| pubmed-article:9855309 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9855309 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:9855309 | lifeskim:mentions | umls-concept:C0002736 | lld:lifeskim |
| pubmed-article:9855309 | lifeskim:mentions | umls-concept:C0241888 | lld:lifeskim |
| pubmed-article:9855309 | lifeskim:mentions | umls-concept:C0037473 | lld:lifeskim |
| pubmed-article:9855309 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:9855309 | lifeskim:mentions | umls-concept:C0521116 | lld:lifeskim |
| pubmed-article:9855309 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:9855309 | pubmed:dateCreated | 1999-2-25 | lld:pubmed |
| pubmed-article:9855309 | pubmed:abstractText | The whole-cell configuration of the patch-clamp recording was used to study the voltage-dependent Na+ currents in a model system for the familial form of amyotrophic lateral sclerosis (ALS) associated with mutations in Cu,Zn superoxide dismutase. Here we report that the amplitude of voltage-gated Na+ currents is significantly reduced in cell lines expressing mutant Cu,Zn superoxide dismutase G93A when compared with the parental, untransfected cell line and to a cell line expressing the wild-type enzyme. This effect is associated with a shift toward positive values of the steady-state inactivation curve of the Na+ currents. These results indicate that expression of a Cu,Zn superoxide dismutase typical of patients affect with familial ALS influence the functionality of the voltage-dependent Na+ channels; this effect may contribute to the pathogenesis of the disease. | lld:pubmed |
| pubmed-article:9855309 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9855309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9855309 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9855309 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9855309 | pubmed:issn | 0959-4965 | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:RotilioGG | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:BernardiGG | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:FerriAA | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:MercuriN BNB | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:GabbianelliRR | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:ZonaCC | lld:pubmed |
| pubmed-article:9855309 | pubmed:author | pubmed-author:CarriM TMT | lld:pubmed |
| pubmed-article:9855309 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9855309 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:9855309 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:9855309 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9855309 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9855309 | pubmed:pagination | 3515-8 | lld:pubmed |
| pubmed-article:9855309 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
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| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
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| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
| pubmed-article:9855309 | pubmed:meshHeading | pubmed-meshheading:9855309-... | lld:pubmed |
| pubmed-article:9855309 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9855309 | pubmed:articleTitle | Voltage-activated sodium currents in a cell line expressing a Cu,Zn superoxide dismutase typical of familial ALS. | lld:pubmed |
| pubmed-article:9855309 | pubmed:affiliation | Dipartimento di Neuroscienze, Università di Roma Tor Vergata, Rome, Italy. | lld:pubmed |
| pubmed-article:9855309 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9855309 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9855309 | lld:pubmed |
