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Proc. Natl. Acad. Sci","volume":"106","author":"SB Khatau","year":"2009","journal-title":"U. S. A"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"21305","DOI":"10.1074\/jbc.R800020200","article-title":"Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction","volume":"283","author":"L Schaefer","year":"2008","journal-title":"J Biol Chem"},{"key":"ref54","first-page":"269","article-title":"Integrins. Cell Tissue Res","volume":"339","author":"M Barczyk","year":"2010"},{"key":"ref55","first-page":"e15746","article-title":"Acidic extracellular pH promotes activation of integrin alpha(v)beta(3) PLoS. One","volume":"6","author":"RK Paradise","year":"2011"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"3366","DOI":"10.1128\/MCB.01403-10","article-title":"Talin1 regulates integrin turnover to promote embryonic epithelial morphogenesis","volume":"31","author":"J Liu","year":"2011","journal-title":"Mol Cell Biol"},{"key":"ref57","first-page":"3484","article-title":"Differential effects of CD18, CD29, and CD49 integrin subunit inhibition on neutrophil migration in pulmonary inflammation. J.Immunol","volume":"166","author":"VC Ridger","year":"2001"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1038\/328649a0","article-title":"Site-specific phosphorylation induces disassembly of vimentin filaments in vitro","volume":"328","author":"M Inagaki","year":"1987","journal-title":"Nature"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"1557","DOI":"10.1046\/j.1523-1755.2000.00317.x","article-title":"Small proteoglycans of normal adult human kidney: distinct expression patterns of decorin, biglycan, fibromodulin, and lumican","volume":"58","author":"L Schaefer","year":"2000","journal-title":"Kidney Int"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1002\/(SICI)1097-4652(199807)176:1<92::AID-JCP11>3.0.CO;2-Q","article-title":"Reduced viability of human vascular endothelial cells cultured on Matrigel","volume":"176","author":"V Ranta","year":"1998","journal-title":"J Cell Physiol"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.semcdb.2009.08.005","article-title":"Collagen-based cell migration models in vitro and in vivo","volume":"20","author":"K Wolf","year":"2009","journal-title":"Semin Cell Dev Biol"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"31956","DOI":"10.1074\/jbc.M401409200","article-title":"Integrin-mediated cell adhesion to type I collagen fibrils","volume":"279","author":"J Jokinen","year":"2004","journal-title":"J Biol Chem"},{"key":"ref63","unstructured":"Bhide VM, Laschinger CA, Arora PD, Lee W, Hakkinen L, <etal>et al<\/etal>.. 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