Research Interests:
Research Interests:
Research Interests: Virology, Biological Sciences, Cell line, Mutation, Mice, and 3 moreAnimals, Temperature, and Base Sequence
ULBPs are human ligands for NKG2D, an activating receptor expressed on natural killer (NK) cells, NK1.1 T cells, and T cells. ULBPs are expressed by a variety of leukemias, carcinomas, melanomas, and tumor cell lines. ULBP expression... more
ULBPs are human ligands for NKG2D, an activating receptor expressed on natural killer (NK) cells, NK1.1 T cells, and T cells. ULBPs are expressed by a variety of leukemias, carcinomas, melanomas, and tumor cell lines. ULBP expression correlates with improved survival in can- cer patients, however, the nature of the immune response that ULBPs elicit is not well understood. We
Research Interests:
Interleukin 1 (IL-1) is a two-member family of proteins (IL-1..cap alpha.. and IL-1..beta..) that mediates a diverse series of immune and inflammatory responses. These two proteins have only 26% amino acid homology yet bind to the same... more
Interleukin 1 (IL-1) is a two-member family of proteins (IL-1..cap alpha.. and IL-1..beta..) that mediates a diverse series of immune and inflammatory responses. These two proteins have only 26% amino acid homology yet bind to the same receptor. It is of importance to define the active sites of these molecules in order to understand their receptor interactions and the mechanisms
Research Interests: Multidisciplinary, Humans, Beta decay, PNAS, Peptides, and 14 moreActive site, Amino Acid Profile, Biological activity, Amino Acid Sequence, Membrane Protein, Growth Factor, Cell free System, Protein Binding, Organic Compound, Protein Biosynthesis, Molecular Structure, Interleukin, In Vitro Transcription, and Inflammatory response
Research Interests:
Research Interests:
Research Interests:
Interleukin 1 (IL-1) is a two-member family of proteins (IL-1 alpha and IL-1 beta) that mediates a diverse series of immune and inflammatory responses. These two proteins have only 26% amino acid homology yet bind to the same receptor. It... more
Interleukin 1 (IL-1) is a two-member family of proteins (IL-1 alpha and IL-1 beta) that mediates a diverse series of immune and inflammatory responses. These two proteins have only 26% amino acid homology yet bind to the same receptor. It is of importance to define the active sites of these molecules in order to understand their receptor interactions and the mechanisms involved in their multiple biological functions. We report here the localization of the biologically active portions within the initial polypeptide translation products. An in vitro transcription and translation system was used to generate specific fragments of each of the IL-1 molecules, which then were assayed for receptor binding capability and biological activity. Using this system, we have demonstrated that core sequences of amino acids for IL-1 beta (numbers 120-266) and 140 amino acids for IL-1 alpha (numbers 128-267) must be left intact to retain full biological activity and further that the biological activities of the IL-1 polypeptides parallel their receptor binding capabilities.
Research Interests: Multidisciplinary, Humans, Beta decay, PNAS, Peptides, and 14 moreActive site, Amino Acid Profile, Biological activity, Amino Acid Sequence, Membrane Protein, Growth Factor, Cell free System, Protein Binding, Organic Compound, Protein Biosynthesis, Molecular Structure, Interleukin, In Vitro Transcription, and Inflammatory response
Research Interests:
A cDNA encoding biologically active human interleukin 7 was isolated by hybridization with the homologous murine clone. Nucleotide sequence analysis indicated that this cDNA was capable of encoding a protein of 177 amino acids with a... more
A cDNA encoding biologically active human interleukin 7 was isolated by hybridization with the homologous murine clone. Nucleotide sequence analysis indicated that this cDNA was capable of encoding a protein of 177 amino acids with a signal sequence of 25 amino acids and a calculated mass of 17.4 kDa for the mature protein. Recombinant human interleukin 7 stimulated the proliferation of murine pre-B cells and was active on cells harvested from human bone marrow that are enriched for B-lineage progenitor cells. Analysis of RNA by blot hybridization demonstrated the presence of two size classes of interleukin 7 mRNA in human splenic and thymic tissue.