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

The citrate carrier CitS probed by single-molecule fluorescence spectroscopy.

Biophysical journal - 1 Mar 2003

Kästner Christopher N, Prummer Michael, Sick Beate, Renn Alois, Wild Urs P, Dimroth Peter

Abstract excerpt

A prominent region of the Na(+)-dependent citrate carrier (CitS) from Klebsiella pneumoniae is the highly conserved loop X-XI, which contains a putative citrate binding site. To monitor potential conformational changes within this region by single-molecule fluorescence spectroscopy, the target cysteines C398 and C414 of the single-Cys mutants (CitS-sC398, CitS-sC414) were selectively labeled with the...

Read the complete abstract on PubMed

Topics

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

Share to Citric Acid
Share to Conserved Sequence
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Escherichia coli Proteins

Share to Protein Subunits

Share to Spectrometry, Fluorescence

Share to Symporters

Source

Open in PubMed Open full text

Identifiers

PMID: 12609868
DOI: 10.1016/S0006-3495(03)74974-1
PMCID: PMC1302735

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

The citrate carrier CitS probed by single-molecule fluorescence spectroscopy.PMID 12609868Read ↗

High performance intensiometric direct- and inverse-response genetically encoded biosensors for citrateSemantic proximity Read ↗

Structure and elevator mechanism of the Na+-citrate transporter CitS.Semantic proximity Read ↗

A cell-based method to assess the activity of the human sodium-coupled citrate transporterSemantic proximity Read ↗

The mitochondrial citrate transport protein: probing the secondary structure of transmembrane domain III, identification of residues that likely comprise a portion of the citrate transport pathway, and development of a model for the putative TMDIII-TMDIII' interface.Semantic proximity Read ↗

The mitochondrial citrate transport protein: evidence for a steric interaction between glutamine 182 and leucine 120 and its relationship to the substrate translocation pathway and identification of other mechanistically essential residues.Semantic proximity Read ↗

Site-directed fluorescence studies of a prokaryotic ClC antiporter.Semantic proximity Read ↗

Ratiometric Fluorescent Protein Biosensors Reveal Citrate Dynamics and Cellular HeterogeneitySemantic proximity Read ↗

Role of citrate and phosphate anions in the mechanism of iron(III) sequestration by ferric binding protein: kinetic studies of the formation of the holoprotein of wild-type FbpA and its engineered mutants.Semantic proximity Read ↗

Structure of a slow CLC Cl⁻/H+ antiporter from a cyanobacterium.Semantic proximity Read ↗

Electrostatics Govern Protein Orientation on Citrate-Capped Gold NanoparticlesSemantic proximity Read ↗

A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.Semantic proximity Read ↗

Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog.Semantic proximity Read ↗

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