@article {3550,
	title = {ADHESION OF MAMMALIAN-CELLS TO A RECOMBINANT ATTACHMENT FACTOR, CBD/RGD, ANALYZED BY IMAGE-ANALYSIS},
	journal = {Biotechnology and Bioengineering},
	volume = {46},
	number = {3},
	year = {1995},
	note = {ISI Document Delivery No.: QR821Times Cited: 16Cited Reference Count: 26},
	month = {May},
	pages = {185-193},
	type = {Article},
	abstract = {A luminance thresholding procedure was developed to quantify cell attachment of a variety of cell lines to CBD/RGD, a hybrid attachment factor comprising a cellulose binding domain and the fibronectin-like RGD attachment peptide. The technique used local thresholding, median filtering, and opening to separate and count cells on each image. Cell lines exhibited three different patterns of attachment to CBD/RGD, depending on whether it was immobilized on polystyrene or cellulose acetate. Vero, COS, HFF, 3T3, 293, and U373 cells attached well to CBD/RGD immobilized on polystyrene or cellulose acetate. CHO, MRC-5, and HEp-2 cells attached to CBD/RGD immobilized on polystyrene, but not to CBD/RGD immobilized on cellulose acetate. BHK and L cells failed to attach to CBD/RGD immobilized on either polystyrene or cellulose acetate. The attachment of many cell lines to CBD/RGD was comparable with attachment of these cells to fibronectin. (C) 1995 John Wiley \& Sons, Inc.},
	keywords = {ALPHA-V, ARG-GLY-ASP, CELL ATTACHMENT, CELLULASE, CELLULOMONAS FIMI, FIBRONECTIN, FRAGMENT, GROWTH, HEPARIN-BINDING, IMAGE ANALYSIS, MAMMALIAN CELLS, RECEPTOR, RECOGNITION SIGNAL, SURFACES, VITRONECTIN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995QR82100001},
	author = {Wierzba, A. and Reichl, U. and Turner, R. F. B. and Warren, R. A. J. and Kilburn, D. G.}
}
@article {3549,
	title = {PRODUCTION AND PROPERTIES OF A BIFUNCTIONAL FUSION PROTEIN THAT MEDIATES ATTACHMENT OF VERO CELLS TO CELLULOSIC MATRICES},
	journal = {Biotechnology and Bioengineering},
	volume = {47},
	number = {2},
	year = {1995},
	note = {ISI Document Delivery No.: RD894Times Cited: 7Cited Reference Count: 29},
	month = {Jul},
	pages = {147-154},
	type = {Article},
	abstract = {The sequence Arg-Gly-Asp (RGD) in extracellular matrix proteins such as fibronectin, collagen, and laminin mediates cell attachment by interacting with proteins of the integrin family of cell surface receptors. A gene fusion encoding the RGD-containing peptide, fused to the C-terminus of a cellulose-binding domain (CBD/RGD), was expressed in Escherichia coli. Cultures produced up to 50 mg of CBD/RGD per titer, most of which was extracellular. it was purified from the culture supernatant by affinity chromatography on cellulose. CBD/RGD promoted the attachment of green monkey Vero cells to polystyrene and cellulose acetate. Attachment was inhibited by smalt synthetic peptides containing the RGD sequence. CBD/RGD was as effective as collagen in promoting the attachment of Vero cells to Cellsnow(TM) microcarriers. (C) 1995 John Wiley and Sons, Inc.},
	keywords = {ADHESION, ARG-GLY-ASP, BINDING DOMAINS, BIOTECHNOLOGY, CELLULASES, CELLULOMONAS-FIMI, CELLULOSE, CULTURE, FIBRONECTIN, PROTEIN PRODUCTION, SEGMENT, SIGNAL, VITRONECTIN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995RD89400004},
	author = {Wierzba, A. and Reichl, U. and Turner, R. F. B. and Warren, R. A. J. and Kilburn, D. G.}
}
