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1 February 2008
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Fibronectin, one of the typical ligands of integrin, may induce cell attachment and cell spread. On activated integrins binding to the fibronectin, they cluster at the binding site, recruit cytoplasmic proteins to organize focal adhesions and initiate actin stress fibers to rearrange, and finally result in cell adhesion and spreading. Using immunofluorescence to visualize the focal adhesion and actin stress fibers, it was found that after 2 h attachment to fibronectin in serum-free medium, MDA-MB-435 cells were well spread with focal adhesions localized at the periphery of cells and actin stress fibers well organized. For details, see the article by Zhou and colleagues on page 194.Close Modal - PDF Icon PDF LinkTable of Contents
ISSN 1541-7786
EISSN 1557-3125
Journal Archive
Molecular Cancer Research (2002-Present; volumes 1-current)
(ISSN 0008-5472) Published monthly since November, 2002.Cell Growth & Differentiation (1990-2002; volumes 1-13)
(ISSN 1044-9523) Published monthly 1990- September, 2002.Table of Contents
Angiogenesis, Metastasis, and the Cellular Microenvironment
Cancer Genes and Genomics
MDM2 Gene Amplification Is Correlated to Tumor Progression but not to the Presence of SNP309 or TP53 Mutational Status in Primary Colorectal Cancers
Ann Forslund; Zhaoshi Zeng; Li-Xuan Qin; Shoshana Rosenberg; MacKevin Ndubuisi; Hanna Pincas; William Gerald; Daniel A. Notterman; Francis Barany; Philip B. Paty
Cell Cycle, Cell Death, and Senescence
DNA Damage and Cellular Stress Responses
Signaling and Regulation
Correction
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