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

Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases.

Cancer research - 15 Oct 2009

Federici Luca, Lo Sterzo Carlo, Pezzola Silvia, Di Matteo Adele, Scaloni Flavio, Federici Giorgio, Caccuri Anna Maria

Abstract excerpt

Glutathione S-transferases (GST) constitute a superfamily of enzymes with diversified functions including detoxification from xenobiotics. In many human cancers, Pi class GST (GSTP1-1) is overexpressed and contributes to multidrug resistance by conjugating chemotherapeutics. In addition, GSTP1-1...

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents
Share to Binding Sites
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutathione S-Transferase pi

Share to Glutathione Transferase

Share to Mutagenesis, Site-Directed

Share to Oxadiazoles

Share to Protein Conformation

Source

Identifiers

PMID: 19808963
DOI: 10.1158/0008-5472.CAN-09-1314

Genes

GSTP1
GSTM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19808963-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases.PMID 19808963Read ↗

A strong glutathione S-transferase inhibitor overcomes the P-glycoprotein-mediated resistance in tumor cells. 6-(7-Nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol (NBDHEX) triggers a caspase-dependent apoptosis in MDR1-expressing leukemia cells.Semantic proximity Read ↗

Orthogonal protein purification--expanding the repertoire of GST fusion systems.Semantic proximity Read ↗

Molecular evolution of Theta-class glutathione transferase for enhanced activity with the anticancer drug 1,3-bis-(2-chloroethyl)-1-nitrosourea and other alkylating agents.Semantic proximity Read ↗

Mutational analysis of human glutathione transferase A2-2 identifies structural elements supporting high activity with the prodrug azathioprine.Semantic proximity Read ↗

Diuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108V.Semantic proximity Read ↗

Role of Ser11 in the stabilization of the structure of Ochrobactrum anthropi glutathione transferase.Semantic proximity Read ↗

Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity.Semantic proximity Read ↗

Structural, mutagenic, and kinetic analysis of the binding of substrates and inhibitors of human phenylethanolamine N-methyltransferase.Semantic proximity Read ↗

New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.Semantic proximity Read ↗

Differential protection against benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide-induced DNA damage in HepG2 cells stably transfected with allelic variants of pi class human glutathione S-transferase.Semantic proximity Read ↗

Glutathione transferases in the bioactivation of azathioprine.Semantic proximity Read ↗

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis.Semantic proximity Read ↗

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