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

Active site voltage clamp fluorometry of the sodium glucose cotransporter hSGLT1.

Proceedings of the National Academy of Sciences of the United States of America - 14 Nov 2017

Gorraitz Edurne, Hirayama Bruce A, Paz Aviv, Wright Ernest M, Loo Donald D F

Abstract excerpt

In the human sodium glucose cotransporter (hSGLT1) cycle, the protein undergoes conformational changes where the sugar-binding site alternatively faces the external and internal surfaces. Functional site-directed fluorometry was used to probe the conformational changes at the sugar-binding site. Residues (Y290, T287, H83, and N78) were mutated to cysteines. The mutants were expressed in Xenopus laevis oocytes and...

Read the complete abstract on PubMed

Topics

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

Share to Fluorometry
Share to Ions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Animal

Share to Molecular Probe Techniques

Share to Polyethylene Glycols

Share to Rhodamines

Share to Sodium

Share to Symporters

Source

Open in PubMed Open full text

Identifiers

PMID: 29087341
DOI: 10.1073/pnas.1713899114
PMCID: PMC5699082

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Active site voltage clamp fluorometry of the sodium glucose cotransporter hSGLT1.PMID 29087341Read ↗

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

The Human Sodium-Glucose Cotransporter (hSGLT1) Is a Disulfide-Bridged Homodimer with a Re-Entrant C-Terminal Loop.Semantic proximity Read ↗

Structural Basis of the Selective Sugar Transport in Sodium-Glucose Cotransporters.Semantic proximity Read ↗

Membrane topology of loop 13-14 of the Na+/glucose cotransporter (SGLT1): a SCAM and fluorescent labelling study.Semantic proximity Read ↗

Conformational transitions of the sodium-dependent sugar transporter, vSGLT.Semantic proximity Read ↗

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

Functional Site-Directed Fluorometry.Semantic proximity Read ↗

Structural and functional significance of water permeation through cotransporters.Semantic proximity Read ↗

Broadband Tuning the Voltage Dependence of a Sodium ChannelSemantic proximity Read ↗

A highly conserved alanine in the S6 domain of the hERG1 K+ channel is required for normal gating.Semantic proximity Read ↗

Class A GPCRs use the membrane potential to increase their sensitivity and selectivitySemantic proximity Read ↗

The solute carrier SLC9C1 is a Na+/H+-exchanger gated by an S4-type voltage-sensor and cyclic-nucleotide binding.Semantic proximity Read ↗

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