Fibronectin at a glance
By R. Pankov, Kenneth M. Yamada. Journal of Cell Science, 2002
2,063 citations recorded by the source corpus.
Subfields: Cell Biology, Immunology and Allergy, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/99bd725e83a114aa153475db05684b29e867cbc0
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Citations in the corpus
- Extracellular matrix structure. (2016, background): “adhesion and/or migration of cells into fibrin clots as well as in fibrin clearance from circulation in inflammatory conditions [175].”
- The extracellular matrix at a glance (2010, background): “FN is secreted as a dimer joined by two C-terminal disulfide bonds and has several binding sites to other FN dimers, to collagen, to heparin and also to cell-surface integrin receptors (Pankov and Yamada, 2002).”
- Extracellular matrix dynamics in development and regenerative medicine (2008, background): “FN fibrillogenesis by the heterodimeric integrin 5 1 (Danen et al., 1995; Nagai et al., 1991; Pankov and Yamada, 2002; Ruoslahti and Pierschbacher, 1987) depends primarily on its binding with specific sites within the secreted FN dimer [the well-known arginine-glycine-aspartate (RGD) sequence and th”
- Fibronectin is required for integrin o:vβ6‐mediated activation of latent TGF‐β complexes containing LTBP‐1 (2005, background): “Fn is an abundant ECM glycoprotein that plays important roles in cell adhesion, migration, growth, and differentiation (23, 24).”