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MHC class I molecules, for instance, are involved in the binding and presentation of intracellular generated peptides to CD8+ T cells, whereas class II molecules present peptides from extracellular origin to CD4+ T cells.
Classical MHC molecules are cell surface glycoproteins whose primary role is binding and presentation of antigens to T cell receptors as part of a "self/non-self" recognition mechanism representing the first step of adaptive immune response [16].
The reason for this is not clear, but may simply be due to differences in the binding and presentation of epitopes between the distinct MHC class II haplotypes.
Likewise, a negative association suggests that the binding and presentation of a peptide is effective and elicits a successful T-cell cytotoxic response with destruction of leukemia cells.
In a subgroup of three laboratories (Z5, Z6 and Z8), an allogeneic APC population (T2 or K562-A*0201 cells) was added for binding and presentation of the synthetic peptides.
The highly polymorphic HLA DR, DQ, and DP loci are encoded by genes in the human major histocompatibility complex (MHC), and are responsible for the binding and presentation of infection-derived peptides to CD4+ T cells, leading to adaptive immune responses to infections (Cooke and Hill, 2001).
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Variability in the HLA-DRB genes influences antigen binding, and the 1501 allele is thought to increase MS risk by increasing binding to and presentation of aromatic residues present in the myelin basic protein to the Tcell receptor (Ota et al., 1990), leading to increased numbers of MBP-reactive Tcells (Oksenberg et al., 1993).
Moreover, they are essential for the binding, transport, and presentation of growth factors, inflammatory signals, chemoattractants, and soluble antigens that govern the differentiation, proliferation, survival, polarity, and migration of immune cells [ 38].
Interestingly, the significant reduction in terms of cytotoxicity is not accompanied by a significant reduction in the uptake (~15 20%), binding, catabolism, processing, and presentation of immunodominant peptides to CD4+ or CD8+ T cells from these LLO mutants, confirming that antigenicity of LLO is also independent of its cytotoxic property [ 18].
It is possible that the highly specific heparin-binding domains of VEGF limits loading due to the specific orientation and presentation of binding sites presented by heparin.
Their function has been postulated to include roles in peptide-binding and presentation, but without cleavage.
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binding and discovery of
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binding and hemolysis of
binding and hybridization of
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