Associated Papers
A small molecule stabilizer rescues the surface expression of nearly all missense variants in a GPCR.
Mighell TL et al.
Nature Structural & Molecular Biology, 2025
40983772 (PubMed )
Supplement: 41594_2025_1659_MOESM5_ESM.xlsx › Fig._2a
Inactive structures of the vasopressin V2 receptor reveal distinct binding modes for Tolvaptan and Mambaquaretin toxin.
Fouillen A et al.
Nature Communications, 2025
Integrating Population Variants and Protein Structural Analysis to Improve Clinical Genetic Diagnosis and Treatment in Nephrogenic Diabetes Insipidus.
Liao P et al.
Frontiers in Pediatrics, 2021
33996673 (PubMed )
Supplement: Data_Sheet_1.pdf
[Analysis of AVPR2 gene mutation in a pedigree affected with congenital nephrogenic diabetes insipidus].
Dai Z et al.
Zhonghua Yi Xue Yi Chuan Xue Za Zhi = Zhonghua Yixue Yichuanxue Zazhi = Chinese Journal of Medical Genetics, 2016
How genetic errors in GPCRs affect their function: Possible therapeutic strategies.
Stoy H et al.
Genes & Diseases, 2015
26229975 (PubMed )
Supplement: mmc1.docx
Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases.
Ryu GM et al.
Nucleic Acids Research, 2009
19139070 (PubMed )
Supplement: gkn1008_nar-01723-s-2008-File009.xls › TypeII_
Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus.
Robben JH et al.
American Journal of Physiology. Renal Physiology, 2006
Molecular and cellular defects in nephrogenic diabetes insipidus.
Knoers NV et al.
Pediatric Nephrology (berlin, Germany), 2001
Association of calnexin with wild type and mutant AVPR2 that causes nephrogenic diabetes insipidus.
Morello JP et al.
Biochemistry, 2001
Nephrogenic diabetes insipidus: functional analysis of new AVPR2 mutations identified in Italian families.
Albertazzi E et al.
Journal of the American Society of Nephrology : Jasn, 2000
Select a paper to view details