Xport-A functions as a chaperone by stabilizing the first 5 transmembrane domains of Rhodopsin-1

Identification of Small Molecular Chaperones Binding P23H Mutant Opsin through an In Silico Structure-Based Approach

IJMS, Free Full-Text

Structure network-based landscape of rhodopsin misfolding by mutations and algorithmic prediction of small chaperone action - Computational and Structural Biotechnology Journal

TRP and Rhodopsin Transport Depends on Dual XPORT ER Chaperones Encoded by an Operon - ScienceDirect

EMC is required for biogenesis and membrane insertion of Xport-A, an essential chaperone of rhodopsin-1 and the TRP channel

Full article: The role of motor proteins in photoreceptor protein transport and visual function

Endoplasmic reticulum membrane complex (EMC) is not required for the

Chemical and pharmacological chaperones as new therapeutic agents, Expert Reviews in Molecular Medicine

Rhodopsin as a Molecular Target to Mitigate Retinitis Pigmentosa

Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 - ScienceDirect