Article
In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER.
The EMBO journal - 15 Mar 1995
Schmitz A, Maintz M, Kehle T, Herzog V
Abstract excerpt
The signal for degradation of proteins in the endoplasmic reticulum (ER) is thought to be the exposure of internal domains which are buried when the protein has adopted its correct conformation and which are also exposed in assembly intermediates. This raises the question of why the intermediates...
Topics
- Adenosine Triphosphate
- Animals
- Base Sequence
- CHO Cells
- Carrier Proteins
- Cricetinae
- Endoplasmic Reticulum
- Endoplasmic Reticulum Chaperone BiP
- Heat-Shock Proteins
- Hexosaminidases
- Insulin
- Iodide Peroxidase
- Molecular Chaperones
- Molecular Sequence Data
- Mutation
- Proinsulin
- Protein Conformation
- Protein Folding