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  • 1
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    Calcium-binding site properties in calmodulin [Biophysics and Computational Biology] (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-03-02
    Description: Calmodulin (CaM) is a Ca2+-sensing protein that is highly conserved and ubiquitous in eukaryotes. In humans it is a locus of life-threatening cardiomyopathies. The primary function of CaM is to transduce Ca2+ concentration into cellular signals by binding to a wide range of target proteins in a Ca2+-dependent manner. We...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    Electrostatic influences of charged inner pore residues on the conductance and gating of small conductance Ca2+ activated K+ channels [Biophysics and Computational Biology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-04-13
    Description: SK channels underlie important physiological functions by linking calcium signaling with neuronal excitability. Potassium currents through SK channels demonstrate inward rectification, which further reduces their small outward conductance. Although it has been generally attributed to block of outward current by intracellular divalent ions, we find that inward rectification is in fact an intrinsic property of SK channels independent of intracellular blockers. We identified three charged residues in the S6 transmembrane domain of SK channels near the inner mouth of the pore that collectively control the conductance and rectification through an electrostatic mechanism. Additionally, electrostatic contributions from these residues also play an important role in determining the intrinsic open probability of SK channels in the absence of Ca2+, affecting the apparent Ca2+ affinity for activation.
    Keywords: Inaugural Articles
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 3
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    LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-07-09
    Description: Large-conductance, voltage- and calcium-activated potassium (BK, or K(Ca)1.1) channels are ubiquitously expressed in electrically excitable and non-excitable cells, either as alpha-subunit (BKalpha) tetramers or together with tissue specific auxiliary beta-subunits (beta1-beta4). Activation of BK channels typically requires coincident membrane depolarization and elevation in free cytosolic Ca(2+) concentration ([Ca(2+)](i)), which are not physiological conditions for most non-excitable cells. Here we present evidence that in non-excitable LNCaP prostate cancer cells, BK channels can be activated at negative voltages without rises in [Ca(2+)](i) through their complex with an auxiliary protein, leucine-rich repeat (LRR)-containing protein 26 (LRRC26). LRRC26 modulates the gating of a BK channel by enhancing the allosteric coupling between voltage-sensor activation and the channel's closed-open transition. This finding reveals a novel auxiliary protein of a voltage-gated ion channel that gives an unprecedentedly large negative shift ( approximately -140 mV) in voltage dependence and provides a molecular basis for activation of BK channels at physiological voltages and calcium levels in non-excitable cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, Jiusheng -- Aldrich, Richard W -- England -- Nature. 2010 Jul 22;466(7305):513-6. doi: 10.1038/nature09162. Epub 2010 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Center for Learning and Memory, University of Texas, Austin, Texas 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20613726" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; *Calcium/analysis ; Cell Line, Tumor ; Humans ; Ion Channel Gating/*physiology ; Large-Conductance Calcium-Activated Potassium Channels/genetics/*metabolism ; Male ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Neoplasm Proteins/chemistry/genetics/*metabolism ; Prostatic Neoplasms/metabolism ; Rats
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Biophysical and molecular mechanisms of Shaker potassium channel inactivation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: The potassium channels encoded by the Drosophila Shaker gene activate and inactivate rapidly when the membrane potential becomes more positive. Site-directed mutagenesis and single-channel patch-clamp recording were used to explore the molecular transitions that underlie inactivation in Shaker potassium channels expressed in Xenopus oocytes. A region near the amino terminus with an important role in inactivation has now been identified. The results suggest a model where this region forms a cytoplasmic domain that interacts with the open channel to cause inactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, T -- Zagotta, W N -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):533-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University, School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2122519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Drosophila melanogaster/*genetics ; Electric Conductivity ; Ion Channel Gating/drug effects/*physiology ; Kinetics ; Membrane Potentials/physiology ; Molecular Sequence Data ; Mutagenesis ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Potassium Channels/genetics/*physiology ; RNA Splicing ; Structure-Activity Relationship ; Trypsin/pharmacology ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: Site-directed mutagenesis experiments have suggested a model for the inactivation mechanism of Shaker potassium channels from Drosophila melanogaster. In this model, the first 20 amino acids form a cytoplasmic domain that interacts with the open channel to cause inactivation. The model was tested by the internal application of a synthetic peptide, with the sequence of the first 20 residues of the ShB alternatively spliced variant, to noninactivating mutant channels expressed in Xenopus oocytes. The peptide restored inactivation in a concentration-dependent manner. Like normal inactivation, peptide-induced inactivation was not noticeably voltage-dependent. Trypsin-treated peptide and peptides with sequences derived from the first 20 residues of noninactivating mutants did not restore inactivation. These results support the proposal that inactivation occurs by a cytoplasmic domain that occludes the ion-conducting pore of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zagotta, W N -- Hoshi, T -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2122520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Drosophila melanogaster/*genetics ; Electric Conductivity ; Hot Temperature ; Ion Channel Gating/drug effects/*physiology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Peptide Fragments/chemistry/*pharmacology ; Potassium Channels/chemistry/genetics/*physiology ; Structure-Activity Relationship ; Trypsin/pharmacology ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Functional stoichiometry of Shaker potassium channel inactivation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-29
    Description: Shaker potassium channels from Drosophila are composed of four identical subunits. The contribution of a single subunit to the inactivation gating transition was investigated. Channels carrying a specific mutation in a single subunit can be labeled in a heterogeneous population and studied quantitatively with scorpion toxin sensitivity as a selection tag. Linkage within a single subunit of a mutation that removes the inactivation gate to a second mutation that affects scorpion toxin sensitivity demonstrates that only a single gate is necessary to produce inactivation. The inactivation rate constant for channels with a single gate was one-fourth that of channels with four gates. In contrast, the rate of recovery from inactivation was independent of the number of gates. It appears that each of the four open inactivation gates in a Shaker potassium channel is independent, but only one of the four gates closes in a mutually exclusive manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacKinnon, R -- Aldrich, R W -- Lee, A W -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 29;262(5134):757-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694359" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Charybdotoxin ; Drosophila ; Ion Channel Gating/drug effects/genetics/*physiology ; Models, Biological ; Mutagenesis, Site-Directed ; Potassium Channels/drug effects/genetics/*physiology ; Scorpion Venoms/pharmacology ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    Single-channel and genetic analyses reveal two distinct A-type potassium channels in Drosophila (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-29
    Description: Whole-cell and single-channel voltage-clamp techniques were used to identify and characterize the channels underlying the fast transient potassium current (A current) in cultured myotubes and neurons of Drosophila. The myotube (A1) and neuronal (A2) channels are distinct, differing in conductance, voltage dependence, and gating kinetics. The myotube currents have a faster and more voltage-dependent macroscopic inactivation rate, a larger steady-state component, and a less negative steady-state inactivation curve than the neuronal currents. The myotube channels have a conductance of 12 to 16 picosiemens, whereas the neuronal channels have a conductance of 5 to 8 picosiemens. In addition, the myotube channel is affected by Shaker mutations, whereas the neuronal channel is not. Together, these data suggest that the two channels are separate molecular structures, the expression of which is controlled, at least in part, by different genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Solc, C K -- Zagotta, W N -- Aldrich, R W -- NS 07158-07/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 29;236(4805):1094-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2437657" target="_blank"〉PubMed〈/a〉
    Keywords: Drosophila/*genetics/metabolism ; Electrophysiology ; Ion Channels/*metabolism ; Muscles/metabolism ; Mutation ; Neurons/metabolism ; Potassium/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Effect of forskolin on voltage-gated K+ channels is independent of adenylate cyclase activation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Forskolin is commonly used to stimulate adenylate cyclase in the study of modulation of ion channels and other proteins by adenosine 3',5'-monophosphate (cAMP)-dependent second messenger systems. In addition to its action on adenylate cyclase, forskolin directly alters the gating of a single class of voltage-dependent potassium channels from a clonal pheochromocytoma (PC12) cell line. This alteration occurred in isolated cell-free patches independent of soluble cytoplasmic enzymes. The effect of forskolin was distinct from those of other agents that raise intracellular cAMP levels. The 1,9-dideoxy derivative of forskolin, which is unable to activate the cyclase, was also effective in altering the potassium channel activity. This direct action of forskolin can lead to misinterpretation of results in experiments in which forskolin is assumed to selectively activate adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, T -- Garber, S S -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University, School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2454506" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Adenylyl Cyclases/*metabolism ; Adrenal Gland Neoplasms/metabolism ; Colforsin/analogs & derivatives/*pharmacology ; Cyclic AMP/metabolism ; Electric Conductivity ; Enzyme Activation/drug effects ; Ion Channels/drug effects/*physiology ; Kinetics ; Pheochromocytoma/metabolism ; Potassium/*metabolism ; Theophylline/pharmacology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
    Electronic Resource
    Electronic Resource
    A reinterpretation of mammalian sodium channel gating based on single channel recording (1983)
    [s.l.] : Nature Publishing Group
    Nature 306 (1983), S. 436-441 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Some of the traditionally held views about how sodium channels work are shown to be incorrect and a new approach to physical theories of sodium channel operation is ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/306436a0
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    Paper (German National Licenses)
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  • 10
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    Alternatively spliced domains interact to regulate BK potassium channel gating (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-11-02
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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