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2004 - Phoenix
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Alexander Oksche
Title:
MD
Email:
Phone:
Work +1-49 (30) 8445-1860, Fax +1-49 (30) 8445-1818
Organization:
Institut Fuer Pharmakologie
Division:
Charite - Berlin
Address:
Thielallee 67-73
Berlin, 14195
Germany
16 Articles
16 Articles
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
Disease-Causing V2 Vasopressin Receptors are Retained in Different Compartments of the Early Secretory Pathway
Pharmacochaperones Post-Translationally Enhance Cell Surface Expression by Increasing Conformational Stability of Wild-Type and Mutant Vasopressin V2 Receptors
The Prostaglandin E2 Analogue Sulprostone Antagonizes Vasopressin-Induced Antidiuresis Through Activation of Rho
Cell-Biologic and Functional Analyses of Five New Aquaporin-2 Missense Mutations that Cause Recessive Nephrogenic Diabetes Insipidus
Heteroligomerization of an Aquaporin-2 Mutant with Wild-Type Aquaporin-2 and Their Misrouting to Late Endosomes/Lysosomes Explains Dominant Nephrogenic Diabetes Insipidus
Variant Amino Acids in the Extracellular Loops of Murine and Human Vasopressin V2 Receptors Account for Differences in Cell Surface Expression and Ligand Affinity
Polarized Expression of the Vasopressin V2 Receptor in Madin-Darby Canine Kidney Cells
Aquaporin-2 Expression in Primary Cultured Rat Inner Medullary Collecting Duct Cells
A Dileucine Sequence and an Upstream Glutamate Residue in the Intracellular Carboxyl Terminus of the Vasopressin V2 Receptor are Essential for Cell Surface Transport in COS.M6 Cells
The Molecular Basis of Nephrogenic Diabetes Insipidus
Folding and Cell Surface Expression of the Vasopressin V2 Receptor: Requirement of the Intracellular C-terminus
Congenital Nephrogenic Diabetes Insipidus
Two Novel Mutations in the Aquaporin-2 and the Vasopressin V2 Receptor Genes in Patients with Congenital Nephrogenic Diabetes Insipidus
Vasopressin V2 Receptor Mutants that Cause X-linked Nephrogenic Diabetes Insipidus: Analysis of Expression, Processing, and Function
Two Novel Mutations in the Vasopressin V2 Receptor Gene in Patients with Congenital Nephrogenic Diabetes Insipidus
10 Conference Proceedings
10 Conference Proceedings
Transport Defects of V2 Receptor Mutants Found in Patients with X-linked Nephrogenic Diabetes Insipidus
Aquaporin-2 Expression in Primary Cultures of Rat Inner Medullary Collecting Duct Cells - A New In-Vitro Model System Facilitating the Study of the Vasopressin-Regulated Antidiuretic Machinery at the Cellular Level
Analysis of naturally occurring and in vitro mutations of the V2 receptor gene interfering with proper splicing
Naturally occurring and in vitro mutations defining the role of the NPXXY motif in the vasopressin V2 receptor
Molecular mechanisms underlying dominant Nephrogenic Diabetes Insipidus caused by mutations in the AQP2 gene
Cell biological and functional analysis of five new Aquaporin-2 gene missense mutations in recessive Nephrogenic Diabetes Insipidus
Comparative analysis of human and murine vasopressin V2 receptor genes and their encoded proteins reveal striking differences in their genomic structure and functional properties
Lack of AVP-induced phosphorylation of the Aquaporin-2 mutants AQP2-R254L and AQP2-R254Q explains dominant Nephrogenic Diabetes Insipidus
Characterization of mutant vasopressin V2 receptors with a misfolded AVP binding site
Differences between ER-retained vasopressin V2 receptor mutants in antagonist-mediated restoration of cell surface expression
16 Articles
16 Articles