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

Conformationally sensitive residues in transmembrane domain 9 of the Na+/dicarboxylate co-transporter.

The Journal of biological chemistry - 10 Aug 2001

Pajor A M

Abstract excerpt

The Na(+)/dicarboxylate co-transporter, NaDC-1, couples the transport of sodium and Krebs cycle intermediates, such as succinate and citrate. Previous studies identified two functionally important amino acids, Glu-475 and Cys-476, located in transmembrane domain (TMD) 9 of NaDC-1. In the present study, each amino acid in TMD-9 was mutated to cysteine, one at a time, and the accessibility of the...

Read the complete abstract on PubMed

Topics

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

Share to Cations
Share to Electrophysiology
Share to Indicators and Reagents

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

Share to Mesylates

Share to Oligonucleotides

Share to Organic Anion Transporters, Sodium-Dependent

Share to Symporters

Share to Xenopus

Source

Identifiers

PMID: 11399753
DOI: 10.1074/jbc.M011387200

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

Conformationally sensitive residues in transmembrane domain 9 of the Na+/dicarboxylate co-transporter.PMID 11399753Read ↗

Conformationally sensitive residues in extracellular loop 5 of the Na+/dicarboxylate co-transporter.Semantic proximity Read ↗

Transmembrane helix 7 in the Na+/dicarboxylate cotransporter 1 is an outer helix that contains residues critical for function.Semantic proximity Read ↗

Threonine-509 is a determinant of apparent affinity for both substrate and cations in the human Na+/dicarboxylate cotransporter.Semantic proximity Read ↗

Role of Sodium dependent SLC13 transporter and its inhibitors in various metabolic disordersSemantic proximity Read ↗

Identification of a disulfide bridge linking the fourth and the seventh extracellular loops of the Na+/glucose cotransporter.Semantic proximity Read ↗

Single nucleotide polymorphisms in the human Na+-dicarboxylate cotransporter affect transport activity and protein expression.Semantic proximity Read ↗

An investigation of cysteine mutants on the cytoplasmic loop X/XI in the melibiose transporter of Escherichia coli by using thiol reagents: implication of structural conservation of charged residues.Semantic proximity Read ↗

Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter.Semantic proximity Read ↗

Sodium-dependent reorganization of the sugar-binding site of SGLT1.Semantic proximity Read ↗

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

An N-terminal nucleotide-binding site in VDAC1: involvement in regulating mitochondrial function.Semantic proximity Read ↗

Mitochondrial NAD+ gradient sustained by membrane potential and transport.Semantic proximity Read ↗

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