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._2j
Characterization of five novel vasopressin V2 receptor mutants causing nephrogenic diabetes insipidus reveals a role of tolvaptan for M272R-V2R mutation.
Prosperi F et al.
Scientific Reports, 2020
Corrigendum to: the role of conserved extracellular cysteine residues in vasopressin V2 receptor function and properties of two naturally occurring mutant receptors with additional extracellular cysteine residues.
Schulein R et al.
Febs Letters, 2000
Structural implication for receptor oligomerization from functional reconstitution studies of mutant V2 vasopressin receptors.
Schulz A et al.
The Journal of Biological Chemistry, 2000
The role of conserved extracellular cysteine residues in vasopressin V2 receptor function and properties of two naturally occurring mutant receptors with additional extracellular cysteine residues.
Schülein R et al.
Febs Letters, 2000
Effect of mutations in putative hormone binding sites on V2 vasopressin receptor function.
Sebti Y et al.
Research in Pharmaceutical Sciences, 0
Study of V2 vasopressin receptor hormone binding site using in silico methods.
Sebti Y et al.
Research in Pharmaceutical Sciences, 0
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