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 and functional consequences of mutating cysteine residues in the amino terminus of human multidrug resistance-associated protein 1.

The Journal of biological chemistry - 15 Nov 2002

Yang Youyun, Chen Qun, Zhang Jian-Ting

Abstract excerpt

Multidrug resistance-associated protein 1 (MRP1) is a member of the ATP-binding cassette membrane transport superfamily and is responsible for multidrug resistance in cancer cells. Currently, there are nine known human MRPs. Distinct from many other members of the ATP-binding cassette superfamily, human MRP1 and four other MRPs have an additional membrane-spanning domain (MSD) with a putative extracellular amino...

Read the complete abstract on PubMed

Topics

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

Share to Cell Separation
Share to Colchicine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Doxorubicin

Share to Etoposide

Share to Fluorescent Antibody Technique, Indirect

Share to Multidrug Resistance-Associated Proteins

Share to Trypsin

Share to Vincristine

Source

Identifiers

PMID: 12235150
DOI: 10.1074/jbc.M207003200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional consequences of mutating cysteine residues in the amino terminus of human multidrug resistance-associated protein 1.PMID 12235150Read ↗

Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1).Semantic proximity Read ↗

Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1).Semantic proximity Read ↗

Charged Amino Acids in the Sixth Transmembrane Helix of Multidrug Resistance Protein 1 (MRP1/ABCC1) Are Critical Determinants of Transport ActivitySemantic proximity Read ↗

Mutation of proline residues in the NH(2)-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function.Semantic proximity Read ↗

Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region.Semantic proximity Read ↗

Identification of a Nonconserved Amino Acid Residue in Multidrug Resistance Protein 1 Important for Determining Substrate SpecificitySemantic proximity Read ↗

Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1.Semantic proximity Read ↗

Mammalian multidrug-resistance proteins (MRPs)Semantic proximity Read ↗

Identification of an Amino Acid Residue in Multidrug Resistance Protein 1 Critical for Conferring Resistance to AnthracyclinesSemantic proximity Read ↗

Structural, mechanistic and clinical aspects of MRP1.Semantic proximity Read ↗

Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions.Semantic proximity Read ↗

Multidrug resistance proteins (MRPs, ABCCs): importance for pathophysiology and drug therapy.Semantic proximity Read ↗

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