Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP. [electronic resource]
Producer: 19961011Description: 20895-902 p. digitalISSN:- 0021-9258
- 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
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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