Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Investigating the surface expression of the renal type IIa Na+/Pi-cotransporter in Xenopus laevis oocytes.

The Journal of membrane biology - 1 Mar 2001

Traebert M, Köhler K, Lambert G, Biber J, Forster I, Murer H

Abstract excerpt

We have combined a functional assay, surface labeling and immunocytochemical methods to compare total and surface-exposed renal type IIa Na+/Pi cotransporter protein. The wild-type type cotransporter (NaPi-IIa) and its functionally comparable cysteine mutant S460C were expressed in Xenopus oocyte...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biotin
Share to Biotinylation
Share to Electrochemistry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Indicators and Reagents

Share to Mesylates

Share to Oocytes

Share to Symporters

Share to Xenopus laevis

Source

Identifiers

PMID: 11284206
DOI: 10.1007/s002320010059

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11284206-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Investigating the surface expression of the renal type IIa Na+/Pi-cotransporter in Xenopus laevis oocytes.PMID 11284206Read ↗

Essential cysteine residues of the type IIa Na+/Pi cotransporter.Semantic proximity Read ↗

An apical expression signal of the renal type IIc Na+-dependent phosphate cotransporter in renal epithelial cells.Semantic proximity Read ↗

Identification of a carboxyl-terminal motif essential for the targeting of Na+-HCO-3 cotransporter NBC1 to the basolateral membrane.Semantic proximity Read ↗

N-Glycosylation at two sites critically alters thiazide binding and activity of the rat thiazide-sensitive Na(+):Cl(-) cotransporter.Semantic proximity Read ↗

Characterization of a murine type II sodium-phosphate cotransporter expressed in mammalian small intestine.Semantic proximity Read ↗

Functional characterization of two naturally occurring mutations in the human sodium-phosphate cotransporter type IIa.Semantic proximity Read ↗

Identification of functionally important sites in the first intracellular loop of the NaPi-IIa cotransporter.Semantic proximity Read ↗

Processing and stability of type IIc sodium-dependent phosphate cotransporter mutations in patients with hereditary hypophosphatemic rickets with hypercalciuria.Semantic proximity Read ↗

Asn441 plays a key role in folding and function of the Na+/I- symporter (NIS).Semantic proximity Read ↗

Molecular analysis of a congenital iodide transport defect: G543E impairs maturation and trafficking of the Na+/I- symporter.Semantic proximity Read ↗

The Iodide Transport Defect-Causing Y348D Mutation in the Na+/I- Symporter Renders the Protein Intrinsically Inactive and Impairs Its Targeting to the Plasma Membrane.Semantic proximity Read ↗

Sorting of rat SPNT in renal epithelium is independent of N-glycosylation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.