Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Mark D Ware"'
Publikováno v:
Human Mutation. 27:1024-1029
The 185delAG mutation (c.68_69delAG; ter39) in the BRCA1 gene is a founder Jewish Ashkenazi mutation that is carried by 1% of this population and has been identified in thousands of breast or ovarian cancer patients. We have previously described that
Autor:
Mark D. Ware, D DeSilva, Olga M. Sinilnikova, Dominique Stoppa-Lyonnet, Sean V. Tavtigian, Sylvie Mazoyer
Publikováno v:
Oncogene. 25:323-328
BRCA2 (BReast CAncer susceptibility gene 2) germline mutation carriers are at increased risk for breast and ovarian cancers. Mutations occurring in the ovarian cancer cluster region (OCCR) are linked to higher ovarian cancer and/or lower breast cance
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:
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
Publikováno v:
Journal of Biological Chemistry. 272:10998-11001
We recently purified and cloned a 145-kDa protein that becomes tyrosine phosphorylated and associated with Shc in response to multiple cytokines. Based on its predicated amino acid sequence and its enzymatic activity, we have called this protein SHIP
Autor:
Olga Anczuków, Olga M. Sinilnikova, Monique Buisson, Almoutassem B. Zetoune, Sylvie Mazoyer, Mark D. Ware, Dominique Stoppa-Lyonnet
Publikováno v:
Human mutation. 29(1)
The nonsense-mediated mRNA decay (NMD) mechanism is an evolutionarily conserved process ensuring the degradation of transcripts carrying premature termination codon(s). NMD is believed to prevent the synthesis of truncated proteins that could be detr
Publikováno v:
Blood. 97(5)
The SH2-containing inositol-5'-phosphatase, SHIP, restrains bone marrow-derived mast cell (BMMC) degranulation, at least in part, by hydrolyzing phosphatidylinositol (PI)-3-kinase generated PI-3,4,5-P(3) (PIP3) to PI-3,4-P(2). To determine which doma
Publikováno v:
Experimental Hematology. 28:84-85
We recently reported that the src homology 2 (SH2)-containing inositol 5-phosphatase, SHIP, acts as a gatekeeper of bone marrow derived mast cell (BMMC) degranulation by preventing inappropriate and excess release of inflammatory mediators (PNAS 95,