| pubmed-article:11707259 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11707259 | lifeskim:mentions | umls-concept:C0218158 | lld:lifeskim |
| pubmed-article:11707259 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:11707259 | lifeskim:mentions | umls-concept:C0184512 | lld:lifeskim |
| pubmed-article:11707259 | lifeskim:mentions | umls-concept:C0282535 | lld:lifeskim |
| pubmed-article:11707259 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:11707259 | lifeskim:mentions | umls-concept:C0596788 | lld:lifeskim |
| pubmed-article:11707259 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11707259 | pubmed:dateCreated | 2001-11-14 | lld:pubmed |
| pubmed-article:11707259 | pubmed:abstractText | The Tec homology (TH) region located N-terminal to the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk) contains two proline-rich SH3-binding sequences (PRRs). We have previously demonstrated that the TH region acts to stabilize intermolecular interactions in N-terminally extended SH3 (PRR-SH3) fragments. Here, we analyze six PRR-SH3 fragments with different proline-to-alanine substitutions in the two PRRs. Gel permeation chromatography and nuclear magnetic resonance spectroscopy show that both PRRs can stabilize self-association. This observation provides an explanation to why the TH region of Btk makes intermolecular interactions, whereas the corresponding interaction in the related Itk kinase with only one PRR, is intramolecular. | lld:pubmed |
| pubmed-article:11707259 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11707259 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11707259 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11707259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11707259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11707259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11707259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11707259 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11707259 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11707259 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:11707259 | pubmed:author | pubmed-author:SmithC ICI | lld:pubmed |
| pubmed-article:11707259 | pubmed:author | pubmed-author:HanssonHH | lld:pubmed |
| pubmed-article:11707259 | pubmed:author | pubmed-author:HärdTT | lld:pubmed |
| pubmed-article:11707259 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11707259 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:11707259 | pubmed:volume | 508 | lld:pubmed |
| pubmed-article:11707259 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11707259 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11707259 | pubmed:pagination | 11-5 | lld:pubmed |
| pubmed-article:11707259 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:meshHeading | pubmed-meshheading:11707259... | lld:pubmed |
| pubmed-article:11707259 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11707259 | pubmed:articleTitle | Both proline-rich sequences in the TH region of Bruton's tyrosine kinase stabilize intermolecular interactions with the SH3 domain. | lld:pubmed |
| pubmed-article:11707259 | pubmed:affiliation | Department of Biotechnology, Royal Institute of Technology (KTH), SCFAB, S-106 91 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:11707259 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11707259 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11707259 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11707259 | lld:pubmed |
