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

Function-dependent conformational changes of the ABCG2 multidrug transporter modify its interaction with a monoclonal antibody on the cell surface.

The Journal of biological chemistry - 11 Feb 2005

Ozvegy-Laczka Csilla, Várady György, Köblös Gabriella, Ujhelly Olga, Cervenak Judit, Schuetz John D, Sorrentino Brian P, Koomen Gerrit-Jan, Váradi András, Német Katalin, Sarkadi Balázs

Abstract excerpt

The human ABCG2 protein is an important primary active transporter for hydrophobic compounds in several cell types, and its overexpression causes multidrug resistance in tumors. A monoclonal antibody (5D3) recognizes this protein on the cell surface. In ABCG2-expressing cells 5D3 antibody showed a saturable labeling and inhibited ABCG2 transport and ATPase function. However, at low antibody concentrations 5D3...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to ATP Binding Cassette Transporter, Subfamily G, Member 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Benzimidazoles

Share to Cell Separation

Share to Drug Resistance, Multiple

Share to Insecta

Share to Mitoxantrone

Share to Vanadates

Source

Identifiers

PMID: 15557326
DOI: 10.1074/jbc.M411338200

Genes

ABCG2
PNP

Variants

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

Function-dependent conformational changes of the ABCG2 multidrug transporter modify its interaction with a monoclonal antibody on the cell surface.PMID 15557326Read ↗

Interaction with the 5D3 monoclonal antibody is regulated by intramolecular rearrangements but not by covalent dimer formation of the human ABCG2 multidrug transporter.Semantic proximity Read ↗

Tumor-acquired somatic mutation affects conformation to abolish ABCG2-mediated drug resistance.Semantic proximity Read ↗

Structure of the human multidrug transporter ABCG2.Semantic proximity Read ↗

Disruption of the Unique ABCG-Family NBD:NBD Interface Impacts Both Drug Transport and ATP Hydrolysis.Semantic proximity Read ↗

Effect of Walker A mutation (K86M) on oligomerization and surface targeting of the multidrug resistance transporter ABCG2.Semantic proximity Read ↗

Mutational studies of G553 in TM5 of ABCG2: a residue potentially involved in dimerization.Semantic proximity Read ↗

ATP-competitive LRRK2 inhibitors interfere with monoclonal antibody binding to the kinase domain of LRRK2 under native conditions. A method to directly monitor the active conformation of LRRK2?Semantic proximity Read ↗

Structure of a zosuquidar and UIC2-bound human-mouse chimeric ABCB1.Semantic proximity Read ↗

Human ABCA3, a product of a responsible gene for abca3 for fatal surfactant deficiency in newborns, exhibits unique ATP hydrolysis activity and generates intracellular multilamellar vesicles.Semantic proximity Read ↗

Phosphorylation by protein kinase CK2 modulates the activity of the ATP binding cassette A1 transporter.Semantic proximity Read ↗

Nonequivalent Nucleotide Trapping in the Two Nucleotide Binding Folds of the Human Multidrug Resistance Protein MRP1Semantic proximity Read ↗

ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain.Semantic proximity Read ↗

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