ArticleProceedings of the National Academy of Sciences of the United States of America2021
Structure of Ycf1p reveals the transmembrane domain TMD0 and the regulatory region of ABCC transporters.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Structural basis for LMBD1-dependent trafficking and cobalamin export of ABCD4.Nature communications · 2026Article
- Reading Between the ABCs: Intrinsic Disorder and Evolutionary Dynamics of Non-Canonical Regions in ABC Transporters.International journal of molecular sciences · 2026Article
- Multi-State Structural Genomics Enables Large-Scale, Mechanistic, and Context-Specific Classification of ABCC6 Genetic Variants Implicated in Calcification Diseases.International journal of molecular sciences · 2026Article
- Structural insights into toxicant export mediated by ABCC2 in Arabidopsis thaliana.Nature communications · 2025Article
- Tolerance of the non-conventional yeast Wickerhamomyces anomalus BT3 to cadmium exposure: a genomic characterization.Current genetics · 2025Article
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cryo-EM reveals a phosphorylated R-domain envelops the NBD1 catalytic domain in an ABC transporter.Life science alliance · 2024Article
- Structural basis for autoinhibition by the dephosphorylated regulatory domain of Ycf1.Nature communications · 2024Article
- Structural basis for the modulation of MRP2 activity by phosphorylation and drugs.Nature communications · 2024Article
- Comparing ATPase activity of ATP-binding cassette subfamily C member 4, lamprey CFTR, and human CFTR using an antimony-phosphomolybdate assay.Frontiers in pharmacology · 2024Article
- Placing steroid hormones within the human ABCC3 transporter reveals a compatible amphiphilic substrate-binding pocket.The EMBO journal · 2023Article
- How Cryo-EM Has Expanded Our Understanding of Membrane Transporters.Drug metabolism and disposition: the biological fate of chemicals · 2023Review
- The inhibition mechanism of the SUR2A-containing KNature communications · 2023Article
- On the interplay between lipids and asymmetric dynamics of an NBS degenerate ABC transporter.Communications biology · 2023Article
- A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance.Molecules (Basel, Switzerland) · 2023Review
- Mechanistic insights on KATP channel regulation from cryo-EM structures.The Journal of general physiology · 2023Review
- Biochemical studies highlight determinants for metal selectivity in the Escherichia coli periplasmic solute binding protein NikA.Metallomics : integrated biometal science · 2022Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation.Nature communications · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP binding cassette (ABC) proteins typically function in active transport of solutes across membranes. The ABC core structure is composed of two transmembrane domains (TMD1 and TMD2) and two cytosolic nucleotide binding domains (NBD1 and NBD2). Some members of the C-subfamily of ABC (ABCC) proteins, including human multidrug resistance proteins (MRPs), also possess an N-terminal transmembrane domain (TMD0) that contains five transmembrane α-helices and is connected to the ABC core by the L0 linker. While TMD0 was resolved in SUR1, the atypical ABCC protein that is part of the hetero-octameric ATP-sensitive K
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