Zobrazeno 1 - 10
of 44
pro vyhledávání: '"B M Sefton"'
Publikováno v:
The Journal of Immunology. 153:5465-5472
A mAb produced by immunization of mice with tyrosine-phosphorylated proteins from activated B lymphocytes was found to recognize valosin-containing protein (VCP). VCP is the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein and has lo
Publikováno v:
Molecular and Cellular Biology. 14:2429-2437
The tyrosine protein kinase p56lck transduces signals important for antigen-induced T-cell activation. In transgenic mice, p56lck is oncogenic when overexpressed or expressed as a mutant, catalytically activated enzyme. In humans, the LCK gene is loc
Autor:
Andrey S. Shaw, E D Cahir McFarland, T R Hurley, Matthew L. Thomas, B M Sefton, Jeanette T. Pingel
Publikováno v:
Proceedings of the National Academy of Sciences. 90:1402-1406
Stimulation of tyrosine phosphorylation is an early and important event in antigen-induced T-cell activation. T-cell clones deficient in expression of CD45, a transmembrane protein-tyrosine-phosphatase (protein-tyrosine-phosphate phosphohydrolase, EC
Autor:
K, Luo, B M, Sefton
Publikováno v:
Molecular and Cellular Biology. 12:4724-4732
p56lck, a member of the src family of cytoplasmic tyrosine kinases, is expressed predominantly in T cells where it associates with the T-cell surface molecules CD4 and CD8. Mutants of CD4 and CD8 that have lost the ability to associate with p56lck no
Autor:
M A Campbell, B M Sefton
Publikováno v:
The EMBO Journal. 9:2125-2131
Activation of both T and B lymphocytes through their membrane receptors for antigen is known to induce breakdown of inositol phospholipids. In addition, T cell activation by antigen is accompanied by increased protein tyrosine phosphorylation of comp
Publikováno v:
Molecular and Cellular Biology. 10:1853-1862
We report that the cytoplasmic domains of the T-lymphocyte glycoproteins CD4 and CD8 alpha contain short related amino acid sequences that are involved in binding the amino-terminal domain of the intracellular tyrosine protein kinase, p56lck. Transfe
Autor:
J Chalupny, Andrey S. Shaw, P Kavathas, B M Sefton, Craig Hammond, K E Amrein, John K. Rose, J A Whitney
Publikováno v:
Molecular and Cellular Biology. 10:1853-1862
We report that the cytoplasmic domains of the T-lymphocyte glycoproteins CD4 and CD8 alpha contain short related amino acid sequences that are involved in binding the amino-terminal domain of the intracellular tyrosine protein kinase, p56lck. Transfe
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 153(12)
A mAb produced by immunization of mice with tyrosine-phosphorylated proteins from activated B lymphocytes was found to recognize valosin-containing protein (VCP). VCP is the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein and has lo
Publikováno v:
The Journal of biological chemistry. 269(18)
In addition to membrane immunoglobulin (mIg), the B-cell antigen receptor contains Ig-alpha/Ig-beta heterodimers that link mIg to intracellular signaling molecules. To compare the ability of the cytoplasmic domains of Ig-alpha and Ig-beta to transduc
Publikováno v:
Advances in experimental medicine and biology. 365
In B lymphocytes, the cytoplasmic domains of the membrane immunoglobulin-associated heterodimeric Ig-alpha and Ig-beta proteins link membrane immunoglobulin to intracellular signalling molecules. We constructed chimeric genes encoding the extracellul