| pubmed-article:12137563 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12137563 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:12137563 | lifeskim:mentions | umls-concept:C1709016 | lld:lifeskim |
| pubmed-article:12137563 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:12137563 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:12137563 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:12137563 | pubmed:dateCreated | 2002-10-23 | lld:pubmed |
| pubmed-article:12137563 | pubmed:abstractText | Protein domains mediate protein-protein interactions through binding to short peptide motifs in their corresponding ligands. These peptide recognition modules are critical for the assembly of multiprotein complexes. We have arrayed glutathione S-transferase (GST) fusion proteins, with a focus on protein interaction domains, on to nitrocellulose-coated glass slides to generate a protein-domain chip. Arrayed protein-interacting modules included WW (a domain with two conserved tryptophans), SH3 (Src homology 3), SH2, 14.3.3, FHA (forkhead-associated), PDZ (a domain originally identified in PSD-95, DLG and ZO-1 proteins), PH (pleckstrin homology) and FF (a domain with two conserved phenylalanines) domains. Here we demonstrate, using peptides, that the arrayed domains retain their binding integrity. Furthermore, we show that the protein-domain chip can 'fish' proteins out of a total cell lysate; these domain-bound proteins can then be detected on the chip with a specific antibody, thus producing an interaction map for a cellular protein of interest. Using this approach we have confirmed the domain-binding profile of the signalling molecule Sam68 (Src-associated during mitosis 68), and have identified a new binding profile for the core small nuclear ribonucleoprotein SmB'. This protein-domain chip not only identifies potential binding partners for proteins, but also promises to recognize qualitative differences in protein ligands (caused by post-translational modification), thus getting at the heart of signal transduction pathways. | lld:pubmed |
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| pubmed-article:12137563 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12137563 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12137563 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12137563 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12137563 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12137563 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:12137563 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12137563 | pubmed:author | pubmed-author:BedfordMark... | lld:pubmed |
| pubmed-article:12137563 | pubmed:author | pubmed-author:CôtéJocelynJ | lld:pubmed |
| pubmed-article:12137563 | pubmed:author | pubmed-author:EspejoAlexsan... | lld:pubmed |
| pubmed-article:12137563 | pubmed:author | pubmed-author:BednarekAndrz... | lld:pubmed |
| pubmed-article:12137563 | pubmed:author | pubmed-author:RichardStepha... | lld:pubmed |
| pubmed-article:12137563 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12137563 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12137563 | pubmed:volume | 367 | lld:pubmed |
| pubmed-article:12137563 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12137563 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12137563 | pubmed:pagination | 697-702 | lld:pubmed |
| pubmed-article:12137563 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:meshHeading | pubmed-meshheading:12137563... | lld:pubmed |
| pubmed-article:12137563 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12137563 | pubmed:articleTitle | A protein-domain microarray identifies novel protein-protein interactions. | lld:pubmed |
| pubmed-article:12137563 | pubmed:affiliation | The University of Texas M.D. Anderson Cancer Center, Science Park - Research Division, P.O. Box 389, Smithville, TX 78957, USA. | lld:pubmed |
| pubmed-article:12137563 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12137563 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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