The number of different peptides presented by major histocompatibility complex class I molecules to the immune system's T lymphocytes is inversely correlated with cell surface expression and is strongly associated with the response to infectious disease.

Downregulation of mitochondrial activity by immunosuppressive tumor-derived soluble factors leads to systemic unresponsiveness to the PD-1 blockade therapy.

We reveal TAPBPR is a peptide exchange catalyst which restricts the peptide repertoire presented by MHC I on cells, a finding which has important implications for all aspects of immune recognition.

The recently discovered peptide editor TAPBPR binds to UDP-glucose:glycoprotein glucosyltransferase 1 to provide quality control in the antigen presentation pathway by facilitating the reglucosylation of the glycan on MHC class I molecules.

A dedicated structural element facilitates chaperone and antigenic peptide selector function of TAP-associated glycoprotein, a major quality assurance auditor in adaptive immunity.

MR1T cells are human polyclonal T cells endowed with diverse effector functions in response to endogenous antigens presented by MHC-class 1-related molecule, MR1.

A recently discovered contagious cancer in the Tasmanian devil has the potential to become widespread in the population due to the loss of histocompatibility antigens that are allogeneic to its hosts.

Immunopeptidomics in combination with novel cell-based assays that assess peptide exchange reveal a critical role for the K22-D35 loop of TAPBPR in mediating peptide dissociation and peptide selection on MHC I.

A new type of hybrid nonribosomal peptide synthetase (NRPS)-like-pteridine synthase biosynthetic pathway has been illuminated via genome mining.

Antigen-specific control of CD4+ T cell trans-migration by brain endothelial cells via presentation of CNS-derived antigens in MHC-II molecules.