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1 ffinities, not unlike those of some lectins (carbohydrate-binding proteins).
2 plays active-site properties unexpected of a carbohydrate-binding protein.
3 relaxation switch assay for the detection of carbohydrate binding proteins.
4 ates and glycoproteins to lectins, which are carbohydrate binding proteins.
5 mains that are structurally similar to known carbohydrate-binding proteins.
6 is a member of a highly conserved family of carbohydrate-binding proteins.
7 to unveil new functions of both glycans and carbohydrate-binding proteins.
8 nges can influence the ligand specificity of carbohydrate-binding proteins.
9 logy with sugar recognition sites in several carbohydrate-binding proteins.
10 any of the conserved residues found in these carbohydrate-binding proteins.
11 ohydrate ligands is demonstrated using three carbohydrate-binding proteins, a single chain antibody,
13 al platform for assessing the specificity of carbohydrate binding proteins, an important step in func
14 e "F-type" fold), which is shared with other carbohydrate-binding proteins and apparently unrelated p
15 Galectin-3 (Gal-3) is a member of a class of carbohydrate-binding proteins and plays a role in a numb
16 c parameters, (2) to capture efficiently the carbohydrate-binding protein, and (3) to identify the in
17 is of all predicted glycoside hydrolases and carbohydrate-binding proteins, and three-dimensional str
20 mechanism similar to other known hevein-like carbohydrate-binding proteins but differing in carbohydr
22 out both glycan structure and recognition by carbohydrate-binding proteins (CBPs) and is now being ex
26 he enhanced affinities of lectins, which are carbohydrate binding proteins, for multivalent carbohydr
30 DX-52-1, reporting that the multifunctional carbohydrate-binding protein galectin-3 is a secondary t
32 acterial secretion systems directs cytosolic carbohydrate-binding protein Galectin-3 to PVs and that
33 rface of the cells by an endogenous bivalent carbohydrate binding protein (galectin-1) leads to apopt
35 eptide derived by digestion of a 15N-labeled carbohydrate-binding protein, galectin-3, is presented.
37 nstrate for the first time the importance of carbohydrate-binding proteins galectins-3 and -7 in re-e
38 cleotide microarray that contains probes for carbohydrate-binding proteins, glycosyltransferases, and
39 hat are highly efficient in interacting with carbohydrate binding proteins, has been a goal of synthe
40 Galectin-1 (Gal-1), a member of a family of carbohydrate-binding proteins, has been shown to modulat
42 ing monolayer containing lectin interface (a carbohydrate binding protein, herein ArtinM) as the bio-
43 zed directly on TentaGel beads interact with carbohydrate-binding proteins in a polyvalent manner.
44 ge-like cells, but retain selectivity toward carbohydrate-binding proteins in protein-rich biological
45 ted that expression of galectin 3 (Gal-3), a carbohydrate binding protein is significantly upregulate
48 nized cross-linked lattices with multivalent carbohydrate binding proteins (lectins) together with th
49 esults obtained to date in the inhibition of carbohydrate binding proteins (lectins), but we will als
50 immobilized carbohydrates was confirmed with carbohydrate-binding proteins (lectins) detected by both
53 structural similarity to some integrins and carbohydrate-binding proteins led to the hypothesis that
55 They are recognized by selectins or other carbohydrate-binding proteins or by complementary carboh
58 regulated gene which encodes a cell surface carbohydrate binding protein, significantly reduced GAS
59 ng class of potential antivirals encompasses carbohydrate-binding proteins, such as antibodies and le
61 anovirin-N that represents a new tetravalent carbohydrate binding protein that is stable over a large
63 Our findings indicate that Nesd is a novel carbohydrate-binding protein that functions together wit
65 tionarily ancient family of Ca(+2)-dependent carbohydrate-binding proteins that are involved in the i
68 wo-component system flanked by two predicted carbohydrate-binding proteins that is absolutely require
71 represents a first step in the evolution of carbohydrate-binding proteins that use a reactive unnatu
72 ba cyst wall proteins include Jacob lectins (carbohydrate-binding proteins) that crosslink chitin, ch
73 atural glycosaminoglycans (GAG), and lectins/carbohydrate binding proteins using matrix-assisted lase
75 In addition, we have discovered that the carbohydrate-binding protein wheat germ agglutinin speci
77 teract highly specific with lectins, natural carbohydrate-binding proteins, which property is used in
81 ectin-1, a member of the conserved family of carbohydrate-binding proteins with affinity for beta-gal
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