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

Reconciling contradictory findings: Glucose transporter 1 (GLUT1) functions as an oligomer of allosteric, alternating access transporters.

The Journal of biological chemistry - 22 Dec 2017

Lloyd Kenneth P, Ojelabi Ogooluwa A, De Zutter Julie K, Carruthers Anthony

Abstract excerpt

Recent structural studies suggest that GLUT1 (glucose transporter 1)-mediated sugar transport is mediated by an alternating access transporter that successively presents exofacial (e2) and endofacial (e1) substrate-binding sites. Transport studies, however, indicate multiple, interacting (allosteric), and co-existent, exo- and endofacial GLUT1 ligand-binding sites. The present study asks whether these...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Glucose Transporter Type 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Maltose

Share to Molecular Docking Simulation

Share to Protein Interaction Domains and Motifs

Share to Stochastic Processes

Share to Structural Homology, Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 29066623
DOI: 10.1074/jbc.M117.815589
PMCID: PMC5743077

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reconciling contradictory findings: Glucose transporter 1 (GLUT1) functions as an oligomer of allosteric, alternating access transporters.PMID 29066623Read ↗

Will the original glucose transporter isoform please stand up!Semantic proximity Read ↗

Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in Sugar Porter familySemantic proximity Read ↗

Predicting the Three-Dimensional Structure of the Human Facilitative Glucose Transporter Glut1 by a Novel Evolutionary Homology Strategy: Insights on the Molecular Mechanism of Substrate Migration, and Binding Sites for Glucose and Inhibitory MoleculesSemantic proximity Read ↗

Mechanistic Insights into the Substrate Egress Pathways of Human Glucose Transporters GLUT1 and GLUT9Semantic proximity Read ↗

Crystal structure of the human glucose transporter GLUT1.Semantic proximity Read ↗

Distinct Allosteric Networks Underlie Mechanistic Speciation of ABC Transporters.Semantic proximity Read ↗

Pathogenic mutations causing glucose transport defects in GLUT1 transporter: The role of intermolecular forces in protein structure-function.Semantic proximity Read ↗

Title: Identification of new GLUT2-selective inhibitors through in silico ligand screening and validation in eukaryotic expression systemsSemantic proximity Read ↗

Substrate binding and lipid-mediated allostery in the human organic anion transporter 1 at the atomic-scaleSemantic proximity Read ↗

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

What we know about facilitative glucose transporters: Lessons from cultured cells, animal models, and human studiesSemantic proximity Read ↗

Insights into mechanism of glucokinase activation: observation of multiple distinct protein conformations.Semantic proximity Read ↗

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