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

Identification and functional characterization of novel nonsynonymous variants in the human multidrug and toxin extrusion 2-K.

Drug metabolism and disposition: the biological fate of chemicals - 1 Sept 2014

Nishimura Kenta, Ide Ryosuke, Hirota Takeshi, Kawazu Kana, Kodama Sho, Takesue Hiroaki, Ieiri Ichiro

Abstract excerpt

This study was performed to identify genetic polymorphisms in multidrug and toxin extrusion 2-K (MATE2-K, SLC47A2), a proton/organic cation antiporter that plays a role in the transport of organic cations across the apical membrane in kidney epithelial cells into the urine, and to demonstrate their effects on MATE2-K functions in vitro. Four of the thirty single nucleotide polymorphisms (SNPs) we identified in...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Membrane

Share to Gene Frequency

Share to HEK293 Cells

Share to Kinetics

Share to Organic Cation Transport Proteins

Share to Polymorphism, Single Nucleotide

Source

Identifiers

PMID: 24985703
DOI: 10.1124/dmd.114.056887

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and functional characterization of novel nonsynonymous variants in the human multidrug and toxin extrusion 2-K.PMID 24985703Read ↗

Functional characterization of MATE2-K genetic variants and their effects on metformin pharmacokinetics.Semantic proximity Read ↗

Identification of multidrug and toxin extrusion (MATE1 and MATE2-K) variants with complete loss of transport activity.Semantic proximity Read ↗

Human multidrug and toxin extrusion 1 (MATE1/SLC47A1) transporter: functional characterization, interaction with OCT2 (SLC22A2), and single nucleotide polymorphisms.Semantic proximity Read ↗

Organic cation transporters (OCTs, MATEs), in vitro and in vivo evidence for the importance in drug therapy.Semantic proximity Read ↗

Organic cation transporter OCTs (SLC22) and MATEs (SLC47) in the human kidney.Semantic proximity Read ↗

Importance of the multidrug and toxin extrusion MATE/SLC47A family to pharmacokinetics, pharmacodynamics/toxicodynamics and pharmacogenomics.Semantic proximity Read ↗

Mammalian MATE (SLC47A) transport proteins: impact on efflux of endogenous substrates and xenobiotics.Semantic proximity Read ↗

Genetic variants in multidrug and toxic compound extrusion-1, hMATE1, alter transport function.Semantic proximity Read ↗

A common 5'-UTR variant in MATE2-K is associated with poor response to metformin.Semantic proximity Read ↗

The Impact of Genetic Polymorphisms in Organic Cation Transporters on Renal Drug DispositionSemantic proximity Read ↗

Organic cation transporters and their pharmacokinetic and pharmacodynamic consequences.Semantic proximity Read ↗

Identification and functional characterization of novel MATE1 genetic variations in Koreans.Semantic proximity Read ↗

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