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

Conserved charged amino acid residues in the extracellular region of sodium/iodide symporter are critical for iodide transport activity.

Journal of biomedical science - 23 Nov 2010

Li Chia-Cheng, Ho Tin-Yun, Kao Chia-Hung, Wu Shih-Lu, Liang Ji-An, Hsiang Chien-Yun

Abstract excerpt

BACKGROUND: Sodium/iodide symporter (NIS) mediates the active transport and accumulation of iodide from the blood into the thyroid gland. His-226 located in the extracellular region of NIS has been demonstrated to be critical for iodide transport in our previous study. The conserved charged amino acid residues in the extracellular region of NIS were therefore characterized in this study. METHODS: Fourteen charged...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Iodides

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Symporters

Source

Open in PubMed Open full text

Identifiers

PMID: 21092238
DOI: 10.1186/1423-0127-17-89
PMCID: PMC3002920

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved charged amino acid residues in the extracellular region of sodium/iodide symporter are critical for iodide transport activity.PMID 21092238Read ↗

A homozygous missense mutation of the sodium/iodide symporter gene causing iodide transport defect.Semantic proximity Read ↗

The sodium/iodide Symporter (NIS): characterization, regulation, and medical significance.Semantic proximity Read ↗

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

Novel, missense and loss-of-function mutations in the sodium/iodide symporter gene causing iodide transport defect in three Japanese patients.Semantic proximity Read ↗

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

Sodium/Iodide Symporter Mutant V270E Causes Stunted Growth but No Cognitive Deficiency.Semantic proximity Read ↗

Mutations in the sodium/iodide symporter (NIS) gene as a cause for iodide transport defects and congenital hypothyroidism.Semantic proximity Read ↗

The sodium iodide symporter: its pathophysiological and therapeutic implications.Semantic proximity Read ↗

A novel peculiar mutation in the sodium/iodide symporter gene in spanish siblings with iodide transport defect.Semantic proximity Read ↗

Brief Report: A Novel Sodium/Iodide Symporter Mutation, S356F, Causing Congenital Hypothyroidism.Semantic proximity Read ↗

The iodide-transport-defect-causing mutation R124H: a δ-amino group at position 124 is critical for maturation and trafficking of the Na+/I- symporter.Semantic proximity Read ↗

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