Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Harlan N. Bradford"'
Publikováno v:
Journal of Biological Chemistry. 294:2422-2435
The proteolytic conversion of factor V to factor Va is central for amplified flux through the blood coagulation cascade. Heterodimeric factor Va is produced by cleavage at three sites in the middle of factor V by thrombin, yielding an N terminus–de
Publikováno v:
Blood. 132:24-24
Anticoagulation requires a careful balance to achieve antithrombotic efficacy without disrupting normal hemostasis. Although current generation direct oral anticoagulants (DOACs) offer advantages over traditional warfarin or heparin therapy they stil
Membrane Binding by Prothrombin Mediates Its Constrained Presentation to Prothrombinase for Cleavage
Publikováno v:
Journal of Biological Chemistry. 288:27789-27800
Long-standing dogma proposes a profound contribution of membrane binding by prothrombin in determining the rate at which it is converted to thrombin by prothrombinase. We have examined the action of prothrombinase on full-length prothrombin variants
Thrombin is produced from the C-terminal half of prothrombin following its proteolytic activation. The N-terminal half, released as the propiece Fragment 12 (F12), is composed of an N-terminal γ-carboxyglutamate domain (Gla) followed by two kringles
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f74c716eac8bb8cff661fb6bc60264d
https://europepmc.org/articles/PMC4900261/
https://europepmc.org/articles/PMC4900261/
Publikováno v:
Journal of Biological Chemistry. 287:30414-30425
Thrombin is produced by the ordered action of prothrombinase on two cleavage sites in prothrombin. Meizothrombin, a proteinase precursor of thrombin, is a singly cleaved species that accumulates abundantly as an intermediate. We now show that covalen
Publikováno v:
Journal of Biological Chemistry. 285:328-338
Prothrombinase converts prothrombin to thrombin via cleavage at Arg320 followed by cleavage at Arg271. Exosite-dependent binding of prothrombin to prothrombinase facilitates active site docking by Arg320 and initial cleavage at this site. Precise pos
Autor:
Harlan N. Bradford, Vaibhav Katkade, John P. Gaughan, Irma Isordia-Salas, Tracee S. Panetti, Abigail A. Soyombo, Robert W. Colman
Publikováno v:
Thrombosis and Haemostasis. 94:606-614
SummaryDomain 5 (D5) of cleaved high molecular weight kininogen (HKa) inhibits angiogenesis in vivo and endothelial cell migration in vitro, but the cell signaling pathways involved in HKa and D5 inhibition of endothelial cell migration are incomplet
Autor:
Irma M. Sainz, Yan-Lin Guo, Harlan N. Bradford, E. Premkumar Reddy, James S. Song, Abdel Bior, Stephen C. Cosenza, Irma Isordia-Salas, Robert W. Colman, Robin A. Pixley
Publikováno v:
Blood. 104:2065-2072
We have shown that human high molecular weight kininogen is proangiogenic due to release of bradykinin. We now determined the ability of a murine monoclonal antibody to the light chain of high molecular weight kininogen, C11C1, to inhibit tumor growt
Autor:
Harlan N. Bradford, Raul A. Dela Cadena, Satya P. Kunapuli, Jing-Fei Dong, José A. López, Robert W. Colman
Publikováno v:
Blood. 90:1508-1515
We and others have shown that both high and low molecular mass kininogens are able to inhibit the thrombin-induced aggregation of gel-filtered platelets, indicating that the locus for inhibition resides in the heavy chain. The inhibitory site is pres
Autor:
Robert W. Colman, Harlan N. Bradford, Raul A. DeLa Cadena, Jing Fei Dong, José A. López, Satya P. Kunapuli
Publikováno v:
Blood. 90:1508-1515
We and others have shown that both high and low molecular mass kininogens are able to inhibit the thrombin-induced aggregation of gel-filtered platelets, indicating that the locus for inhibition resides in the heavy chain. The inhibitory site is pres