Pages that link to "Q46449902"
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The following pages link to A structural basis for CD8+ T cell-dependent recognition of non-homologous peptide ligands: implications for molecular mimicry in autoreactivity (Q46449902):
Displaying 12 items.
- The MHC Class I Cancer-Associated Neoepitope Trh4 Linked with Impaired Peptide Processing Induces a Unique Noncanonical TCR Conformer (Q27703723) (← links)
- Inflammation-associated nitrotyrosination affects TCR recognition through reduced stability and alteration of the molecular surface of the MHC complex (Q28481493) (← links)
- Structural allele-specific patterns adopted by epitopes in the MHC-I cleft and reconstruction of MHC:peptide complexes to cross-reactivity assessment (Q28752409) (← links)
- Distortion of the Major Histocompatibility Complex Class I Binding Groove to Accommodate an Insulin-derived 10-Mer Peptide (Q35905292) (← links)
- CD8 single-cell gene coexpression reveals three different effector types present at distinct phases of the immune response (Q36229371) (← links)
- Immune system derived from homeostatic proliferation generates normal CD8 T-cell memory but altered repertoires and diminished heterologous immune responses (Q36787568) (← links)
- CrossTope: a curate repository of 3D structures of immunogenic peptide: MHC complexes. (Q43213104) (← links)
- Unexpected T-cell recognition of an altered peptide ligand is driven by reversed thermodynamics (Q44447688) (← links)
- Crystal structures of H-2Db in complex with the LCMV-derived peptides GP92 and GP392 explain pleiotropic effects of glycosylation on antigen presentation and immunogenicity (Q47144276) (← links)
- The immunoproteasome subunit LMP7 is required in the murine thymus for filling up a hole in the T cell repertoire (Q47601349) (← links)
- Cross-recognition of a myelin peptide by CD8+ T cells in the CNS is not sufficient to promote neuronal damage. (Q48211678) (← links)
- Successive crystal structure snapshots suggest the basis for MHC class I peptide loading and editing by tapasin (Q91943742) (← links)