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

Effects of truncation of the COOH-terminal region of a Na+-independent neutral and basic amino acid transporter on amino acid transport in Xenopus oocytes.

The Journal of biological chemistry - 12 Jul 1996

Miyamoto K, Segawa H, Tatsumi S, Katai K, Yamamoto H, Taketani Y, Haga H, Morita K, Takeda E

Abstract excerpt

To determine the role of a neutral and basic amino acid transporter (NBAT) in amino acid transport, we microinjected several COOH-terminal deletion mutants of NBAT cRNA into Xenopus oocytes and measured transport activity for arginine, leucine, and cystine in the presence and absence of sodium. Wild-type NBAT significantly stimulated the uptake of all three amino acids 10-20-fold compared with controls. On the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cloning, Molecular

Share to DNA, Complementary

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Sequence Deletion

Source

Identifiers

PMID: 8663184
DOI: 10.1074/jbc.271.28.16758

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of truncation of the COOH-terminal region of a Na+-independent neutral and basic amino acid transporter on amino acid transport in Xenopus oocytes.PMID 8663184Read ↗

Transporters for Cationic Amino Acids in Animal Cells: Discovery, Structure, and FunctionSemantic proximity Read ↗

Molecular cloning of mouse amino acid transport system B0, a neutral amino acid transporter related to Hartnup disorder.Semantic proximity Read ↗

Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1.Semantic proximity Read ↗

Cystinuria-specific rBAT(R365W) mutation reveals two translocation pathways in the amino acid transporter rBAT-b0,+AT.Semantic proximity Read ↗

Electrogenic Na/HCO3 cotransporter (NBCe1) variants expressed in Xenopus oocytes: functional comparison and roles of the amino and carboxy termini.Semantic proximity Read ↗

Cationic amino acids involved in dicarboxylate binding of the flounder renal organic anion transporter.Semantic proximity Read ↗

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

Identification of a chloride ion binding site in Na+/Cl -dependent transporters.Semantic proximity Read ↗

A novel role of the C-terminus of b 0,+ AT in the ER-Golgi trafficking of the rBAT-b 0,+ AT heterodimeric amino acid transporter.Semantic proximity Read ↗

The putative amino-terminal signal peptide of the cloned rat brain Na(+)-Ca2+ exchanger gene (RBE-1) is not mandatory for functional expression.Semantic proximity Read ↗

Structural and functional basis of amino acid specificity in the invertebrate cotransporter KAAT1.Semantic proximity Read ↗

Amino acid substitutions in the pore of rat glutamate receptors at sites influencing block by polyamines.Semantic proximity Read ↗

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