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

Functional analysis of the human concentrative nucleoside transporter-1 variant hCNT1S546P provides insight into the sodium-binding pocket.

American journal of physiology. Cell physiology - 1 Jan 2012

Cano-Soldado Pedro, Gorraitz Edurne, Errasti-Murugarren Ekaitz, Casado F Javier, Lostao M Pilar, Pastor-Anglada Marçal

Abstract excerpt

SLC28 genes, encoding concentrative nucleoside transporter proteins (CNT), show little genetic variability, although a few single nucleotide polymorphisms (SNPs) have been associated with marked functional disturbances. In particular, human CNT1S546P had been reported to result in negligible thym...

Read the complete abstract on PubMed

Topics

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

Share to Dogs
Share to Endoplasmic Reticulum
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Transport Proteins

Share to Proline

Share to Protein Transport

Share to Serine

Share to Sodium

Source

Identifiers

PMID: 21998139
DOI: 10.1152/ajpcell.00198.2011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21998139-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of the human concentrative nucleoside transporter-1 variant hCNT1S546P provides insight into the sodium-binding pocket.PMID 21998139Read ↗

Functional characterization of a nucleoside-derived drug transporter variant (hCNT3C602R) showing altered sodium-binding capacity.Semantic proximity Read ↗

Identification and functional characterization of variants in human concentrative nucleoside transporter 3, hCNT3 (SLC28A3), arising from single nucleotide polymorphisms in coding regions of the hCNT3 gene.Semantic proximity Read ↗

Identification and functional analysis of variants in the human concentrative nucleoside transporter 2, hCNT2 (SLC28A2) in Chinese, Malays and Indians.Semantic proximity Read ↗

Conserved residues F316 and G476 in the concentrative nucleoside transporter 1 (hCNT1) affect guanosine sensitivity and membrane expression, respectively.Semantic proximity Read ↗

A proton-mediated conformational shift identifies a mobile pore-lining cysteine residue (Cys-561) in human concentrative nucleoside transporter 3.Semantic proximity Read ↗

Functional analysis of genetic variants in the human concentrative nucleoside transporter 3 (CNT3; SLC28A3).Semantic proximity Read ↗

The human concentrative and equilibrative nucleoside transporter families, SLC28 and SLC29.Semantic proximity Read ↗

Identification of amino acid residues responsible for the pyrimidine and purine nucleoside specificities of human concentrative Na(+) nucleoside cotransporters hCNT1 and hCNT2.Semantic proximity Read ↗

Genetic analysis and functional characterization of polymorphisms in the human concentrative nucleoside transporter, CNT2.Semantic proximity Read ↗

Functional and genetic diversity in the concentrative nucleoside transporter, CNT1, in human populations.Semantic proximity Read ↗

Missense mutation T485S alters NBCe1-A electrogenicity causing proximal renal tubular acidosis.Semantic proximity Read ↗

Cysteine-accessibility analysis of transmembrane domains 11-13 of human concentrative nucleoside transporter 3.Semantic proximity Read ↗

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