(Q40373611)

English

The hydrophobic amino acid residues in the membrane-proximal C tail of the G protein-coupled vasopressin V2 receptor are necessary for transport-competent receptor folding

scientific article published on September 2005

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

The hydrophobic amino acid residues in the membrane-proximal C tail of the G protein-coupled vasopressin V2 receptor are necessary for transport-competent receptor folding (English)

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

G protein-coupled receptor

0 references

protein folding

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0 references

1 reference

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author name string

Anja Thielen

1

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Morad Oueslati

2

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Ricardo Hermosilla

3

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Gerd Krause

4

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Alexander Oksche

5

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Walter Rosenthal

6

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Ralf Schülein

7

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

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publication date

1 September 2005

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Europe PubMed Central

PubMed publication ID

19 September 2017

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

579

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Europe PubMed Central

PubMed publication ID

19 September 2017

23

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

5227-5235

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

A novel C-terminal motif is necessary for the export of the vasopressin V1b/V3 receptor to the plasma membrane.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

A conserved motif for the transport of G protein-coupled receptors from the endoplasmic reticulum to the cell surface

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Crystal structure of rhodopsin: A G protein-coupled receptor

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Truncation of the A1 adenosine receptor reveals distinct roles of the membrane-proximal carboxyl terminus in receptor folding and G protein coupling

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Functional rescue of the nephrogenic diabetes insipidus-causing vasopressin V2 receptor mutants G185C and R202C by a second site suppressor mutation

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Pharmacochaperones post-translationally enhance cell surface expression by increasing conformational stability of wild-type and mutant vasopressin V2 receptors

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Evidence that helix 8 of rhodopsin acts as a membrane-dependent conformational switch

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.043

21 January 2018

Identifiers

10.1016/J.FEBSLET.2005.08.043

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

19 September 2017

ResearchGate publication ID

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