▪ Abstract Classical class I molecules assemble in the endoplasmic reticulum (ER) with
peptides mostly generated from cytosolic proteins by the proteasome. The activity of the …

▪ Abstract Major histocompatibility complex (MHC) class I molecules bind peptides derived
from cellular proteins and display them for surveillance by the immune system. These …

Large multisubunit proteasomal complexes, catalyzing an extralysosomal, ATP‐dependent
pathway for selective degradation of unnecessary proteins, are thought to be responsible for …

MHC class I molecules present antigenic peptides that are mostly derived from endogenous
cytosolic proteins. Recent studies addressing the function of the proteasome and its activator …

MHC class II molecules assemble in the endoplasmic reticulum in a chaperone-mediated
fashion to form a nine-chain structure consisting of three alpha beta dimers associated with …

Background Intracellular proteins are processed into small peptides that bind HLA class I
molecules of the major histocompatibility complex (MHC) in order to be presented to T …

MHC class I molecules present degradation products derived from intracellular proteins,
whereas MHC class II molecules generally present peptides derived from extracellular or …

LMP2 and LMP7 are proteins encoded by MHC genes that are tightly linked to the genes
encoding TAP, the transporter that conveys peptides from the cytosol to the endoplasmic …

MHC-class-I-presented peptides are predominantly generated by the proteasome system.
IFN-γ strongly influences the processing efficiency by inducing immunoproteasome …

Processing of antigens for presentation by major histocompatibility complex (MHC) class I
molecules requires the activity of the proteasome. The 20S proteasome complex is …