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Hanke, W., Cook, N. J., Kaupp, U. B. (1988) cGMP-dependent channel protein from photoreceptor membranes: single-channel activity of the purified and reconstituted protein. Proceedings of the National Academy of Sciences, 85 (1) 94-98 doi:10.1073/pnas.85.1.94

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Reference TypeJournal (article/letter/editorial)
TitlecGMP-dependent channel protein from photoreceptor membranes: single-channel activity of the purified and reconstituted protein.
JournalProceedings of the National Academy of Sciences
AuthorsHanke, W.Author
Cook, N. J.Author
Kaupp, U. B.Author
Year1988 (January 1)Volume85
Issue1
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.85.1.94Search in ResearchGate
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Mindat Ref. ID1465467Long-form Identifiermindat:1:5:1465467:1
GUID0
Full ReferenceHanke, W., Cook, N. J., Kaupp, U. B. (1988) cGMP-dependent channel protein from photoreceptor membranes: single-channel activity of the purified and reconstituted protein. Proceedings of the National Academy of Sciences, 85 (1) 94-98 doi:10.1073/pnas.85.1.94
Plain TextHanke, W., Cook, N. J., Kaupp, U. B. (1988) cGMP-dependent channel protein from photoreceptor membranes: single-channel activity of the purified and reconstituted protein. Proceedings of the National Academy of Sciences, 85 (1) 94-98 doi:10.1073/pnas.85.1.94
In(1988, January) Proceedings of the National Academy of Sciences Vol. 85 (1) Proceedings of the National Academy of Sciences

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Cook, N. J., Hanke, W., Kaupp, U. B. (1987) Identification, purification, and functional reconstitution of the cyclic GMP-dependent channel from rod photoreceptors. Proceedings of the National Academy of Sciences, 84 (2) 585-589 doi:10.1073/pnas.84.2.585
Clack, J. W., Stein, P. J. (1988) Opsin exhibits cGMP-activated single-channel activity. Proceedings of the National Academy of Sciences, 85 (24) 9806-9810 doi:10.1073/pnas.85.24.9806
Matthews, G. (1987) Single-channel recordings demonstrate that cGMP opens the light-sensitive ion channel of the rod photoreceptor. Proceedings of the National Academy of Sciences, 84 (1) 299-302 doi:10.1073/pnas.84.1.299
Weigele, J. B., Barchi, R. L. (1982) Functional reconstitution of the purified sodium channel protein from rat sarcolemma. Proceedings of the National Academy of Sciences, 79 (11) 3651-3655 doi:10.1073/pnas.79.11.3651
(1988) Channel protein engineering: Synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers. Proceedings of the National Academy of Sciences, 85 (14) 5343 doi:10.1073/pnas.85.14.5343
Tank, D. W., Huganir, R. L., Greengard, P., Webb, W. W. (1983) Patch-recorded single-channel currents of the purified and reconstituted Torpedo acetylcholine receptor. Proceedings of the National Academy of Sciences, 80 (16) 5129-5133 doi:10.1073/pnas.80.16.5129
Eismann, E., Muller, F., Heinemann, S. H., Kaupp, U. B. (1994) A single negative charge within the pore region of a cGMP-gated channel controls rectification, Ca2+ blockage, and ionic selectivity. Proceedings of the National Academy of Sciences, 91 (3) 1109-1113 doi:10.1073/pnas.91.3.1109
Oiki, S., Danho, W., Montal, M. (1988) Channel protein engineering: synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers. Proceedings of the National Academy of Sciences, 85 (7) 2393-2397 doi:10.1073/pnas.85.7.2393
Pohl, P., Saparov, S. M., Borgnia, M. J., Agre, P. (2001) Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ. Proceedings of the National Academy of Sciences, 98 (17) 9624-9629 doi:10.1073/pnas.161299398
Burt, J. M., Spray, D. C. (1988) Single-channel events and gating behavior of the cardiac gap junction channel. Proceedings of the National Academy of Sciences, 85 (10) 3431-3434 doi:10.1073/pnas.85.10.3431
Jazwinski, S. M. (1988) CDC7-dependent protein kinase activity in yeast replicative-complex preparations. Proceedings of the National Academy of Sciences, 85 (7) 2101-2105 doi:10.1073/pnas.85.7.2101
 
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