The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Membrane topology distinguishes a subfamily of the ATP‐binding cassette (ABC) transporters
Open accessAbstract
A group of ATP‐binding cassette (ABC) transporters, including the yeast cadmium transporter (YCF1), the mammalian multidrug resistance‐associated protein (MRP), the multispecific organic anion transporter and its congener (MOAT and EBCR), as well as the sulfonylurea receptor (SUR), group into a subfamily by sequence comparison. We suggest that these MRP‐related proteins are also characterized by a special, common membrane topology pattern. The most studied ABC transporters, the cystic fibrosis transmembrane conductance regulator (CFTR) and the multidrug resistance (MDR) proteins, were shown to contain a tandem repeat of six transmembrane helices, each set followed by an ATP‐binding domain. According to the present study, in contrast to various membrane topology predictions proposed for the different MRP‐related proteins, they all seem to have a CFTR/MDR‐like core structure, and an additional, large, N‐terminal hydrophobic region. This latter domain is predicted to contain 4–6 (most probably 5) transmembrane helices, and is occasionally glycosylated on the cell surface. Since all the MRP‐related transporters were shown to interact with anionic compounds, the N‐terminal membrane‐bound domain may have a key role in these interactions.
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Cites
Overexpression of a Transporter Gene in a Multidrug-Resistant Human Lung Cancer Cell Line
Cole, S. P. C., Bhardwaj, G., Gerlach, J. H., Mackie, J. E., Grant, C. E., Almquist, K. C., Stewart, A. J., Kurz, E. U., Duncan, A. M. V., & Deeley, R. G. (1992) · Science · doi:10.1126/science.1360704 · Cited by 3,037
Cited by
The HMMTOP transmembrane topology prediction server
Tusnády, G. E., & Simon, I. (2001) · Bioinformatics · doi:10.1093/bioinformatics/17.9.849 · Cited by 1,907
Self-citationA New ER Trafficking Signal Regulates the Subunit Stoichiometry of Plasma Membrane KATP Channels
Zerangue, N., Schwappach, B., Jan, Y. N., & Jan, L. Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)80708-4 · Cited by 1,025
Deeley, R. G., Westlake, C., & Cole, S. P. C. (2006) · Physiological Reviews · doi:10.1152/physrev.00035.2005 · Cited by 761
Molecular Biology of Adenosine Triphosphate-Sensitive Potassium Channels*
Aguilar-Bryan, L., & Bryan, J. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.2.0361 · Cited by 698
Li, W., Zhang, H., Assaraf, Y. G., Zhao, K., Xu, X., Xie, J., Yang, D.-H., & Chen, Z.-S. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2016.05.001 · Cited by 673
Metadata
- Authors
- Tusnády, G. E., Bakos, É., Váradi, A., & Sarkadi, B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-02-03
- Volume
- 402
- Issue
- 1
- Pages
- 1-3
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2019710821
- Cited by
- 244
- References
- 1
- FWCI
- 13.75
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Tusnády, G. E., Bakos, É., Váradi, A., & Sarkadi, B. (1997). Membrane topology distinguishes a subfamily of the ATP‐binding cassette (ABC) transporters. FEBS Letters. https://doi.org/10.1016/s0014-5793(96)01478-0
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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