Campylobacter jejuni infection and Guillain-Barré syndrome
10.1056/nejm199511233332102 · doi-reference
Occurrence of MRI abnormalities in patients with isolated optic neuritis
10.1159/000117361 · doi-reference
Structural evidence for induced fit as a mechanism for antibody-antigen recognition
10.1126/science.1546293 · doi-reference
Peptide recognition by two HLA-A2/ Tax11-19-specific T cell clones in relationship to their MHC/peptide/TCR crystal structures
10.4049/jimmunol.162.9.5389 · doi-reference
Structure of a covalently stabilized complex of a human αβ T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
10.1093/emboj/19.21.5611 · doi-reference
The crystal structure of a T cell receptor in complex with peptide and MHC class II
10.1126/science.286.5446.1913 · doi-reference
Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
10.1126/science.279.5354.1166 · doi-reference
An αβ T cell receptor structure at 2.5Å and its orientation in the TCR-MHC complex
10.1126/science.274.5285.209 · doi-reference
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
10.1016/s1074-7613(00)80080-1 · doi-reference
Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids
10.1016/s1074-7613(00)80546-4 · doi-reference
Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
10.1038/384134a0 · doi-reference
HLA class II allelic variation and susceptibility to pemphigus vulgaris
10.1073/pnas.85.10.3504 · doi-reference
X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II
10.1016/s1074-7613(00)80369-6 · doi-reference
Peptide binding specificity of HLA-DR4 molecules: correlation with rheumatoid arthritis association
10.1084/jem.181.5.1847 · doi-reference
HLA class II region nucleotide sequences
10.1111/j.1399-0039.1995.tb03125.x · doi-reference
Effect of natural polymorphism at residue 86 of the HLA-DRβ chain on peptide binding
10.4049/jimmunol.147.4.1292 · doi-reference
Crystallographic anlaysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
10.1073/pnas.93.2.734 · doi-reference
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
10.1038/368215a0 · doi-reference
