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- Xport-A functions as a chaperone by stabilizing the first 5 transmembrane domains of Rhodopsin-1
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 five transmembrane domains of rhodopsin-1 - ScienceDirect
Rhodopsin biosynthesis defects in santa maria¹. (A) Previously proposed
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TRP and Rhodopsin Transport Depends on Dual XPORT ER Chaperones Encoded by an Operon - ScienceDirect
Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 - ScienceDirect
Xport-A functions as a chaperone by stabilizing the first five transmembrane domains of rhodopsin-1 - ScienceDirect
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The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins
