| Year |
Citation |
Score |
| 2015 |
Roth R, Swanson R, Izaguirre G, Bock SC, Gettins PG, Olson ST. Saturation mutagenesis of the antithrombin reactive center loop P14 residue supports a 3-step mechanism of heparin allosteric activation involving intermediate and fully-activated states. The Journal of Biological Chemistry. PMID 26359493 DOI: 10.1074/Jbc.M115.678839 |
0.477 |
|
| 2009 |
Boucher L, de la Cruz R, Bock S, Wintrode PL. Conformational Dynamics of Antithrombin III With its Allosteric Activator Heparin Biophysical Journal. 96: 69a. DOI: 10.1016/J.Bpj.2008.12.258 |
0.64 |
|
| 2004 |
Schedin-Weiss S, Desai UR, Bock SC, Olson ST, Björk I. Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change. Biochemistry. 43: 675-83. PMID 14730971 DOI: 10.1021/Bi030173B |
0.5 |
|
| 2003 |
Jairajpuri MA, Lu A, Desai U, Olson ST, Bjork I, Bock SC. Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation. The Journal of Biological Chemistry. 278: 15941-50. PMID 12556442 DOI: 10.1074/Jbc.M212319200 |
0.461 |
|
| 2002 |
Schedin-Weiss S, Arocas V, Bock SC, Olson ST, Björk I. Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding. Biochemistry. 41: 12369-76. PMID 12369826 |
0.441 |
|
| 2002 |
Olson ST, Björk I, Bock SC. Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants. Trends in Cardiovascular Medicine. 12: 198-205. PMID 12161073 |
0.479 |
|
| 2002 |
Jairajpuri MA, Lu A, Bock SC. Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition. The Journal of Biological Chemistry. 277: 24460-5. PMID 11971909 DOI: 10.1074/jbc.M203127200 |
0.421 |
|
| 2002 |
Schedin-Weiss S, Desai UR, Bock SC, Gettins PG, Olson ST, Björk I. Importance of lysine 125 for heparin binding and activation of antithrombin. Biochemistry. 41: 4779-88. PMID 11939772 DOI: 10.1021/Bi012163L |
0.501 |
|
| 2001 |
Arocas V, Bock SC, Raja S, Olson ST, Bjork I. Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding. The Journal of Biological Chemistry. 276: 43809-17. PMID 11567021 DOI: 10.1074/jbc.M105294200 |
0.538 |
|
| 2001 |
Chuang YJ, Swanson R, Raja SM, Bock SC, Olson ST. The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activation. Biochemistry. 40: 6670-9. PMID 11380262 DOI: 10.1021/bi002933d |
0.389 |
|
| 2000 |
Arocas V, Turk B, Bock SC, Olson ST, Björk I. The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139. Biochemistry. 39: 8512-8. PMID 10913257 DOI: 10.1021/bi9928243 |
0.46 |
|
| 2000 |
Desai U, Swanson R, Bock SC, Bjork I, Olson ST. Role of arginine 129 in heparin binding and activation of antithrombin. The Journal of Biological Chemistry. 275: 18976-84. PMID 10764763 DOI: 10.1074/Jbc.M001340200 |
0.542 |
|
| 1999 |
Arocas V, Bock SC, Olson ST, Björk I. The role of Arg46 and Arg47 of antithrombin in heparin binding. Biochemistry. 38: 10196-204. PMID 10433728 DOI: 10.1021/bi990686b |
0.486 |
|
| 1997 |
Ersdal-Badju E, Lu A, Zuo Y, Picard V, Bock SC. Identification of the antithrombin III heparin binding site. The Journal of Biological Chemistry. 272: 19393-400. PMID 9235938 DOI: 10.1074/jbc.272.31.19393 |
0.552 |
|
| 1997 |
Turk B, Brieditis I, Bock SC, Olson ST, Björk I. The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Biochemistry. 36: 6682-91. PMID 9184148 DOI: 10.1021/bi9702492 |
0.431 |
|
| 1995 |
Ersdal-Badju E, Lu A, Peng X, Picard V, Zendehrouh P, Turk B, Björk I, Olson ST, Bock SC. Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells. The Biochemical Journal. 323-30. PMID 7646463 DOI: 10.1042/bj3100323 |
0.377 |
|
| 1993 |
Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, Abildgaard U, Ireland H, Thompson E, Sas G. Pleiotropic effects of antithrombin strand 1C substitution mutations. The Journal of Clinical Investigation. 90: 2422-33. PMID 1469094 DOI: 10.1172/JCI116133 |
0.409 |
|
| 1992 |
Olds RJ, Lane DA, Boisclair M, Sas G, Bock SC, Thein SL. Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F. Febs Letters. 300: 241-6. PMID 1555650 DOI: 10.1016/0014-5793(92)80854-A |
0.411 |
|
| 1986 |
Ghosh SS, Bock SC, Rokita SE, Kaiser ET. Modification of the active site of alkaline phosphatase by site-directed mutagenesis. Science (New York, N.Y.). 231: 145-8. PMID 3510454 DOI: 10.1126/Science.3510454 |
0.381 |
|
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