The Chaperone Environment at the Cytoplasmic Face of the Endoplasmic Reticulum Can Modulate Rhodopsin Processing and Inclusion Formation
Open Access
- 1 May 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (21) , 19087-19094
- https://doi.org/10.1074/jbc.m212349200
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- A Rhodopsin Mutant Linked to Autosomal Dominant Retinitis Pigmentosa Is Prone to Aggregate and Interacts with the Ubiquitin Proteasome SystemJournal of Biological Chemistry, 2002
- Protein Misfolding, Amyloid Formation, and NeurodegenerationNeuron, 2002
- Specificity in intracellular protein aggregation and inclusion body formationProceedings of the National Academy of Sciences, 2001
- Unfolding retinal dystrophies: a role for molecular chaperones?Trends in Molecular Medicine, 2001
- Identification of an Outer Segment Targeting Signal in the Cooh Terminus of Rhodopsin Using Transgenic Xenopus laevisThe Journal of cell biology, 2000
- Rhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1Cell, 1999
- A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segmentJournal of Neuroscience, 1994
- Structure and Function in Rhodopsin. 7. Point Mutations Associated with Autosomal Dominant Retinitis PigmentosaBiochemistry, 1994
- Transgenic mice with a rhodopsin mutation (Pro23His): A mouse model of autosomal dominant retinitis pigmentosaNeuron, 1992
- Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa.Proceedings of the National Academy of Sciences, 1991