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

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

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

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

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

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

EMC is required for biogenesis of Xport‐A, an essential chaperone of Rhodopsin‐1 and the TRP channel

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

Structural basis for effector transmembrane domain recognition by type VI secretion system chaperones

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

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

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

Dimeric Rhodopsin R135L Mutant-Transducin-like Complex Sheds Light on Retinitis Pigmentosa Misfunctions

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

Intracellular microbial rhodopsin-based optogenetics to control metabolism and cell signaling - Chemical Society Reviews (RSC Publishing) DOI:10.1039/D3CS00699A

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

Endoplasmic reticulum membrane complex (EMC) may assist the exit of

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

Loss of hiro Accelerates the Course of Age-Related Retinal Degeneration

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

Chaperoning G protein-coupled receptors: from cell biology to therapeutics. - Abstract - Europe PMC

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

Advancing synthetic biology through cell-free protein synthesis - Computational and Structural Biotechnology Journal

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

The trafficking of bacterial type rhodopsins into the Chlamydomonas eyespot and flagella is IFT mediated

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

The Role of EMC during Membrane Protein Biogenesis: Trends in Cell Biology

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

EMC is required for the biogenesis of Xport-A in mammalian cells. A

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

A model for EMC function in biogenesis of multi-pass membrane proteins.