Zobrazeno 1 - 10
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pro vyhledávání: '"Mark PEEK"'
Publikováno v:
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Computing/infrastructure as a service continues to evolve with bare metal, virtual machines, containers and now serverless granular computing service offerings. Granular computing enables developers to decompose their applications into smaller logica
Publikováno v:
FEBS Letters. 579:1945-1950
Hepsin, a type II transmembrane serine protease, is highly upregulated in prostate cancer and promotes tumor progression and metastasis. We generated a soluble form of hepsin comprising the entire extracellular domain to show that it efficiently conv
Autor:
Charles Eigenbrot, Jihong Yang, Robert F. Kelley, Paul Moran, Michael T. Lipari, Daniel Kirchhofer, Mark Peek
Publikováno v:
Biochemistry. 43:1223-1229
Tissue factor (TF) binds the zymogen (VII) and activated (VIIa) forms of coagulation factor VII with high affinity. The structure determined for the sTF-VIIa complex [Banner, D. W., et al. (1996) Nature 380, 41-46] shows that all four domains of VIIa
Autor:
Paul Moran, Mark Peek, Racquel Corpuz, Charles Eigenbrot, Daniel Kirchhofer, Wei Li, Robert A. Lazarus, Jennifer Stamos, Saloumeh Kadkhodayan, J. Michael Elliott
Publikováno v:
Journal of Biological Chemistry. 278:36341-36349
Hepatocyte growth factor activator inhibitor-1 (HAI-1) is an integral membrane protein expressed on epithelial cells and contains two extracellular Kunitz domains (N-terminal KD1 and C-terminal KD2) known to inhibit trypsin-like serine proteases. In
Publikováno v:
Biochemical Journal. 363:387-393
Highly potent bifunctional inhibitors of Factor VIIa (FVIIa) were generated by linking two distinct peptides, recently shown to bind to two discrete exosites on the FVIIa protease domain [Dennis, Eigenbrot, Skelton, Ultsch, Santell, Dwyer, O'Connell
Autor:
Paul Moran, Michael T. Lipari, Robert F. Kelley, Charles Eigenbrot, Daniel Kirchhofer, Mark Peek
Publikováno v:
Biochemistry. 40:675-682
Tissue factor is the cell membrane-anchored cofactor for factor VIIa and triggers the coagulation reactions. The initial step is the conversion of factor VII to factor VIIa which, in vitro, is efficiently catalyzed by low concentrations of factor Xa.
Autor:
Louis Burcklen, Canio J. Refino, Daniel Kirchhofer, Mark Peek, Jacques Himber, Shelley Suggett, Brigitte Devaux, Paul Moran
Publikováno v:
Thrombosis and Haemostasis. 82:1188-1195
Summary10C12, a human antibody F(ab’)2, which specifically binds to the Gla domain of factor IX, interfered with all known coagulation processes that involve factor IX/IXa. These include the function of the intrinsic Xase complex and the activation
Autor:
Lydia Santell, Mark Peek, Michael T. Lipari, Robert A. Lazarus, Paul Moran, Xiaoyi Yao, Karen Billeci, Daniel Kirchhofer, Henry R. Maun, Charles Eigenbrot, Christian Wiesmann
Publikováno v:
The Journal of biological chemistry. 279(38)
Hepatocyte growth factor (HGF), a plasminogen-related growth factor, is the ligand for Met, a receptor tyrosine kinase implicated in development, tissue regeneration, and invasive tumor growth. HGF acquires signaling activity only upon proteolytic cl
Publikováno v:
The Journal of biological chemistry. 277(49)
Hepatocyte growth factor (HGF), the ligand for the receptor tyrosine kinase c-Met, is composed of an alpha-chain containing four Kringle domains (K1-K4) and a serine protease domain-like beta-chain. Receptor activation by HGF is contingent upon prior
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