| pubmed-article:1661143 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C0020731 | lld:lifeskim |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C0028630 | lld:lifeskim |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C0018338 | lld:lifeskim |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C0031640 | lld:lifeskim |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C0040663 | lld:lifeskim |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:1661143 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1661143 | pubmed:issue | 50 | lld:pubmed |
| pubmed-article:1661143 | pubmed:dateCreated | 1992-1-30 | lld:pubmed |
| pubmed-article:1661143 | pubmed:abstractText | Transducin, the signal coupling protein of retinal rod photoreceptor cells, is one of a family of G proteins that can be inactivated by pertussis toxin. We have investigated the nature of this inactivation in order to determine (1) whether it requires the toxin-catalyzed transfer of ADP-ribose from NAD+ to cysteine-347 of the alpha subunit and (2) whether it involves locking the alpha subunit in the inactive conformation characteristic of its GDP-bound state, or is limited to disruption of binding to photoexcited rhodopsin (R*). Our results indicate that all observed effects of pertussis toxin treatment, including a shift in the electrophoretic mobility of transducin's alpha subunit and functional inactivation, require NAD+ and that the appearance of the shift parallels incorporation of ADP-ribose. We have also found that, apart from interactions with photoexcited rhodopsin, the functional properties of ADP-ribosylated transducin are essentially the same as those of unmodified transducin. Normal spontaneous nucleotide exchange kinetics and the ability to activate cGMP phosphodiesterase are preserved following quantitative ADP-ribosylation, as are the abilities to hydrolyze GTP, to bind to a dye affinity column, and to display enhanced fluorescence upon addition of Al3+ and F-. Thus, ADP-ribosylation merely blocks catalysis of transducin nucleotide exchange by R* and does not lock transducin in an inactive state.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
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| pubmed-article:1661143 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1661143 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1661143 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1661143 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1661143 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1661143 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1661143 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1661143 | pubmed:author | pubmed-author:WenselT GTG | lld:pubmed |
| pubmed-article:1661143 | pubmed:author | pubmed-author:DisherR MRM | lld:pubmed |
| pubmed-article:1661143 | pubmed:author | pubmed-author:RamdasLL | lld:pubmed |
| pubmed-article:1661143 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1661143 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:1661143 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:1661143 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1661143 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1661143 | pubmed:pagination | 11637-45 | lld:pubmed |
| pubmed-article:1661143 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:1661143 | pubmed:meshHeading | pubmed-meshheading:1661143-... | lld:pubmed |
| pubmed-article:1661143 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1661143 | pubmed:articleTitle | Nucleotide exchange and cGMP phosphodiesterase activation by pertussis toxin inactivated transducin. | lld:pubmed |
| pubmed-article:1661143 | pubmed:affiliation | Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030. | lld:pubmed |
| pubmed-article:1661143 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1661143 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1661143 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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