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

Cysteine 144 in the third transmembrane domain of the creatine transporter is located close to a substrate-binding site.

The Journal of biological chemistry - 14 Dec 2001

Dodd J R, Christie D L

Abstract excerpt

All creatine transporters contain a cysteine residue (Cys(144)) in the third transmembrane domain that is not present in other members of the Na+,Cl(-)-dependent family of neurotransmitter transporters. Site-directed mutagenesis and reaction with methane thiosulfonates were used to investigate the importance of Cys(144) for transporter function. Replacement of Cys(144) with Ser did not significantly affect the...

Read the complete abstract on PubMed

Topics

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

Share to Biotinylation
Share to Chlorine
Share to Creatine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ethyl Methanesulfonate

Share to Indicators and Reagents

Share to Mesylates

Share to Sodium

Source

Identifiers

PMID: 11598117
DOI: 10.1074/jbc.M107137200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cysteine 144 in the third transmembrane domain of the creatine transporter is located close to a substrate-binding site.PMID 11598117Read ↗

Substituted cysteine accessibility of the third transmembrane domain of the creatine transporter: defining a transport pathway.Semantic proximity Read ↗

The interaction of the gamma-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV.Semantic proximity Read ↗

The loop between helix 4 and helix 5 in the monocarboxylate transporter MCT1 is important for substrate selection and protein stability.Semantic proximity Read ↗

Dynamic modification of a mutant cytoplasmic cysteine residue modulates the conductance of the human 5-HT3A receptor.Semantic proximity Read ↗

Role of the juxtamembrane region of cytoplasmic loop 3 in the gating and conductance of the cystic fibrosis transmembrane conductance regulator chloride channel.Semantic proximity Read ↗

Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance.Semantic proximity Read ↗

Transmembrane domain 8 of the {gamma}-aminobutyric acid transporter GAT-1 lines a cytoplasmic accessibility pathway into its binding pocket.Semantic proximity Read ↗

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

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

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

Functional and electrophysiological characterization of four non-truncating mutations responsible for creatine transporter (SLC6A8) deficiency syndrome.Semantic proximity Read ↗

Variable reactivity of an engineered cysteine at position 338 in cystic fibrosis transmembrane conductance regulator reflects different chemical states of the thiol.Semantic proximity Read ↗

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