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

Location of the antidepressant binding site in the serotonin transporter: importance of Ser-438 in recognition of citalopram and tricyclic antidepressants.

The Journal of biological chemistry - 10 Apr 2009

Andersen Jacob, Taboureau Olivier, Hansen Kasper B, Olsen Lars, Egebjerg Jan, Strømgaard Kristian, Kristensen Anders S

Abstract excerpt

The serotonin transporter (SERT) regulates extracellular levels of serotonin (5-hydroxytryptamine, 5HT) in the brain by transporting 5HT into neurons and glial cells. The human SERT (hSERT) is the primary target for drugs used in the treatment of emotional disorders, including depression. hSERT belongs to the solute carrier 6 family that includes a bacterial leucine transporter (LeuT), for which a high resolution...

Read the complete abstract on PubMed

Topics

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

Share to Antidepressive Agents, Tricyclic
Share to Citalopram

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Inhibitory Concentration 50

Share to Models, Chemical

Share to Molecular Conformation

Share to Serine

Share to Serotonin

Share to Serotonin Plasma Membrane Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19213730
DOI: 10.1074/jbc.M806907200
PMCID: PMC2665081

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Location of the antidepressant binding site in the serotonin transporter: importance of Ser-438 in recognition of citalopram and tricyclic antidepressants.PMID 19213730Read ↗

Mutational mapping and modeling of the binding site for (S)-citalopram in the human serotonin transporter.Semantic proximity Read ↗

Antidepressant specificity of serotonin transporter suggested by three LeuT-SSRI structures.Semantic proximity Read ↗

Transmembrane domain 6 of the human serotonin transporter contributes to an aqueously accessible binding pocket for serotonin and the psychostimulant 3,4-methylene dioxymethamphetamine.Semantic proximity Read ↗

Structural basis for action by diverse antidepressants on biogenic amine transporters.Semantic proximity Read ↗

High- and low-affinity binding of S-citalopram to the human serotonin transporter mutated at 20 putatively important amino acid positions.Semantic proximity Read ↗

Structural basis for recognition of diverse antidepressants by the human serotonin transporter.Semantic proximity Read ↗

Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis.Semantic proximity Read ↗

Tyr-95 and Ile-172 in transmembrane segments 1 and 3 of human serotonin transporters interact to establish high affinity recognition of antidepressants.Semantic proximity Read ↗

The antidepressant drug vilazodone is an allosteric inhibitor of the serotonin transporter.Semantic proximity Read ↗

Interaction of antidepressants with the serotonin and norepinephrine transporters: mutational studies of the S1 substrate binding pocket.Semantic proximity Read ↗

Structural basis for recognition of diverse antidepressants by the human serotonin transporterSemantic proximity Read ↗

Identification of a single amino acid, phenylalanine 586, that is responsible for high affinity interactions of tricyclic antidepressants with the human serotonin transporter.Semantic proximity Read ↗

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