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Na+, K+-ATPase Isozyme Diversity; Comparative Biochemistry and Physiological Implications of Novel Functional Interactions
Abstract
Na+, K+-ATPase is ubiquitously expressed in the plasma membrane ofall animal cells where it serves as the principal regulator of intracellularion homeostasis. Na+, K+-ATPase is responsible for generating andmaintaining transmembrane ionic gradients that are of vital importance forcellular function and subservient activities such as volume regulation, pHmaintenance, and generation of action potentials and secondary activetransport. The diversity of Na+, K+-ATPase subunit isoforms andtheir complex spatial and temporal patterns of cellular expression suggestthat Na+, K+-ATPase isozymes perform specialized physiologicalfunctions. Recent studies have shown that the α subunit isoformspossess considerably different kinetic properties and modes of regulationand the β subunit isoforms modulate the activity, expression and plasmamembrane targeting of Na+, K+-ATPase isozymes. This review focuseson recent developments in Na+, K+-ATPase research, and in particular reportsof expression of isoforms in various tissues and experiments aimed atelucidating the intrinsic structural features of isoforms important forNa+, K+-ATPase function.
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Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNA
Riordan, J. R., Rommens, J. M., Kerem, B.-S., Alon, N., Rozmahel, R., Grzelczak, Z., Zielenski, J., Lok, S., Plavsic, N., Chou, J.-L., et al. (1989) · Science · doi:10.1126/science.2475911 · Cited by 7,418
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Endogenous Cardiotonic Steroids: Physiology, Pharmacology, and Novel Therapeutic Targets
Bagrov, A. Y., Shapiro, J. I., & Fedorova, O. V. (2009) · Pharmacological Reviews · doi:10.1124/pr.108.000711 · Cited by 532
Vanmolkot, K. R. J., Kors, E. E., Hottenga, J., Terwindt, G. M., Haan, J., Hoefnagels, W. A. J., Black, D. F., Sandkuijl, L. A., Frants, R. R., Ferrari, M. D., et al. (2003) · Annals of Neurology · doi:10.1002/ana.10674 · Cited by 360
Richards, J. G., Semple, J. W., Bystriansky, J. S., & Schulte, P. M. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00701 · Cited by 358
Cardiotonic steroids on the road to anti-cancer therapy
Mijatovic, T., Van Quaquebeke, E., Delest, B., Debeir, O., Darro, F., & Kiss, R. (2007) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2007.06.002 · Cited by 317
Metadata
- Authors
- Mobasheri, A., Avila, J., Cózar-Castellano, I., Brownleader, M. D., Trevan, M., Francis, M. J. O., Lamb, J. F., & Martín-Vasallo, P.
- Venue
- Bioscience Reports
- Publisher
- Portland Press Ltd.
- Published
- 2000-04-01
- Volume
- 20
- Issue
- 2
- Pages
- 51-91
- ISSN
- 0144-8463 (ISSN-L)
- 1573-4935
- OpenAlex
- W165193783
- Cited by
- 331
- References
- 1
- FWCI
- 3.60
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Na+, K+-ATPase Isozyme Diversity; Comparative Biochemistry and Physiological Implications of Novel Functional Interactions. https://app.cochat.ai/papers/10.1023/a:1005580332144
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- Mobasheri, A., Avila, J., Cózar-Castellano, I., Brownleader, M. D., Trevan, M., Francis, M. J. O., Lamb, J. F., & Martín-Vasallo, P. (2000). Na+, K+-ATPase Isozyme Diversity; Comparative Biochemistry and Physiological Implications of Novel Functional Interactions. Bioscience Reports. https://doi.org/10.1023/a%3A1005580332144
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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