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

Interaction of C-terminal loop 13 of sodium-glucose cotransporter SGLT1 with lipid bilayers.

Biochemistry - 28 Jun 2005

Raja M Mobeen, Kinne Rolf K H

Abstract excerpt

We have previously shown that C-terminal loop 13 of SGLT1 acts as a major binding domain for the aglucon residues of d-glucose transport inhibitors, phlorizin (Raja, M. M., Tyagi, N. K., and Kinne, R. K. H. (2003) Phlorizin Recognition in a C-terminal Fragment of SGLT1 Studied by Tryptophan Scann...

Read the complete abstract on PubMed

Topics

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

Share to Fluorescence
Share to Lipid Bilayers
Share to Liposomes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Monosaccharide Transport Proteins

Share to Phosphatidylcholines

Share to Phosphatidylglycerols

Share to Spectrometry, Fluorescence

Share to Tryptophan

Source

Identifiers

PMID: 15966736
DOI: 10.1021/bi050323d

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-15966736-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction of C-terminal loop 13 of sodium-glucose cotransporter SGLT1 with lipid bilayers.PMID 15966736Read ↗

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

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

Binding of phlorizin to the C-terminal loop 13 of the Na(+)/glucose cotransporter does not depend on the [560-608] disulfide bond.Semantic proximity Read ↗

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

D-Glucose-recognition and phlorizin-binding sites in human sodium/D-glucose cotransporter 1 (hSGLT1): a tryptophan scanning study.Semantic proximity Read ↗

Analysis of transmembrane segment 8 of the GLUT1 glucose transporter by cysteine-scanning mutagenesis and substituted cysteine accessibility.Semantic proximity Read ↗

Active site voltage clamp fluorometry of the sodium glucose cotransporter hSGLT1.Semantic proximity Read ↗

Transmembrane segment 3 of the Glut1 glucose transporter is an outer helix.Semantic proximity Read ↗

Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III.Semantic proximity Read ↗

Alteration of sugar-induced conformational changes of the melibiose permease by mutating Arg141 in loop 4-5.Semantic proximity Read ↗

Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport.Semantic proximity Read ↗

Transmembrane segment 12 of the Glut1 glucose transporter is an outer helix and is not directly involved in the transport mechanism.Semantic proximity Read ↗

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