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NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1

Wissmann, R. and Baukrowitz, T. and Kalbacher, H. and Kalbitzer, Hans Robert and Ruppersberg, J. P. and Pongs, O. and Antz, C. and Fakler, B. (1999) NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. The Journal of biological chemistry 274 (50), pp. 35521-35525.

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Abstract

Rapid N-type inactivation of voltage-dependent potassium (Kv) channels controls membrane excitability and signal propagation in central neurons and is mediated by protein domains (inactivation gates) occluding the open channel pore from the cytoplasmic side. Inactivation domains (ID) are donated either by the pore-forming alpha-subunit or certain auxiliary beta-subunits. Upon coexpression, ...

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Item Type:Article
Date:1999
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
10585425PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
AnimalsMESH
Binding SitesMESH
FemaleMESH
Kv1.1 Potassium ChannelMESH
Membrane Potentials/physiologyMESH
Molecular Sequence DataMESH
Nuclear Magnetic Resonance, Biomolecular/methodsMESH
Oocytes/physiologyMESH
Peptide Fragments/metabolismMESH
Potassium Channels/physiologyMESH
Potassium Channels, Voltage-GatedMESH
Recombinant Proteins/metabolismMESH
Tetraethylammonium/pharmacologyMESH
Xenopus laevisMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 08:08
Last Modified:13 Sep 2010 08:08
Item ID:16557
Owner Only: item control page
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