyl moiety. Tryptophan 160-170 serpin family C member 1 Homo sapiens 54-66 6693405-8 1984 The site of labeling corresponds to Trp 49, which is located within the disulfide-stabilized loops near the NH2-terminal end of the antithrombin III molecule. Tryptophan 36-39 serpin family C member 1 Homo sapiens 132-148 710412-5 1978 The binding of either fraction to antithrombin was found to result in an increase of the tryptophan fluorescence of the protein. Tryptophan 89-99 serpin family C member 1 Homo sapiens 34-46 7406509-0 1980 Tryptophan residue at the heparin binding site in antithrombin III. Tryptophan 0-10 serpin family C member 1 Homo sapiens 50-66 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. Tryptophan 89-99 serpin family C member 1 Homo sapiens 25-41 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. Tryptophan 89-99 serpin family C member 1 Homo sapiens 238-254 7356660-8 1980 These results indicate that the integrity of a specific tryptophan residue is critical to the binding of heparin to antithrombin III. Tryptophan 56-66 serpin family C member 1 Homo sapiens 116-132 656463-0 1978 The increase in human antithrombin III tryptophan fluorescence produced by heparin. Tryptophan 39-49 serpin family C member 1 Homo sapiens 22-38 32194638-10 2020 This novel mutation resulted in a substitution of arginine by tryptophan, leading to antithrombin resistance (ATR). Tryptophan 62-72 serpin family C member 1 Homo sapiens 85-97 24016-0 1977 Quenching of tryptophan fluorescence in human antithrombin III by iodide ion. Tryptophan 13-23 serpin family C member 1 Homo sapiens 46-62 24016-1 1977 Iodide is an efficient quencher of antithrombin III intrinsic tryptophan fluorescence. Tryptophan 62-72 serpin family C member 1 Homo sapiens 35-51 24016-4 1977 The binding of heparin to antithrombin III influences the number of solvent-exposed tryptophan residues. Tryptophan 84-94 serpin family C member 1 Homo sapiens 26-42 65182-0 1977 Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence. Tryptophan 75-85 serpin family C member 1 Homo sapiens 28-44 18375953-9 2008 The prelatent form was conformationally altered from native antithrombin as judged from an attenuation of tryptophan fluorescence changes following heparin activation and a reduced thermal stability. Tryptophan 106-116 serpin family C member 1 Homo sapiens 60-72 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Tryptophan 255-265 serpin family C member 1 Homo sapiens 0-12 16128566-0 2005 Importance of tryptophan 49 of antithrombin in heparin binding and conformational activation. Tryptophan 14-24 serpin family C member 1 Homo sapiens 31-43 16128566-1 2005 Tryptophan 49 of antithrombin, the primary inhibitor of blood clotting proteinases, has previously been implicated in binding the allosteric activator, heparin, by chemical modification and mutagenesis studies. Tryptophan 0-10 serpin family C member 1 Homo sapiens 17-29 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)). Tryptophan 44-54 serpin family C member 1 Homo sapiens 120-132 9722560-2 1998 We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans. Tryptophan 61-64 serpin family C member 1 Homo sapiens 29-41 9722560-2 1998 We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans. Tryptophan 175-186 serpin family C member 1 Homo sapiens 29-41 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 79-82 serpin family C member 1 Homo sapiens 44-56 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 95-98 serpin family C member 1 Homo sapiens 44-56 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 95-98 serpin family C member 1 Homo sapiens 44-56 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 95-98 serpin family C member 1 Homo sapiens 44-56 9722560-5 1998 Trp-49 and Trp-225 underwent spectral shifts of 15 nm to blue and 5 nm to red, respectively, in the antithrombin-heparin complex. Tryptophan 0-3 serpin family C member 1 Homo sapiens 100-112 9722560-5 1998 Trp-49 and Trp-225 underwent spectral shifts of 15 nm to blue and 5 nm to red, respectively, in the antithrombin-heparin complex. Tryptophan 11-14 serpin family C member 1 Homo sapiens 100-112 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Tryptophan 56-67 serpin family C member 1 Homo sapiens 81-93 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Tryptophan 155-158 serpin family C member 1 Homo sapiens 81-93 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Tryptophan 167-170 serpin family C member 1 Homo sapiens 81-93