ArticleBiochemistry2010
Role of transmembrane segment 5 and extracellular loop 3 in the homodimerization of human ABCC1.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- Oligomerization of drug transporters: Forms, functions, and mechanisms.Acta pharmaceutica Sinica. B · 2024Review
- Insights Into the Mechanism of MCT8 Oligomerization.Journal of the Endocrine Society · 2020Article
- Human bile acid transporter ASBT (SLC10A2) forms functional non-covalent homodimers and higher order oligomers.Biochimica et biophysica acta. Biomembranes · 2018Article
- Determinants of 14-3-3σ protein dimerization and function in drug and radiation resistance.The Journal of biological chemistry · 2013Article
- Casein kinase 2α regulates multidrug resistance-associated protein 1 function via phosphorylation of Thr249.Molecular pharmacology · 2012Article
- Different roles of TM5, TM6, and ECL3 in the oligomerization and function of human ABCG2.Biochemistry · 2012Article
- Human ABCC1 interacts and colocalizes with ATP synthase α, revealed by interactive proteomics analysis.Journal of proteome research · 2012Article
- Multidrug resistance-associated protein 1 (MRP1/ABCC1) polymorphism: from discovery to clinical application.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Resistance to multiple anticancer agents is a major obstacle in the successful treatment of cancers. Overexpression of some ATP-binding cassette (ABC) membrane transporters such as ABCC1 has been shown to be a major contributor of multidrug resistance (MDR) in both laboratory cell line models and the clinical setting. ABCC1 has been thought to function as a homodimer with a putative dimerization domain located in the first 281 amino acid residues, including MSD0 and L0 domains. In this study, we further mapped in detail the dimerization site and placed it in TM5 and ECL3 in MSD0 using co-expression and co-immunoprecipitation of a series of deletion constructs. TM5 and ECL3 in one subunit appear to interact with TM5 and ECL3 in the opposing subunit in a sequence-independent manner, but their physical location together with the hydrophobicity of TM5 and the length of ECL3 appears to be important contributors to the dimerization ability of ABCC1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.