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(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

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Reference TypeJournal (article/letter/editorial)
TitleChannel protein engineering: Synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers
JournalProceedings of the National Academy of Sciences
Year1988 (July 1)Volume85
Issue14
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.85.14.5343Search in ResearchGate
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Mindat Ref. ID1467257Long-form Identifiermindat:1:5:1467257:0
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Full Reference(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
Plain Text(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
In(1988, July) Proceedings of the National Academy of Sciences Vol. 85 (14) Proceedings of the National Academy of Sciences

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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
Schindler, H., Rosenbusch, J. P. (1978) Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proceedings of the National Academy of Sciences, 75 (8) 3751-3755 doi:10.1073/pnas.75.8.3751
Tosteson, M. T., Auld, D. S., Tosteson, D. C. (1989) Voltage-gated channels formed in lipid bilayers by a positively charged segment of the Na-channel polypeptide. Proceedings of the National Academy of Sciences, 86 (2) 707-710 doi:10.1073/pnas.86.2.707
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
Oiki, S., Danho, W., Madison, V., Montal, M. (1988) M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Proceedings of the National Academy of Sciences, 85 (22) 8703-8707 doi:10.1073/pnas.85.22.8703
Mauro, A., Blake, M., Labarca, P. (1988) Voltage gating of conductance in lipid bilayers induced by porin from outer membrane of Neisseria gonorrhoeae. Proceedings of the National Academy of Sciences, 85 (4) 1071-1075 doi:10.1073/pnas.85.4.1071
Pollard, H. B., Rojas, E. (1988) Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes. Proceedings of the National Academy of Sciences, 85 (9) 2974-2978 doi:10.1073/pnas.85.9.2974
Ismailov, I. I., Shlyonsky, V. G., Benos, D. J. (1997) Streaming potential measurements in    -rat epithelial Na+ channel in planar lipid bilayers. Proceedings of the National Academy of Sciences, 94 (14) 7651-7654 doi:10.1073/pnas.94.14.7651
Tejedor, F. J., Catterall, W. A. (1988) Site of covalent attachment of alpha-scorpion toxin derivatives in domain I of the sodium channel alpha subunit. Proceedings of the National Academy of Sciences, 85 (22) 8742-8746 doi:10.1073/pnas.85.22.8742
(1988) Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence. Proceedings of the National Academy of Sciences, 85 (14) 5056 doi:10.1073/pnas.85.14.5056
Hartshorne, R. P., Keller, B. U., Talvenheimo, J. A., Catterall, W. A., Montal, M. (1985) Functional reconstitution of the purified brain sodium channel in planar lipid bilayers. Proceedings of the National Academy of Sciences, 82 (1) 240-244 doi:10.1073/pnas.82.1.240
 
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