| pubmed-article:15578931 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0872252 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C1328819 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0336791 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15578931 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:15578931 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:15578931 | pubmed:dateCreated | 2004-12-6 | lld:pubmed |
| pubmed-article:15578931 | pubmed:abstractText | A novel strategy that targets protein for degradation has recently been developed by exploiting a protein-targeting chimeric molecule ('Protac'). Typically, the chimeric Protac is composed of a small-molecule ligand ('bait') on one end and a synthetic octapeptide on the other. This octapeptide is recognized by E3 ubiquitin ligase pVHL (von Hippel Lindau tumor suppressor protein), thereby recruiting a small molecule-bound protein ('prey') to pVHL for ubiquitination and degradation. Since selective degradation of a cellular protein generates a "loss of function" mutation, this protein knock-out strategy may be useful to study the function of a given protein or to evaluate whether a cellular protein is a potential target for drug intervention, in a manner reminiscent of gene knock-out or siRNA approaches. Herein, we show that a synthetic pentapeptide is sufficient to interact with pVHL E3 ligase, and that the pentapeptide-based Protac efficiently induces ubiquitination and degradation of target protein. Our results also demonstrate that the pentapeptide-based Protac can enter cells efficiently to exerts its biological activity effectively. These results suggest that the synthetic pentapeptide can be used either directly in the preparation of cell-permeable Protacs or as a template to develop peptidomimetic or non-peptide Protacs. | lld:pubmed |
| pubmed-article:15578931 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15578931 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15578931 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15578931 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15578931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15578931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15578931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15578931 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15578931 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15578931 | pubmed:issn | 1386-2073 | lld:pubmed |
| pubmed-article:15578931 | pubmed:author | pubmed-author:KimKK | lld:pubmed |
| pubmed-article:15578931 | pubmed:author | pubmed-author:LeeHH | lld:pubmed |
| pubmed-article:15578931 | pubmed:author | pubmed-author:HoAA | lld:pubmed |
| pubmed-article:15578931 | pubmed:author | pubmed-author:ZhangDD | lld:pubmed |
| pubmed-article:15578931 | pubmed:author | pubmed-author:JeongY SYS | lld:pubmed |
| pubmed-article:15578931 | pubmed:author | pubmed-author:BaekS-HSH | lld:pubmed |
| pubmed-article:15578931 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15578931 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:15578931 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15578931 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15578931 | pubmed:pagination | 689-97 | lld:pubmed |
| pubmed-article:15578931 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:meshHeading | pubmed-meshheading:15578931... | lld:pubmed |
| pubmed-article:15578931 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15578931 | pubmed:articleTitle | Targeted degradation of proteins by small molecules: a novel tool for functional proteomics. | lld:pubmed |
| pubmed-article:15578931 | pubmed:affiliation | Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 907 Rose Street, Lexington, Kentucky 40536, USA | lld:pubmed |
| pubmed-article:15578931 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15578931 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15578931 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15578931 | lld:pubmed |
