Associated Papers
CANDID Study: Clinical and Molecular Characterization of Congenital Arginine Vasopressin-Resistance and the Use of a Novel Diagnostic Biomarker in Indian Children.
Banerjee S et al.
Indian Journal of Pediatrics, 2026
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
Phenotype and renal outcomes of patients with congenital arginine vasopressin-resistance.
Tseng MH et al.
Nephrology, Dialysis, Transplantation : Official Publication of the European Dialysis and Transplant Association - European Renal Association, 2025
A Pedigree Study of Hereditary Diabetes Insipidus Caused by X Chromosome AVPR2 Gene Mutation.
Li L et al.
International Medical Case Reports Journal, 2025
Novel AVPR2 mutations in congenital nephrogenic diabetes insipidus: clinical characteristics and genetic analysis.
Xue K et al.
Frontiers in Pediatrics, 2025
Clinical, Genetic and Functional Characterization of a Novel AVPR2 Missense Mutation in a Woman with X-Linked Recessive Nephrogenic Diabetes Insipidus.
Selvaraj S et al.
Journal of Personalized Medicine, 2022
Targeting trafficking as a therapeutic avenue for misfolded GPCRs leading to endocrine diseases.
Ulloa-Aguirre A et al.
Frontiers in Endocrinology, 2022
Novel AVPR2 mutations and clinical characteristics in 28 Chinese families with congenital nephrogenic diabetes insipidus.
Li Q et al.
Journal of Endocrinological Investigation, 2021
Misfolded G Protein-Coupled Receptors and Endocrine Disease. Molecular Mechanisms and Therapeutic Prospects.
Ulloa-Aguirre A et al.
International Journal of Molecular Sciences, 2021
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
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
Novel and recurrent variants in AVPR2 in 19 families with X-linked congenital nephrogenic diabetes insipidus.
Joshi S et al.
European Journal of Pediatrics, 2018
Pharmacoperone drugs: targeting misfolded proteins causing lysosomal storage-, ion channels-, and G protein-coupled receptors-associated conformational disorders.
Hou ZS et al.
Expert Review of Clinical Pharmacology, 2018
Pharmacological Chaperones as Potential Therapeutic Strategies for Misfolded Mutant Vasopressin Receptors.
Mouillac B et al.
Handbook of Experimental Pharmacology, 2018
How genetic errors in GPCRs affect their function: Possible therapeutic strategies.
Stoy H et al.
Genes & Diseases, 2015
Vasopressin receptors and pharmacological chaperones: from functional rescue to promising therapeutic strategies.
Mouillac B et al.
Pharmacological Research, 2014
A de novo novel missense mutation in AVPR2 with severe nephrogenic diabetes insipidus.
Kobayashi D et al.
Ndt Plus, 2010
Intracellular activation of vasopressin V2 receptor mutants in nephrogenic diabetes insipidus by nonpeptide agonists.
Robben JH et al.
Proceedings of the National Academy of Sciences of the United States of America, 2009
Nephrogenic diabetes insipidus (NDI): clinical, laboratory and genetic characterization of five Brazilian patients.
Vaisbich MH et al.
Clinics (sao Paulo, Brazil), 2009
AVPR2 variants and mutations in nephrogenic diabetes insipidus: review and missense mutation significance.
Spanakis E et al.
Journal of Cellular Physiology, 2008
Derlin-1 and p97/valosin-containing protein mediate the endoplasmic reticulum-associated degradation of human V2 vasopressin receptors.
Schwieger I et al.
Molecular Pharmacology, 2008
Molecular genetic study of congenital nephrogenic diabetes insipidus and rescue of mutant vasopressin V2 receptor by chemical chaperones.
Cheong HI et al.
Nephrology (carlton, Vic.), 2007
Functional rescue of vasopressin V2 receptor mutants in MDCK cells by pharmacochaperones: relevance to therapy of nephrogenic diabetes insipidus.
Robben JH et al.
American Journal of Physiology. Renal Physiology, 2007
Pharmacological chaperones in nephrogenic diabetes insipidus: possibilities for clinical application.
Robben JH et al.
Biodrugs : Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy, 2007
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
Pharmacologic chaperones as a potential treatment for X-linked nephrogenic diabetes insipidus.
Bernier V et al.
Journal of the American Society of Nephrology : Jasn, 2006
Characterization of vasopressin V2 receptor mutants in nephrogenic diabetes insipidus in a polarized cell model.
Robben JH et al.
American Journal of Physiology. Renal Physiology, 2005
Disease-causing V(2) vasopressin receptors are retained in different compartments of the early secretory pathway.
Hermosilla R et al.
Traffic (copenhagen, Denmark), 2004
Pharmacochaperones post-translationally enhance cell surface expression by increasing conformational stability of wild-type and mutant vasopressin V2 receptors.
Wüller S et al.
The Journal of Biological Chemistry, 2004
Molecular and cellular defects in nephrogenic diabetes insipidus.
Knoers NV et al.
Pediatric Nephrology (berlin, Germany), 2001
[From genes to disease: from vasopressin-V2-receptor and aquaporine-2 to nephrogenic diabetes insipidus].
Knoers NV et al.
Nederlands Tijdschrift Voor Geneeskunde, 2000
Pharmacological chaperones: a new twist on receptor folding.
Morello JP et al.
Trends in Pharmacological Sciences, 2000
Report of 33 novel AVPR2 mutations and analysis of 117 families with X-linked nephrogenic diabetes insipidus.
Arthus MF et al.
Journal of the American Society of Nephrology : Jasn, 2000
Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants.
Morello JP et al.
The Journal of Clinical Investigation, 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
Clinical presentation and follow-up of 30 patients with congenital nephrogenic diabetes insipidus.
van Lieburg AF et al.
Journal of the American Society of Nephrology : Jasn, 1999
AVPR2 variants and V2 vasopressin receptor function in nephrogenic diabetes insipidus.
Wildin RS et al.
Kidney International, 1998
Functional studies of twelve mutant V2 vasopressin receptors related to nephrogenic diabetes insipidus: molecular basis of a mild clinical phenotype.
Ala Y et al.
Journal of the American Society of Nephrology : Jasn, 1998
The molecular basis of nephrogenic diabetes insipidus.
Oksche A et al.
Journal of Molecular Medicine (berlin, Germany), 1998
Mutational analyses of AVPR2 gene in three Japanese families with X-linked nephrogenic diabetes insipidus: two recurrent mutations, R137H and deltaV278, caused by the hypermutability at CpG dinucleotides.
Shoji Y et al.
Human Mutation, 1998
Vasopressin V2 receptor mutants that cause X-linked nephrogenic diabetes insipidus: analysis of expression, processing, and function.
Oksche A et al.
Molecular Pharmacology, 1996
Molecular analysis of X-linked nephrogenic diabetes insipidus.
Fujiwara TM et al.
European Journal of Endocrinology, 1996
Heterogeneous AVPR2 gene mutations in congenital nephrogenic diabetes insipidus.
Wildin RS et al.
American Journal of Human Genetics, 1994
Nature and recurrence of AVPR2 mutations in X-linked nephrogenic diabetes insipidus.
Bichet DG et al.
American Journal of Human Genetics, 1994
Inheritance of mutations in the V2 receptor gene in thirteen families with nephrogenic diabetes insipidus.
Knoers NV et al.
Kidney International, 1994
Mutations and diseases of G protein coupled receptors.
Birnbaumer M
Journal of Receptor and Signal Transduction Research, 0