Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Elliott Schiffmann"'
Publikováno v:
Journal of Lipid Research, Vol 2, Iss 3, Pp 258-262 (1961)
Three analogues of mevalonic acid have been found to inhibit cholesterol biosynthesis in liver homogenates in the following order of efficacy: 3-methyl-3-hydroxy pentanoic acid > Δ2-3-methyl pentenoic acid > Δ3-3-methyl pentenoic acid. The hydroxy
Externí odkaz:
https://doaj.org/article/f4d583ab8e634c97816c41904c3853ed
Autor:
Elise C. Kohn, Gambrill H. Hollister, Lance A. Liotta, Elliott Schiffmann, Sharon Wahl, John D. Dipersio
Publikováno v:
International Journal of Cancer. 53:968-972
Tumor metastasis is the primary cause of death for cancer patients. The metastatic cascade requires successful tumor cell invasion into and through vascular and parenchymal barriers. We have shown that autocrine motility factor (AMF, autotaxin) and t
Autor:
Raejean Hermansen, Eunjin Koh, David D. Roberts, Mary L. Stracke, Elliott Schiffmann, Russell W. Bandle, Timothy Clair
Publikováno v:
Cellular Signalling. 19:1328-1338
Lysophosphatidic acid (LPA) stimulates sphingosine-1-phosphate (S1P)-sensitive motility in NIH3T3 clone7 cells. S1P inhibits motility only when added to the bottom well of the Boyden chamber, suggesting that pseudopodia can respond to their microenvi
Publikováno v:
Cell Motility and the Cytoskeleton. 46:279-284
Secreted motility-stimulating factors are often expressed and secreted at low concentrations that are difficult to detect by Northern or Western blot analysis. Autotaxin (ATX) is a tumor-secreted autocrine motility-stimulating factor that has been as
Autor:
Suk Woo Nam, Elisa C. Woodhouse, Lance A. Liotta, Peter T. Mulvaney, Rima Khaddurah-Daouk, Timothy Clair, Margaret O'Keefe, Mary L. Stracke, Elliott Schiffmann
Publikováno v:
International Journal of Cancer. 78:46-52
Cyclocreatine (1-carboxymethyl-2-iminoimidazolidine), an analog of creatine and a substrate for creatine kinase (EC 2.7.3.2), inhibits the stimulated motility of tumor cells which possess creatine kinase. A2058-055 human melanoma cells, transfected w
Publikováno v:
Kidney International. 43(1):151-157
Cytoskeletal agents inhibit motility and adherence of human tumor cells. Cytoskeletal agents have been demonstrated to inhibit stimulated motility and substrate adherence by the human tumor cell line, A2058. cis -tubulozole, taxol, and cytochalasin D
Autor:
Vittoria Cioce, Henry C. Krutzsch, Mary L. Stracke, Edward J. Unsworth, Elliott Schiffmann, A Arestad, Lance A. Liotta
Publikováno v:
Journal of Biological Chemistry. 267:2524-2529
Autotaxin (ATX) is a potent human motility-stimulating protein that has been identified in the conditioned medium from A2058 melanoma cells. This protein has been purified to homogeneity utilizing a strategy involving five column steps. Homogeneity o
Publikováno v:
The Journal of Cell Biology
Transduction of signals initiating motility by extracellular matrix (ECM) molecules differed depending on the type of matrix molecule and whether the ligand was in solution or bound to a substratum. Laminin, fibronectin, and type IV collagen stimulat
L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine, autotaxin
Autor:
Russell W. Bandle, Eunjin Koh, Mary L. Stracke, Lance A. Liotta, Malgorzata M. Ptaszynska, Timothy Clair, Elliott Schiffmann
Publikováno v:
Lipids in Health and Disease, Vol 4, Iss 1, p 5 (2005)
Lipids in Health and Disease
Lipids in Health and Disease
Background Autotaxin (ATX, NPP-2), originally purified as a potent tumor cell motility factor, is now known to be the long-sought plasma lysophospholipase D (LPLD). The integrity of the enzymatic active site, including three crucial histidine moietie
Autor:
Timothy, Clair, Junken, Aoki, Eunjin, Koh, Russell W, Bandle, Suk Woo, Nam, Malgorzata M, Ptaszynska, Gordon B, Mills, Elliott, Schiffmann, Lance A, Liotta, Mary L, Stracke
Publikováno v:
Cancer research. 63(17)
Autotaxin (ATX) is an exoenzyme that potently induces tumor cell motility, and enhances experimental metastasis and angiogenesis. ATX was shown recently to be identical to serum lysophospholipase D activity, producing lysophosphatidic acid (LPA) from