| pubmed-article:14580569 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14580569 | lifeskim:mentions | umls-concept:C0039421 | lld:lifeskim |
| pubmed-article:14580569 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:14580569 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:14580569 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:14580569 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:14580569 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:14580569 | pubmed:dateCreated | 2003-10-28 | lld:pubmed |
| pubmed-article:14580569 | pubmed:abstractText | Biophotonics techniques, especially those involving fluorescence, are widely used in proteomics to characterize the in vitro interactions between proteins in high-throughput mode. On the other hand, fluorescence-based imaging studies often show that protein activity is regulated through large protein complexes that transiently form at specific sites in the cell. One could therefore argue that a systematic functional analysis of the human proteome requires technologies that are capable of time and spatially resolved, multiplexed analysis of protein interactions within cells. | lld:pubmed |
| pubmed-article:14580569 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14580569 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14580569 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14580569 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14580569 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14580569 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14580569 | pubmed:issn | 1367-5931 | lld:pubmed |
| pubmed-article:14580569 | pubmed:author | pubmed-author:MarriottGerar... | lld:pubmed |
| pubmed-article:14580569 | pubmed:author | pubmed-author:YanYulingY | lld:pubmed |
| pubmed-article:14580569 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14580569 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:14580569 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14580569 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14580569 | pubmed:pagination | 635-40 | lld:pubmed |
| pubmed-article:14580569 | pubmed:dateRevised | 2009-8-25 | lld:pubmed |
| pubmed-article:14580569 | pubmed:meshHeading | pubmed-meshheading:14580569... | lld:pubmed |
| pubmed-article:14580569 | pubmed:meshHeading | pubmed-meshheading:14580569... | lld:pubmed |
| pubmed-article:14580569 | pubmed:meshHeading | pubmed-meshheading:14580569... | lld:pubmed |
| pubmed-article:14580569 | pubmed:meshHeading | pubmed-meshheading:14580569... | lld:pubmed |
| pubmed-article:14580569 | pubmed:meshHeading | pubmed-meshheading:14580569... | lld:pubmed |
| pubmed-article:14580569 | pubmed:meshHeading | pubmed-meshheading:14580569... | lld:pubmed |
| pubmed-article:14580569 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14580569 | pubmed:articleTitle | Analysis of protein interactions using fluorescence technologies. | lld:pubmed |
| pubmed-article:14580569 | pubmed:affiliation | Department of Physiology, University of Wisconsin-Madison, 1300 University Avenue, Madison, WI 53706, USA. | lld:pubmed |
| pubmed-article:14580569 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14580569 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14580569 | pubmed:publicationType | Review | lld:pubmed |
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