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Radzyukevich, T. L., Lingrel, J. B, Heiny, J. A. (2009) The cardiac glycoside binding site on the Na,K-ATPase α2 isoform plays a role in the dynamic regulation of active transport in skeletal muscle. Proceedings of the National Academy of Sciences, 106 (8) 2565-2570 doi:10.1073/pnas.0804150106

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Reference TypeJournal (article/letter/editorial)
TitleThe cardiac glycoside binding site on the Na,K-ATPase α2 isoform plays a role in the dynamic regulation of active transport in skeletal muscle
JournalProceedings of the National Academy of Sciences
AuthorsRadzyukevich, T. L.Author
Lingrel, J. BAuthor
Heiny, J. A.Author
Year2009 (February 24)Volume106
Issue8
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0804150106Search in ResearchGate
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Mindat Ref. ID1772617Long-form Identifiermindat:1:5:1772617:3
GUID0
Full ReferenceRadzyukevich, T. L., Lingrel, J. B, Heiny, J. A. (2009) The cardiac glycoside binding site on the Na,K-ATPase α2 isoform plays a role in the dynamic regulation of active transport in skeletal muscle. Proceedings of the National Academy of Sciences, 106 (8) 2565-2570 doi:10.1073/pnas.0804150106
Plain TextRadzyukevich, T. L., Lingrel, J. B, Heiny, J. A. (2009) The cardiac glycoside binding site on the Na,K-ATPase α2 isoform plays a role in the dynamic regulation of active transport in skeletal muscle. Proceedings of the National Academy of Sciences, 106 (8) 2565-2570 doi:10.1073/pnas.0804150106
In(2009, February) Proceedings of the National Academy of Sciences Vol. 106 (8) Proceedings of the National Academy of Sciences

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Dostanic-Larson, I., Van Huysse, J. W., Lorenz, J. N., Lingrel, J. B (2005) From The Cover: The highly conserved cardiac glycoside binding site of Na,K-ATPase plays a role in blood pressure regulation. Proceedings of the National Academy of Sciences, 102 (44) 15845-15850 doi:10.1073/pnas.0507358102
Kaplan, J. H. (2005) The sodium pump and hypertension: A physiological role for the cardiac glycoside binding site of the Na,K-ATPase. Proceedings of the National Academy of Sciences, 102 (44) 15723-15724 doi:10.1073/pnas.0507965102
Shamraj, O. I., Lingrel, J. B. (1994) A putative fourth Na+,K(+)-ATPase alpha-subunit gene is expressed in testis. Proceedings of the National Academy of Sciences, 91 (26) 12952-12956 doi:10.1073/pnas.91.26.12952
Shull, M. M., Lingrel, J. B. (1987) Multiple genes encode the human Na+,K+-ATPase catalytic subunit. Proceedings of the National Academy of Sciences, 84 (12) 4039-4043 doi:10.1073/pnas.84.12.4039
LINGREL, JERRY B, ARGÜELLO, JOSÉ M., HUYSSE, JAMES, KUNTZWEILER, THERESA A. (1997) Cation and Cardiac Glycoside Binding Sites of the Na,K-ATPase. Annals of the New York Academy of Sciences, 834 (1) 194-206 doi:10.1111/j.1749-6632.1997.tb52251.x
Hakimjavadi, Hesamedin, Stiner, Cory, Radzyukevich, Tatiana, Lingrel, Jerry, Norman, Natalie, Landero Figueroa, Julio, Heiny, Judith (2018) K+ and Rb+ Affinities of the Na,K-ATPase α1 and α2 Isozymes: An Application of ICP-MS for Quantification of Na+ Pump Kinetics in Myofibers. International Journal of Molecular Sciences, 19. 2725pp. doi:10.3390/ijms19092725
Parker, T G, Chow, K L, Schwartz, R J, Schneider, M D (1990) Differential regulation of skeletal alpha-actin transcription in cardiac muscle by two fibroblast growth factors. Proceedings of the National Academy of Sciences, 87 (18) 7066-7070 doi:10.1073/pnas.87.18.7066
Hall, C., Ruoho, A. (1980) Ouabain-binding-site photoaffinity probes that label both subunits of Na+,K+-ATPase. Proceedings of the National Academy of Sciences, 77 (8) 4529-4533 doi:10.1073/pnas.77.8.4529
Bao, J., Oishi, K., Yamada, T., Liu, L., Nakamura, A., Uchida, M. K., Kohama, K. (2002) Role of the short isoform of myosin light chain kinase in the contraction of cultured smooth muscle cells as examined by its down-regulation. Proceedings of the National Academy of Sciences, 99 (14) 9556-9561 doi:10.1073/pnas.142298599
Johnson, J. H., Crider, B. P. (1989) Increases in Na+,K+-ATPase activity of erythrocytes and skeletal muscle after chronic ethanol consumption: evidence for reduced efficiency of the enzyme. Proceedings of the National Academy of Sciences, 86 (20) 7857-7860 doi:10.1073/pnas.86.20.7857
Clapcote, S. J., Duffy, S., Xie, G., Kirshenbaum, G., Bechard, A. R., Rodacker Schack, V., Petersen, J., Sinai, L., Saab, B. J., Lerch, J. P., Minassian, B. A., Ackerley, C. A., Sled, J. G., Cortez, M. A., Henderson, J. T., Vilsen, B., Roder, J. C. (2009) Mutation I810N in the  3 isoform of Na+,K+-ATPase causes impairments in the sodium pump and hyperexcitability in the CNS. Proceedings of the National Academy of Sciences, 106 (33) 14085-14090 doi:10.1073/pnas.0904817106
 
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