The Chaperone Environment at the Cytoplasmic Face of the Endoplasmic Reticulum Can Modulate Rhodopsin Processing and Inclusion Formation (Q28117679)

4 January 2017

title

The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation (English)

1 reference

4 January 2017

The Chaperone Environment at the Cytoplasmic Face of the Endoplasmic Reticulum Can Modulate Rhodopsin Processing and Inclusion Formation (English)

1 reference

https://api.crossref.org/works/10.1074/JBC.M212349200

3 January 2024

main subject

endoplasmic reticulum

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0 references

1 reference

https://api.crossref.org/works/10.1074/JBC.M212349200

3 January 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.M212349200

3 January 2024

J. Paul Chapple

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A12754272

3 January 2024

Michael E. Cheetham

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A12754272

3 January 2024

language of work or name

English

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publication date

23 May 2003

1 reference

full work available at URL

4 January 2017

http://www.jbc.org/article/S0021925820801318/pdf

file format

Portable Document Format

online access status

open access

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A12754272

https://api.elsevier.com/content/article/PII:S0021925820801318?httpAccept=text/xml

3 January 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.M212349200

https://api.elsevier.com/content/article/PII:S0021925820801318?httpAccept=text/plain

3 January 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.M212349200

https://syndication.highwire.org/content/doi/10.1074/jbc.M212349200

3 January 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.M212349200

Journal of Biological Chemistry

3 January 2024

published in

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4 January 2017

volume

278

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4 January 2017

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4 January 2017

page(s)

19087–19094

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Identification of an outer segment targeting signal in the COOH terminus of rhodopsin using transgenic Xenopus laevis

4 January 2017

cites work

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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1

21 January 2018

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Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa

21 January 2018

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Transgenic mice with a rhodopsin mutation (Pro23His): a mouse model of autosomal dominant retinitis pigmentosa

21 January 2018

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Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa

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A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system

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Specificity in intracellular protein aggregation and inclusion body formation

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Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones?

21 January 2018

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Unfolding retinal dystrophies: a role for molecular chaperones?

21 January 2018

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The J-domain family and the recruitment of chaperone power

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21 January 2018

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Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons

21 January 2018

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Inhibition of hsc70-catalysed clathrin uncoating by HSJ1 proteins.

21 January 2018

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21 January 2018

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The Leber congenital amaurosis gene product AIPL1 is localized exclusively in rod photoreceptors of the adult human retina

21 January 2018

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Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane

21 January 2018

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Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3

21 January 2018

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HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria

21 January 2018

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Isoprenylation of the plant molecular chaperone ANJ1 facilitates membrane association and function at high temperature

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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

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Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast

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The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis

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A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment

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3 January 2024

115

2907

Saliba

2002

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Biosynthesis and degradation of CFTR.

3 January 2024

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3 January 2024

Identifiers

0 references

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