| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-67 |
Sentence |
denotes |
Engineered xyloglucan specificity in a carbohydrate-binding module. |
| T1 |
0-67 |
Sentence |
denotes |
Engineered xyloglucan specificity in a carbohydrate-binding module. |
| T1 |
0-67 |
Sentence |
denotes |
Engineered xyloglucan specificity in a carbohydrate-binding module. |
| TextSentencer_T2 |
68-229 |
Sentence |
denotes |
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. |
| T2 |
68-229 |
Sentence |
denotes |
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. |
| T2 |
68-229 |
Sentence |
denotes |
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. |
| TextSentencer_T3 |
230-404 |
Sentence |
denotes |
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. |
| T3 |
230-404 |
Sentence |
denotes |
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. |
| T3 |
230-404 |
Sentence |
denotes |
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. |
| TextSentencer_T4 |
405-592 |
Sentence |
denotes |
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. |
| T4 |
405-592 |
Sentence |
denotes |
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. |
| T4 |
405-592 |
Sentence |
denotes |
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. |
| TextSentencer_T5 |
593-890 |
Sentence |
denotes |
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. |
| T5 |
593-890 |
Sentence |
denotes |
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. |
| T5 |
593-890 |
Sentence |
denotes |
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. |
| TextSentencer_T6 |
891-1139 |
Sentence |
denotes |
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. |
| T6 |
891-1139 |
Sentence |
denotes |
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. |
| T6 |
891-1139 |
Sentence |
denotes |
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. |