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pro vyhledávání: '"F. Jirik"'
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Publikováno v:
Biochemical and Biophysical Research Communications. 200:577-583
4-Difluoromethylphenyl bis(cyclohexylammonium) phosphate was synthesized in 4 steps starting from dibenzyl phosphite and shown to be a time-dependent suicide inactivator of human prostatic acid phosphatase and the SHP protein tyrosine phosphatase. Th
Publikováno v:
The Journal of Immunology. 152:455-466
We previously developed a transgenic (Tg) murine lineage (B10.S-Tg31e), which secretes the hepatitis B e Ag (HBeAg) into the serum at a concentration of 10 ng/ml. This serum concentration was sufficient to render B10.S-Tg31e mice functionally toleran
Publikováno v:
The Journal of Immunology. 151:5699-5703
We previously reported that a chimeric protein consisting of the human p55 TNF receptor covalently linked to a murine IgG1 Fc heavy chain acts as an efficient TNF inhibitor, as a result of its high binding affinity for native TNF trimers of both muri
Publikováno v:
The Journal of biological chemistry. 272(22)
The cytoplasmic tyrosine phosphatases, SHP1 and SHP2, are implicated in the control of cellular proliferation and survival. Here we demonstrate that both SHP1 and SHP2 associate with the betac subunit of the human interleukin-3 (IL-3) receptor follow
Publikováno v:
Protein science : a publication of the Protein Society. 4(1)
We describe a simple, fast, sensitive, and nonisotopic bioanalytical technique for the detection of tyrosine-phosphorylated peptides and the determination of sites of protein tyrosine phosphorylation. The technique employs a protein tyrosine phosphat
Publikováno v:
The Journal of biological chemistry. 269(38)
Binding of interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor (GM-CSF) to their high affinity cell surface receptors induces tyrosine phosphorylation of a similar set of protein substrates. We have identified one of these common
Publikováno v:
The Journal of biological chemistry. 269(8)
The src homology 2 (SH2) domain containing protein-tyrosine-phosphatase SH-PTP2, was over-expressed in Escherichia coli for a kinetic study employing a set of synthetic 13- to 14-mer phosphopeptide substrates. The full-length SH-PTP2 protein, as well
Autor:
T. Pawson, E. H. Fischer, Benjamin G. Neel, Z. Zhao, Kohzoh Imai, James N. Ihle, Matthew L. Thomas, Masaaki Adachi, S.-H. Shen, F. Jirik, A. Ullrich
Publikováno v:
Cell. 85:15
Publikováno v:
The Journal of Immunology. 134:3281-3285
Genetic studies of human immunoglobulin variable regions have been hampered by the lack of anti-idiotypic antibodies that recognize specific heavy and light chain variable region sequences. Sixty percent of human monoclonal IgM anti-IgG autoantibodie