Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP.

Beggah, A

Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP. [electronic resource] - The Journal of biological chemistry Aug 1996 - 20895-902 p. digital

Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.

0021-9258

10.1074/jbc.271.34.20895 doi


Animals
Base Sequence
Biological Transport
Carrier Proteins--metabolism
Cell Compartmentation
Cloning, Molecular
DNA Primers--chemistry
DNA, Complementary--genetics
Endoplasmic Reticulum Chaperone BiP
Endoplasmic Reticulum, Rough--metabolism
H(+)-K(+)-Exchanging ATPase--metabolism
Heat-Shock Proteins
Macromolecular Substances
Molecular Chaperones--metabolism
Molecular Sequence Data
Oocytes
Precipitin Tests
Protein Binding
Protein Folding
Rats
Sequence Alignment
Sequence Homology, Amino Acid
Sodium-Potassium-Exchanging ATPase--chemistry
Xenopus laevis