A unique tumor antigen produced by a single amino acid substitution
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چکیده
منابع مشابه
A Single Amino Acid Substitution in the Human Histocompatibility Leukocyte Antigen Dr3 R Chain Selectively Alters Antigen Presentation
Activation of antigen-specific helper/inducer T cells requires that antigen be presented by APC in association with self MHC class II molecules (1). Recent evidence indicates that APC accomplish this by degrading exogenous soluble proteins to peptide fragments, which become bound to class II molecules (2, 3) . The amino acid residues of human class II molecules that interact with immunogenic pe...
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Activation of T lymphocytes by immunogenic peptides bound to HLA molecules is a central event in the generation of an immune response. To determine the sites on HLA molecules involved in this process, we isolated mutant EBV-transformed B cell clones that express altered HLA-DR3 molecules. One mutant has lost the ability to stimulate a T cell clone specific for a mycobacterial protein, but retai...
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Previous results indicated that performance of chicks fed a high level (10%) of poultry by-product meal(PBM) was lower than performance of chicks fed a corn-soybean meal (SBM) diet. The latter difference was hypothesized to be due to variation in digestible amino acid (AA) levels among the diets. This study evaluated diets containing PBM formulated on equivalent total AA basis vs. an equivalent...
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MOTIVATION We address the question of whether there exists an effective evolutionary model of amino-acid substitution that forms a metric-distance function. There is always a trade-off between speed and sensitivity among competing computational methods of determining sequence homology. A metric model of evolution is a prerequisite for the development of an entire class of fast sequence analysis...
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A point mutation (1 277 CGG to CAG) was identified in the R-type pyruvate kinase (PK) cDNA of a PK variant, PK Sapporo, associated with hereditary non-spherocytic hemolytic anemia. The mutation causes a single amino acid substitution from Arg to Gln at the 426th amino acid residue of human R-type PK; consequently, the hydrophobicity around the mutated site is drastically decreased. The amino ac...
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ژورنال
عنوان ژورنال: Immunity
سال: 1995
ISSN: 1074-7613
DOI: 10.1016/1074-7613(95)90078-0