@article { ISI:000242270800002,
	title = {Engineered xyloglucan specificity in a carbohydrate-binding module},
	journal = {GLYCOBIOLOGY},
	volume = {16},
	number = {12},
	year = {2006},
	month = {DEC},
	pages = {1171-1180},
	type = {Article},
	abstract = {The field of plant cell wall biology is constantly growing and consequently so is the need for more sensitive and specific probes for individual wall components. Xyloglucan is a key polysaccharide widely distributed in the plant kingdom in both structural and storage tissues that exist in both fucosylated and non-fucosylated variants. Presently, the only xyloglucan marker available is the monoclonal antibody CCRC-M1 that is specific to terminal alpha-1,2-linked fucosyl residues on xyloglucan oligo- and polysaccharides. As a viable alternative to searches for natural binding proteins or creation of new monoclonal antibodies, an approach to select xyloglucan-specific binding proteins from a combinatorial library of the carbohydrate-binding module, CBM4-2, from xylanase Xyn10A of Rhodothermus marinus is described. Using phage display technology in combination with a chemoenzymatic method to anchor xyloglucan to solid supports, the selection of xyloglucan-binding modules with no detectable residual wild-type xylan and beta-glucan-binding ability was achieved.},
	issn = {0959-6658},
	doi = {10.1093/glycob/cwl038},
	author = {Gunnarsson, Lavinia Cicortas and Zhou, Qi and Montanier, Cedric and Karlsson, Eva Nordberg and Brumer, Harry and Ohlin, Mats}
}
