| pubmed-article:16307476 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16307476 | lifeskim:mentions | umls-concept:C0150369 | lld:lifeskim |
| pubmed-article:16307476 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:16307476 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16307476 | lifeskim:mentions | umls-concept:C0018321 | lld:lifeskim |
| pubmed-article:16307476 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:16307476 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:16307476 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:16307476 | pubmed:dateCreated | 2005-11-25 | lld:pubmed |
| pubmed-article:16307476 | pubmed:abstractText | The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi) by guanine nucleotide-binding proteins (GNBPs) is a fundamental enzyme reaction in living cells that acts as an important timer in a variety of biological processes. This reaction is intrinsically slow but can be stimulated by GTPase-activating proteins (GAPs) by several orders of magnitude. In the present study, we synthesized and characterized a new fluorescent nucleotide, 2'(3')-O-(N-ethylcarbamoyl-(5''-carboxytetramethylrhodamine) amide)-GTP, or tamraGTP, which is sensitive towards conformational changes of certain GNBPs induced by GTP hydrolysis. Unlike other fluorescent nucleotides, tamra-GTP allows real-time monitoring of the kinetics of the intrinsic and GAP-catalyzed GTP hydrolysis reactions of small GNBPs from the Rho family. | lld:pubmed |
| pubmed-article:16307476 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16307476 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16307476 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16307476 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16307476 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16307476 | pubmed:issn | 1431-6730 | lld:pubmed |
| pubmed-article:16307476 | pubmed:author | pubmed-author:AhmadianMoham... | lld:pubmed |
| pubmed-article:16307476 | pubmed:author | pubmed-author:GoodyRoger... | lld:pubmed |
| pubmed-article:16307476 | pubmed:author | pubmed-author:DvorskyRadova... | lld:pubmed |
| pubmed-article:16307476 | pubmed:author | pubmed-author:BeckerChristi... | lld:pubmed |
| pubmed-article:16307476 | pubmed:author | pubmed-author:EberthAlexand... | lld:pubmed |
| pubmed-article:16307476 | pubmed:author | pubmed-author:BesteAndreaA | lld:pubmed |
| pubmed-article:16307476 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16307476 | pubmed:volume | 386 | lld:pubmed |
| pubmed-article:16307476 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16307476 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16307476 | pubmed:pagination | 1105-14 | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:meshHeading | pubmed-meshheading:16307476... | lld:pubmed |
| pubmed-article:16307476 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16307476 | pubmed:articleTitle | Monitoring the real-time kinetics of the hydrolysis reaction of guanine nucleotide-binding proteins. | lld:pubmed |
| pubmed-article:16307476 | pubmed:affiliation | Department of Structural Biology, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany. | lld:pubmed |
| pubmed-article:16307476 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16307476 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16307476 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16307476 | lld:pubmed |
