rdf:type |
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lifeskim:mentions |
umls-concept:C0035820,
umls-concept:C0086376,
umls-concept:C0439799,
umls-concept:C0521390,
umls-concept:C0596235,
umls-concept:C1514562,
umls-concept:C1709059,
umls-concept:C1711351,
umls-concept:C1879647,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:dateCreated |
1998-7-16
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pubmed:databankReference |
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pubmed:abstractText |
1. We studied the G protein inhibition of heteromultimeric neuronal Ca2+ channels by constructing a series of chimeric channels between the strongly modulated alpha1B subunit and the alpha1E(rbEII) subunit, which showed no modulation. 2. In parallel studies, alpha1 subunit constructs were co-expressed together with the accessory Ca2+ channel alpha2-delta and beta2a subunits in mammalian (COS-7) cells and Xenopus oocytes. G protein inhibition of expressed Ca2+ channel currents was induced by co-transfection of Gbeta1 and Ggamma2 subunits in COS-7 cells or activation of co-expressed dopamine (D2) receptors by quinpirole (100 nM) in oocytes. 3. The data indicate that transfer of the alpha1B region containing the N-terminal, domain I and the I-II loop (i.e. the alpha1B1-483 sequence), conferred G protein modulation on alpha1E(rbEII), both in terms of a slowing of activation kinetics and a reduction in current amplitude. 4. In contrast, the data are not consistent with the I-II loop and/or the C-terminal forming a unique site for G protein modulation.
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pubmed:grant |
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-7544301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-7761832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-7969428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-7993634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-8388125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-8637575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-8637576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-8643659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-8756429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-8938130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9006976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9009192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9009193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9037084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9238069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9284307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9481669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547390-9547377
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-3751
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
509 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
163-9
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pubmed:dateRevised |
2010-8-25
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pubmed:meshHeading |
pubmed-meshheading:9547390-Animals,
pubmed-meshheading:9547390-Calcium Channels,
pubmed-meshheading:9547390-Cattle,
pubmed-meshheading:9547390-Cell Line,
pubmed-meshheading:9547390-Electric Stimulation,
pubmed-meshheading:9547390-Electrophysiology,
pubmed-meshheading:9547390-GTP-Binding Proteins,
pubmed-meshheading:9547390-Membrane Potentials,
pubmed-meshheading:9547390-Molecular Sequence Data,
pubmed-meshheading:9547390-Neurons,
pubmed-meshheading:9547390-Oocytes,
pubmed-meshheading:9547390-Patch-Clamp Techniques,
pubmed-meshheading:9547390-Rabbits,
pubmed-meshheading:9547390-Rats,
pubmed-meshheading:9547390-Transfection,
pubmed-meshheading:9547390-Xenopus laevis
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pubmed:year |
1998
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pubmed:articleTitle |
Role of domain I of neuronal Ca2+ channel alpha1 subunits in G protein modulation.
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pubmed:affiliation |
Department of Pharmacology, University College London, London WC1E 6BT, UK. g.stephens@ucl.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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