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

SNPs altering ammonium transport activity of human Rhesus factors characterized by a yeast-based functional assay.

PloS one - 1 Jan 2013

Deschuyteneer Aude, Boeckstaens Mélanie, De Mees Christelle, Van Vooren Pascale, Wintjens René, Marini Anna Maria

Abstract excerpt

Proteins of the conserved Mep-Amt-Rh family, including mammalian Rhesus factors, mediate transmembrane ammonium transport. Ammonium is an important nitrogen source for the biosynthesis of amino acids but is also a metabolic waste product. Its disposal in urine plays a critical role in the regulation of the acid/base homeostasis, especially with an acid diet, a trait of Western countries. Ammonium accumulation...

Topics

Join the communities discussing this publication.

Ammonium Compounds
Blood Proteins
Cation Transport Proteins
Protein Interaction Domains and Motifs
Protein Multimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Subunits

Rh-Hr Blood-Group System

Source

Open in PubMed Open full text

Identifiers

PMID: 23967154
DOI: 10.1371/journal.pone.0071092
PMCID: PMC3742762

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SNPs altering ammonium transport activity of human Rhesus factors characterized by a yeast-based functional assay.PMID 23967154Read ↗

Mechanism of genetic complementation of ammonium transport in yeast by human erythrocyte Rh-associated glycoprotein.Semantic proximity Read ↗

Rhesus factors and ammonium: a function in efflux?Semantic proximity Read ↗

Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cellsSemantic proximity Read ↗

Haploinsufficiency of the ammonia transporter Rhcg predisposes to chronic acidosis: Rhcg is critical for apical and basolateral ammonia transport in the mouse collecting duct.Semantic proximity Read ↗

The 1.3-Å resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH 3 transport by Rhesus family proteinsSemantic proximity Read ↗

Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures.Semantic proximity Read ↗

Rh Type B Glycoprotein Is a New Member of the Rh Superfamily and a Putative Ammonia Transporter in MammalsSemantic proximity Read ↗

Functional analysis of human RhCG: comparison with E. coli ammonium transporter reveals similarities in the pore and differences in the vestibule.Semantic proximity Read ↗

Identification of novel mutations in the SLC25A15 gene in hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome: a clinical, molecular, and functional study.Semantic proximity Read ↗

Prokaryotic ammonium transporters: what has three decades of research revealed?Semantic proximity Read ↗

Molecular biology of Rh proteins and relevance to molecular medicineSemantic proximity Read ↗

The monovalent cation leak in overhydrated stomatocytic red blood cells results from amino acid substitutions in the Rh-associated glycoprotein.Semantic proximity Read ↗

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