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

Identification and characterisation of putative drug binding sites in human ATP-binding cassette B5 (ABCB5) transporter

30 Dec 2020

Abstract excerpt

The human ATP-binding cassette B5 (ABCB5) transporter, a member of the ABC transporter superfamily, is linked to chemoresistance in tumour cells by drug effluxion. However, little is known about its structure and drug-binding sites. In this study, we generated an atomistic model of the full-length human ABCB5 transporter with the highest quality using the X-ray crystal structure of mouse ABCB1 (Pgp1), a close...

Read the complete abstract on PubMed

Topics

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

Share to Drug Transport and Resistance Mechanisms
Share to Pharmacological Effects and Toxicity Studies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33510870
DOI: 10.1016/j.csbj.2020.12.042

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characterisation of putative drug binding sites in human ATP-binding cassette B5 (ABCB5) transporterPMID 33510870Read ↗

Molecular Modeling Studies to Probe the Binding Hypothesis of Novel Lead Compounds against Multidrug Resistance Protein ABCB1Semantic proximity Read ↗

Binding site of ABC transporter homology models confirmed by ABCB1 crystal structureSemantic proximity Read ↗

Expression of human ABCB5 confers resistance to taxanes and anthracyclinesSemantic proximity Read ↗

Molecular evolutionary analysis of ABCB5: the ancestral gene is a full transporter with potentially deleterious single nucleotide polymorphisms.Semantic proximity Read ↗

Deciphering the roles of ABCB5 in normal and cancer cellsSemantic proximity Read ↗

Structure and Mechanism of Human ABC TransportersSemantic proximity Read ↗

Multidrug efflux pumps: The structures of prokaryotic ATP‐binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P‐glycoproteins and homologuesSemantic proximity Read ↗

ATP binding cassette systems: structures, mechanisms, and functionsSemantic proximity Read ↗

An update on ABCB1 pharmacogenetics: insights from a 3D model into the location and evolutionary conservation of residues corresponding to SNPs associated with drug pharmacokinetics.Semantic proximity Read ↗

Multidrug Resistance in Mammals and Fungi—From MDR to PDR: A Rocky Road from Atomic Structures to Transport MechanismsSemantic proximity Read ↗

Molecular modeling of the human multidrug resistance protein 1 (MRP1/ABCC1)Semantic proximity Read ↗

Homology Modeling of the Human P-glycoprotein (ABCB1) and Insights into Ligand Binding through Molecular Docking StudiesSemantic proximity Read ↗

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