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  Soluble ephrin a1 is necessary for the growth of HeLa and SK-BR3 cells

Alford, S., Watson-Hurthig, A., Scott, N., Carette, A., Lorimer, H., Bazowski, J., et al. (2010). Soluble ephrin a1 is necessary for the growth of HeLa and SK-BR3 cells. Cancer Cell International, 10: 41. doi:10.1186/1475-2867-10-41.

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Alford_Soluble_CancerCellInt_2010.pdf (Publisher version), 5MB
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Alford_Soluble_CancerCellInt_2010.pdf
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2010
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This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Alford, Spencer, Author
Watson-Hurthig, Adam, Author
Scott, Nadia1, Author           
Carette, Amanda, Author
Lorimer, Heather, Author
Bazowski, Jessa, Author
Howard, Perry L., Author
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1external, ou_persistent22              

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 Abstract: Ephrin A1 (EFNA1) is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. In malignancy, the precise role of EFNA1 and its preferred receptor, EPHA2, is controversial. Several studies have found that EFNA1 may suppress EPHA2-mediated oncogenesis, or enhance it, depending on cell type and context. However, little is known about the conditions that influence whether EFNA1 promotes or suppresses tumorigenicity. EFNA1 exists in a soluble form as well as a glycophosphatidylinositol (GPI) membrane attached form. We investigated whether the contradictory roles of EFNA1 in malignancy might in part be related to the existence of both soluble and membrane attached forms of EFNA1 and potential differences in the manner in which they interact with EPHA2.

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Language(s): eng - English
 Dates: 2010
 Publication Status: Published online
 Pages: -
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 Rev. Type: Peer
 Identifiers: DOI: 10.1186/1475-2867-10-41
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Title: Cancer Cell International
  Alternative Title : Cancer Cell International
Source Genre: Journal
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Pages: - Volume / Issue: 10 Sequence Number: 41 Start / End Page: - Identifier: ISBN: 1475-2867