Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Jacqueline E. Damen"'
Autor:
Vincent Duronio, Michael Huber, Jacqueline E. Damen, Paul O. Neilsen, Veronica H. Kang, Michael R. Hughes, Gerald Krystal, Michael P. Scheid, Glenn D. Prestwich
Publikováno v:
Journal of Biological Chemistry. 277:9027-9035
Using bone marrow derived mast cells from SH2-containing inositol-5-phosphatase (SHIP) +/+ and −/− mice, we found that the loss of SHIP leads to a dramatic increase in Steel Factor (SF)-stimulated phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,
Autor:
Suzanne M. Chappel, Jacqueline E. Damen, Christian P. Kalberer, Gerald Krystal, R. Keith Humphries, Nicolas Pineault, Cheryl D. Helgason
Publikováno v:
The Journal of Experimental Medicine
In this report, we demonstrate that the Src homology 2 domain–containing inositol-5-phosphatase (SHIP) plays a critical role in regulating both B cell development and responsiveness to antigen stimulation. SHIP−/− mice exhibit a transplantable
Autor:
Gerald Krystal, Jacqueline E Damen, Cheryl D Helgason, Michael Huber, Michael R Hughes, Janet Kalesnikoff, Vivian Lam, Patty Rosten, Mark D Ware, Sandie Yew, R.Keith Humphries
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 31:1007-1010
In 1996 three groups independently cloned a hemopoietic specific, src homology 2-containing inositol 5'-phosphatase which, based on its structure, was called SHIP. More recently, a second more widely expressed SHIP-like protein has been cloned and ca
Autor:
Cheryl D. Helgason, Ling Liu, Michael Huber, Mark D. Ware, Vincent Duronio, Gerald Krystal, Michael P. Scheid, Jacqueline E. Damen, R. Keith Humphries
Publikováno v:
Progress in Biophysics and Molecular Biology. 71:423-434
The recently cloned, hemopoietic-specific, src homology 2 (SH2)-containing inositol phosphatase, SHIP, is rapidly gaining prominence as a potential regulator of all phosphatidylinositol (PI)-3 kinase mediated events since it has been shown both in vi
Autor:
Cheryl D. Helgason, Michael Huber, Jacqueline E. Damen, R. Keith Humphries, Gerald Krystal, Ling Liu
Publikováno v:
Proceedings of the National Academy of Sciences. 95:11330-11335
To clarify the role that the src homology 2-containing inositol phosphatase (SHIP) plays in mast cell degranulation, the gene for SHIP was disrupted by homologous recombination in embryonic stem cells. Bone-marrow-derived mast cells from SHIP+/+, +/
Autor:
Jacqueline E. Damen, Ling Liu, Mark D. Ware, Marina Ermolaeva, Philip W. Majerus, Gerald Krystal
Publikováno v:
Blood. 92:1199-1205
The SH2-containing inositol phosphatase, SHIP, often appears as multiple bands in anti-SHIP immunoblots. To characterize these bands, antisera were generated against the N-terminal (anti-N), mid-region (anti-M), and C-terminal (anti-C) portions of SH
Autor:
Jacqueline E. Damen, Gerald Krystal, Philip W. Majerus, Mark D. Ware, Marina Ermolaeva, Ling Liu
Publikováno v:
Blood. 92:1199-1205
The SH2-containing inositol phosphatase, SHIP, often appears as multiple bands in anti-SHIP immunoblots. To characterize these bands, antisera were generated against the N-terminal (anti-N), mid-region (anti-M), and C-terminal (anti-C) portions of SH
Autor:
Rewa Grewal, R. Keith Humphries, Gerald Krystal, Cheryl D. Helgason, Frank R. Jirik, Anita Borowski, Poul H. Sorensen, Patty Rosten, Jacqueline E. Damen, Suzanne M. Chappel
Publikováno v:
Genes & Development. 12:1610-1620
SHIP is a 145-kDSH2-containinginositol-5-phosphatase widely expressed in hemopoietic cells. It was first identified as a tyrosine phosphoprotein associated with Shc in response to numerous cytokines. SHIP has been implicated in FcγRIIB receptor-medi
Autor:
Jacqueline E. Damen, Véronique Maguer-Satta, Allen C. Eaves, Ling Liu, S Burl, H Chahine, Connie J. Eaves, Gerald Krystal
Publikováno v:
Oncogene. 16:237-248
In patients with chronic myeloid leukemia (CML), the neoplastic (BCR-ABL+) progenitor cells are characterized by an increased proliferative activity. Whether these cells are also resistant to apoptosis and if so, under what conditions remains controv
Publikováno v:
Biochemical and Biophysical Research Communications. 234:198-205
Erythropoietin (EPO) and its cell surface receptor (EPOR) play central roles in the proliferation and differentiation of mammalian erythroid progenitor cells. Recently both the tyrosine residues in the EPOR responsible for the activation of Stat5 and