The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. [electronic resource]
Producer: 20030707Description: 19087-94 p. digitalISSN:- 0021-9258
- Adenosine Triphosphatases -- metabolism
- Alternative Splicing
- Amino Acid Sequence
- Brain Chemistry
- Cell Fractionation
- Cell Line
- Cytoplasm -- chemistry
- Endoplasmic Reticulum -- chemistry
- Fluorescent Antibody Technique
- Gene Expression
- Green Fluorescent Proteins
- HSP40 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins -- metabolism
- Heat-Shock Proteins -- chemistry
- Humans
- Immunosorbent Techniques
- Inclusion Bodies
- Luminescent Proteins -- genetics
- Microscopy, Confocal
- Molecular Chaperones -- chemistry
- Molecular Sequence Data
- Mutagenesis
- Photoreceptor Cells -- chemistry
- Protein Folding
- Protein Isoforms -- analysis
- Protein Prenylation
- Protein Processing, Post-Translational
- Recombinant Proteins
- Retina -- chemistry
- Rhodopsin -- chemistry
- Spinal Cord -- chemistry
- Tissue Distribution
- Transfection
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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