scholarly article | Q13442814 |
P356 | DOI | 10.1038/79716 |
P698 | PubMed publication ID | 11017095 |
P2093 | author name string | Kranz DM | |
P2860 | cites work | Crystal structure of a T cell receptor bound to an allogeneic MHC molecule | Q27627292 |
Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen | Q27748865 | ||
Structural basis of 2C TCR allorecognition of H-2Ld peptide complexes | Q27758459 | ||
The molecular basis of allorecognition | Q28268279 | ||
A basis for alloreactivity: MHC helical residues broaden peptide recognition by the TCR. | Q32061562 | ||
Binding energetics of T-cell receptors: correlation with immunological consequences | Q33720544 | ||
High-affinity reactions between antigen-specific T-cell receptors and peptides associated with allogeneic and syngeneic major histocompatibility complex class I proteins | Q35918289 | ||
Role of 2CT cell receptor residues in the binding of self- and allo-major histocompatibility complexes | Q36368381 | ||
A ubiquitous protein is the source of naturally occurring peptides that are recognized by a CD8+ T-cell clone | Q36699072 | ||
The role of peptides in T cell alloreactivity is determined by self-major histocompatibility complex molecules | Q40895891 | ||
Ligand recognition by alpha beta T cell receptors | Q46222293 | ||
Alanine scanning mutagenesis of an alphabeta T cell receptor: mapping the energy of antigen recognition | Q74545050 | ||
High determinant density may explain the phenomenon of alloreactivity | Q85697732 | ||
P433 | issue | 4 | |
P304 | page(s) | 277-278 | |
P577 | publication date | 2000-10-01 | |
P1433 | published in | Nature Immunology | Q1071725 |
P1476 | title | Incompatible differences: view of an allogeneic pMHC-TCR complex | |
P478 | volume | 1 |