| pubmed-article:20677833 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20677833 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:20677833 | lifeskim:mentions | umls-concept:C0763620 | lld:lifeskim |
| pubmed-article:20677833 | lifeskim:mentions | umls-concept:C0038477 | lld:lifeskim |
| pubmed-article:20677833 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:20677833 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:20677833 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:20677833 | pubmed:dateCreated | 2010-8-3 | lld:pubmed |
| pubmed-article:20677833 | pubmed:abstractText | The EphA2 receptor tyrosine kinase has emerged as a promising new therapeutic target in cancer because of its high level of expression in tumors. EphA2-specific antibodies have been used to deliver drugs and toxins to tumor cells, leading to inhibition of tumor growth and metastatic dissemination. We previously identified two related peptides, YSA and SWL, that selectively bind to the ligand-binding domain of EphA2 but not other Eph receptors and could therefore be useful as selective targeting agents. Here we characterize the two peptides and a series of derivatives. On the basis of systematic amino acid replacements, only five YSA residues appear to be critical for high-affinity receptor binding. Furthermore, a peptide comprising only the first five residues of YSA retains selectivity for EphA2. Similar to ephrin-A1, the physiological ligand for EphA2, both YSA and SWL activate EphA2 and inhibit downstream oncogenic signaling pathways in PC3 cancer cells. The two peptides and derivatives are quite stable in conditioned cell culture medium and show promise for delivering drugs and imaging agents to EphA2-expressing tumors. | lld:pubmed |
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| pubmed-article:20677833 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20677833 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20677833 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20677833 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20677833 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20677833 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20677833 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20677833 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:20677833 | pubmed:author | pubmed-author:PasqualeElena... | lld:pubmed |
| pubmed-article:20677833 | pubmed:author | pubmed-author:HuangZiweiZ | lld:pubmed |
| pubmed-article:20677833 | pubmed:author | pubmed-author:ZhuXuejunX | lld:pubmed |
| pubmed-article:20677833 | pubmed:author | pubmed-author:KoolpeMitchel... | lld:pubmed |
| pubmed-article:20677833 | pubmed:author | pubmed-author:MitraSayantan... | lld:pubmed |
| pubmed-article:20677833 | pubmed:author | pubmed-author:DuggineniSrin... | lld:pubmed |
| pubmed-article:20677833 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20677833 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:20677833 | pubmed:volume | 49 | lld:pubmed |
| pubmed-article:20677833 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20677833 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20677833 | pubmed:pagination | 6687-95 | lld:pubmed |
| pubmed-article:20677833 | pubmed:dateRevised | 2011-8-11 | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:meshHeading | pubmed-meshheading:20677833... | lld:pubmed |
| pubmed-article:20677833 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20677833 | pubmed:articleTitle | Structure-activity relationship analysis of peptides targeting the EphA2 receptor. | lld:pubmed |
| pubmed-article:20677833 | pubmed:affiliation | Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, USA. | lld:pubmed |
| pubmed-article:20677833 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20677833 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:20677833 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
