pubmed-article:2025877 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0929301 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0006141 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0205307 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:2025877 | lifeskim:mentions | umls-concept:C2826170 | lld:lifeskim |
pubmed-article:2025877 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2025877 | pubmed:dateCreated | 1991-6-10 | lld:pubmed |
pubmed-article:2025877 | pubmed:abstractText | Fluorescent lectin binding to cell surfaces was quantitatively analysed by flow cytometry on mortal human breast epithelial cells MCF-10M, the immortalized cell line MCF-10A derived from MCF-10M and sublines of MCF-10A transfected with the neomycin resistance gene (MCF-10Aneo), the c-Ha-ras protooncogene (MCF-10AneoN), or transfected and transformed with the c-Ha-ras activated oncogene (MCF-10AneoT). Immortal MCF-10A cells bound 10-fold more peanut agglutinin (PNA) and soy bean agglutinin (SBA) than did MCF-10M cells. Transformed MCF-10AneoT cells bound approximately ten times more PNA than did non-transformed cells transfected with protooncogene (MCF-10AneoN). Treatment of the transfectants with neuraminidase abrogated the differences in PNA-binding and reduced the differences in SBA binding. SDS-PAGE separation of PNA binding glycoproteins revealed different patterns for all MCF-10A derived sublines. | lld:pubmed |
pubmed-article:2025877 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2025877 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2025877 | pubmed:language | eng | lld:pubmed |
pubmed-article:2025877 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2025877 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2025877 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2025877 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2025877 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2025877 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2025877 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2025877 | pubmed:issn | 0304-3835 | lld:pubmed |
pubmed-article:2025877 | pubmed:author | pubmed-author:RussoJJ | lld:pubmed |
pubmed-article:2025877 | pubmed:author | pubmed-author:BasoloFF | lld:pubmed |
pubmed-article:2025877 | pubmed:author | pubmed-author:MillerF RFR | lld:pubmed |
pubmed-article:2025877 | pubmed:author | pubmed-author:RAYJ MJM | lld:pubmed |
pubmed-article:2025877 | pubmed:author | pubmed-author:ElliottJ WJW | lld:pubmed |
pubmed-article:2025877 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2025877 | pubmed:volume | 57 | lld:pubmed |
pubmed-article:2025877 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2025877 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2025877 | pubmed:pagination | 27-36 | lld:pubmed |
pubmed-article:2025877 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:meshHeading | pubmed-meshheading:2025877-... | lld:pubmed |
pubmed-article:2025877 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:2025877 | pubmed:articleTitle | Cell surface glycosylation changes accompanying immortalization and transformation of normal human mammary epithelial cells. | lld:pubmed |
pubmed-article:2025877 | pubmed:affiliation | Department of Immunology, Michigan Cancer Foundation, Detroit 48201. | lld:pubmed |
pubmed-article:2025877 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2025877 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2025877 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2025877 | lld:pubmed |