| pubmed-article:16968776 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:16968776 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:16968776 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:16968776 | pubmed:dateCreated | 2006-9-20 | lld:pubmed |
| pubmed-article:16968776 | pubmed:abstractText | The hydrolysis of nucleoside triphosphates by enzymes is used as a regulation mechanism in key biological processes. Here, the GTP hydrolysis of the protein complex of Ras with its GTPase-activating protein is monitored at atomic resolution in a noncrystalline state by time-resolved FTIR spectroscopy. At 900 ms, after the attack of water at the gamma-phosphate, there appears a H2PO4- intermediate that is shown to be hydrogen-bonded in an eclipsed conformation to the beta-phosphate of GDP. The H2PO4- intermediate is in a position where it can either reform GTP or be released from the protein in 7 s in the rate-limiting step of the GTPase reaction. We propose that such an intermediate also occurs in other GTPases and ATPases. | lld:pubmed |
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| pubmed-article:16968776 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16968776 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16968776 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16968776 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16968776 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16968776 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16968776 | pubmed:author | pubmed-author:WittinghoferA... | lld:pubmed |
| pubmed-article:16968776 | pubmed:author | pubmed-author:GoodyRoger... | lld:pubmed |
| pubmed-article:16968776 | pubmed:author | pubmed-author:KöttingCarste... | lld:pubmed |
| pubmed-article:16968776 | pubmed:author | pubmed-author:GerwertKlausK | lld:pubmed |
| pubmed-article:16968776 | pubmed:author | pubmed-author:SuveyzdisYanY | lld:pubmed |
| pubmed-article:16968776 | pubmed:author | pubmed-author:BlessenohlMar... | lld:pubmed |
| pubmed-article:16968776 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16968776 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:16968776 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16968776 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16968776 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16968776 | pubmed:pagination | 13911-6 | lld:pubmed |
| pubmed-article:16968776 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16968776 | pubmed:meshHeading | pubmed-meshheading:16968776... | lld:pubmed |
| pubmed-article:16968776 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16968776 | pubmed:articleTitle | A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein. | lld:pubmed |
| pubmed-article:16968776 | pubmed:affiliation | Lehrstuhl für Biophysik and Institut für Physiologische Chemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany. | lld:pubmed |
| pubmed-article:16968776 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16968776 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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