Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Madhu S. Bajaj"'
Autor:
Sathya-Moorthy Ponnuraj, Denis Evseenko, Rodney M. Camire, Harvey R. Herschman, Anne K. Zaiss, Yogesh Kumar, Kanagasabai Vadivel, Matthew W. Bunce, S. Paul Bajaj, Ling Wu, Madhu S. Bajaj
Publikováno v:
The Journal of biological chemistry, vol 289, iss 45
Tissue factor pathway inhibitor-2 (TFPI-2) is a homologue of TFPI-1 and contains three Kunitz-type domains and a basic C terminus region. The N-terminal domain of TFPI-2 is the only inhibitory domain, and it inhibits plasma kallikrein, factor XIa, an
Autor:
Kanagasabai, Vadivel, Yogesh, Kumar, Matthew W, Bunce, Rodney M, Camire, Madhu S, Bajaj, S Paul, Bajaj
Publikováno v:
International biology review. 1(1)
Factor V (FV) B-domain contains an acidic region (FV-AR2) and a basic region (FV-BR), which interact with each other and maintain FV in a procofactor form; removal of either region via deletion/proteolysis results in an active FVa molecule. Tissue fa
Autor:
S. Paul Bajaj, Sayeh Agah, Kanagasabai Vadivel, Madhu S. Bajaj, Kaillathe Padmanabhan, Duilio Cascio, Charles T. Esmon, Sriram Krishnaswamy, Amanda S. Messer
Publikováno v:
Journal of Molecular Biology. 425:1961-1981
Crystal structures of factor (F) VIIa/soluble tissue factor (TF), obtained under high Mg(2+) (50mM Mg(2+)/5mM Ca(2+)), have three of seven Ca(2+) sites in the γ-carboxyglutamic acid (Gla) domain replaced by Mg(2+) at positions 1, 4, and 7. We now re
Autor:
Sreejesh Shanker, S. Paul Bajaj, Gregory W. Lawson, Yogesh Kumar, Godwin I. Ogueli, Kanagasabai Vadivel, Madhu S. Bajaj, Amy E. Schmidt
Publikováno v:
Journal of Biological Chemistry. 286:4329-4340
Tissue factor pathway inhibitor-2 (TFPI-2) inhibits factor XIa, plasma kallikrein, and factor VIIa/tissue factor; accordingly, it has been proposed for use as an anticoagulant. Full-length TFPI-2 or its isolated first Kunitz domain (KD1) also inhibit
Publikováno v:
Journal of Biological Chemistry. 281:24873-24888
Factor VIIa (FVIIa) consists of a γ-carboxyglutamic acid (Gla) domain, two epidermal growth factor-like domains, and a protease domain. FVIIa binds seven Ca2+ ions in the Gla, one in the EGF1, and one in the protease domain. However, blood contains
Autor:
Madhu S. Bajaj, Kanagasabai Vadivel, S. Paul Bajaj, Yogesh Kumar, Joseph A. Loo, Amy E. Schmidt, Sathya M. Ponnuraj, Nalaka Rannulu, Godwin I. Ogueli
Publikováno v:
Biochemistry
Kunitz domain 1 (KD1) of tissue factor pathway inhibitor-2 in which P2′ residue Leu17 (bovine pancreatic trypsin inhibitor numbering) is mutated to Arg selectively inhibits the active site of plasmin with ∼5-fold improved affinity. Thrombin cleav
Publikováno v:
Thrombosis and Haemostasis. 86:959-972
SummaryHuman tissue factor pathway inhibitor (TFPI) is a modular protein comprised of three Kunitz type domains flanked by peptide segments that are less structured. The sequential order of the elements are: an N-terminal acidic region followed by th
Publikováno v:
Thrombosis and Haemostasis. 82:1663-1672
SummaryTissue factor pathway inhibitor (TFPI) plays an important role in regulating tissue factor (TF)-initiated blood coagulation. Since serum stimulation of fibroblasts, vascular smooth muscle cells and cardiac myocytes in culture increases the exp
Publikováno v:
Thrombosis and Haemostasis. 82:1047-1052
SummaryUnder normal physiologic conditions, tissue factor pathway inhibitor (TFPI) is synthesized primarily by the microvascular endothelium. Using Northern blotting, we studied its transcriptional expression in different organs and compared it with
Autor:
Bajaj Sp, Madhu S. Bajaj
Publikováno v:
Thrombosis and Haemostasis. 78:471-477
Tissue factor pathway of coagulation plays a dominant role during normal haemostasis. Tissue factor pathway inhibitor (TFPI), expressed primarily by the microvascular endothelium, appears to be the major physiologic inhibitor of TF-induced coagulatio