Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Michael N. Blackburn"'
Autor:
Nicole McGill, Karan Kapoor, Michael N. Blackburn, Jerome Baudry, Cynthia B. Peterson, Harold V. Meyers
Publikováno v:
Journal of Chemical Information and Modeling. 56:535-547
The risk of serious bleeding is a major liability of anticoagulant drugs that are active-site competitive inhibitors targeting the Factor Xa (FXa) prothrombin (PT) binding site. The present work identifies several new classes of small molecule antico
Publikováno v:
Journal of Biological Chemistry. 275:25402-25410
Plasminogen activator inhibitor-type 1 (PAI-1) is the primary inhibitor of endogenous plasminogen activators that generate plasmin in the vicinity of a thrombus to initiate thrombolysis, or in the pericellular region of cells to facilitate migration
Autor:
Inderjit K. Chhohan, Martin Hibbs, Michael N. Blackburn, Sherin S. Abdel-Meguid, Cheryl A. Janson, Xiayang Qiu
Publikováno v:
Biochemistry. 38:12296-12304
The crystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined at 2.7 A resolution. Several important loops in the active site either become disordered or adopt very different conformations compared to thei
Publikováno v:
Journal of Biological Chemistry. 271:14323-14332
Upon treatment with denaturing agents, vitronectin has been observed to exhibit conformational alterations which are similar to the structural changes detected when vitronectin binds the thrombin-antithrombin complex or associates with the terminal a
Autor:
Giora Z. Feuerstein, Barbara L. Storer, Richard E. Valocik, Paul F. Koster, Michael N. Blackburn, John R. Toomey
Publikováno v:
Thrombosis research. 100(1)
A humanized inhibitory anti-factor IX(a) antibody (SB 249417) has been compared to enoxaparin (Lovenox) in a rat model of arterial thrombosis. Pretreatment of rats with either SB 249417 (3.0 mg/kg, i. v.) or enoxaparin (30.0 mg/kg, i.v. or s.c.) resu
Autor:
Roland A. Newman, Daniel J. O'Shannessy, Raymond W. Sweet, Michael N. Blackburn, Michael Brigham-Burke, Ian Brooks, Walter F Stafford, Thomas M. Smith, Michael L. Doyle, Alemseged Truneh, Reff Mitchell E, Preston Hensley
Publikováno v:
Methods in Enzymology ISBN: 9780121822248
This chapter has described a bioenergetic analysis of the interaction of sCD4 with an IgG1 and two IgG4 derivatives of an anti-sCD4 MAb. The MAbs have identical VH and VL domains but differ markedly in their CH and CL domains, raising the question of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9af27f5ebe39ba56bc016b421ec3b05
https://doi.org/10.1016/s0076-6879(00)23368-5
https://doi.org/10.1016/s0076-6879(00)23368-5
Autor:
Giora Z. Feuerstein, William R. Church, Paul F. Koster, Arun Patel, Peter J. Bugelski, Andrew J. Nichols, Richard E. Valocik, John R. Toomey, Michael N. Blackburn, Audrey Baker
Publikováno v:
Arteriosclerosis, thrombosis, and vascular biology. 19(10)
Abstract —A murine antihuman factor IX monoclonal antibody (BC2) has been generated and evaluated for its capacity to prolong the activated partial thromboplastin time (aPTT) in vitro and ex vivo and to prevent arterial thrombosis in a rat model in
Autor:
John A. Feild, Michael L. Doyle, Po-Huang Liang, Sherin S. Abdel-Meguid, Susan M. Green, Kimberly A. Brun, Audrey E. Baker, Michael N. Blackburn, Kevin O'Donnell
Publikováno v:
Biochemistry. 37(17)
Human cytomegalovirus (CMV) is a member of the Herpesviridae family of viruses that also includes herpes simplex viruses (HSV-1 and HSV-2), varicella-zoster virus (VZV), human herpes virus-6, 7, and 8 (HHV-6, HHV-7, and HHV-8), and Epstein-Barr virus
Publikováno v:
Biochemistry. 36(31)
Factor Xa and thrombin (factor IIa) activate factor VIII (fVIII) by different proteolytic pathways. Thrombin cleaves fVIII at Arg372 between the A1 and A2 domains, at Arg740 between the A2 and B domains, and at Arg1689 between the B and A3 domains to
Publikováno v:
Recombinant Technology in Hemostasis and Thrombosis ISBN: 9781461366447
Antithrombin III is the major physiologic inhibitor of the activated serine proteases of the blood coagulation cascade1. Inactivation of the proteases occurs following cleavage of the Arg393-Ser394 peptide bond and formation of a stable complex betwe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd5caa5450b06435b85459eee2ff9d79
https://doi.org/10.1007/978-1-4615-3698-7_4
https://doi.org/10.1007/978-1-4615-3698-7_4