INTEGRIN LIGANDS

By J. Humphries, Adam Byron, M. Humphries. Journal of Cell Science, 2006

1,649 citations recorded by the source corpus.

Integrins are one of the major families of cell adhesion receptors ([Humphries, 2000][1]; [Hynes, 2002][2]). All integrins are non-covalently linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and

Subfields: Cell Biology, Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/23f12c1d199394d80a8d0f96f662173fd1f80596

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Citations in the corpus

Integrin signalling at a glance (2009, background): “The specifics of extracellular ligand binding and the range of known integrin ligands are reviewed elsewhere ( Humphries et al., 2006; Luo et al., 2007).”
High-resolution atomic force microscopy and spectroscopy of native membrane proteins (2011, background): “Composed of different α and β subunits, integrins form 24 different heterodimers in mammals [379].”
Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “Eighteen a subunits and eight b subunits can assemble in 24 different combinations that have overlapping substrate specificity and cell-type-specific expression patterns (Hynes 2002; Humphries et al. 2006).”
E-cadherin–integrin crosstalk in cancer invasion and metastasis (2013, background): “The resulting multitude of possible combinations gives rise to more than 20 different integrins, which act to differentially control a range of biological processes through selective binding to extracellular substrates (Humphries et al., 2006).”
Synergistic control of cell adhesion by integrins and syndecans (2007, background): “The extracellular domains of integrins interact with various ligands, including ECM glycoproteins and cell-surface protein”
The collagen family. (2011, background): “Collagens are deposited in the extracellular matrix, but they participate in cell-matrix interactions via several receptor families (Heino et al. 2007, 2009; Humphries et al. 2006; Leitinger and Hohenester 2007).”
The extracellular matrix at a glance (2010, background): “Cell adhesion to the ECM is mediated by ECM receptors, such as integrins, discoidin domain receptors and syndecans (Harburger and Calderwood, 2009; Humphries et al., 2006; Leitinger and Hohenester, 2007; Xian et al., 2010).”
Integrins (2009, background): “The RGD sequence is also present in vitronectin, fibrinogen, and the LAP complex part of inactive transforming growth factor-β (TGF-β) and many other ECM proteins (Humphries et al. 2006).”
Tumor angiogenesis: molecular pathways and therapeutic targets (2011, background): “In particular, α v and α 5 β 1 integrins recognize the Arg-Gly-Asp sequence in their respective ligands: α 5 β 1 binds fibronectin, α v β 5 binds vitronectin, and α v β 3 binds many substrates, including fibronectin, vitronectin, von Willebrand factor, tenascin, osteopontin, fibrillin, fibrinog”