PubMed:16902199 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T2","span":{"begin":230,"end":240},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T3","span":{"begin":425,"end":435},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T4","span":{"begin":554,"end":564},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T5","span":{"begin":722,"end":732},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T6","span":{"begin":976,"end":986},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T7","span":{"begin":1023,"end":1033},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T8","span":{"begin":1098,"end":1109},"obj":"https://glytoucan.org/Structures/Glycans/G00024MO"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":230,"end":240},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":425,"end":435},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":554,"end":564},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":722,"end":732},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":976,"end":986},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1023,"end":1033},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":1098,"end":1109},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G25326UC"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00024MO"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"T2","span":{"begin":230,"end":240},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"T3","span":{"begin":425,"end":435},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"T4","span":{"begin":480,"end":487},"obj":"http://www.glycoepitope.jp/epitopes/AN0352"},{"id":"T5","span":{"begin":554,"end":564},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"T6","span":{"begin":722,"end":732},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"T7","span":{"begin":976,"end":986},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"T8","span":{"begin":1023,"end":1033},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T2","span":{"begin":230,"end":240},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T3","span":{"begin":425,"end":435},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T4","span":{"begin":554,"end":564},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T5","span":{"begin":722,"end":732},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T6","span":{"begin":976,"end":986},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T7","span":{"begin":1023,"end":1033},"obj":"https://glytoucan.org/Structures/Glycans/G25326UC"},{"id":"T8","span":{"begin":1098,"end":1109},"obj":"https://glytoucan.org/Structures/Glycans/G00024MO"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":67},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":68,"end":229},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":230,"end":404},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":405,"end":592},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":593,"end":890},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":891,"end":1139},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":67},"obj":"Sentence"},{"id":"T2","span":{"begin":68,"end":229},"obj":"Sentence"},{"id":"T3","span":{"begin":230,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":592},"obj":"Sentence"},{"id":"T5","span":{"begin":593,"end":890},"obj":"Sentence"},{"id":"T6","span":{"begin":891,"end":1139},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":67},"obj":"Sentence"},{"id":"T2","span":{"begin":68,"end":229},"obj":"Sentence"},{"id":"T3","span":{"begin":230,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":592},"obj":"Sentence"},{"id":"T5","span":{"begin":593,"end":890},"obj":"Sentence"},{"id":"T6","span":{"begin":891,"end":1139},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":336,"end":343},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T2","span":{"begin":379,"end":382},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T3","span":{"begin":460,"end":470},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T4","span":{"begin":677,"end":687},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T5","span":{"begin":856,"end":868},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/374811"},{"id":"T6","span":{"begin":856,"end":876},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/29549"},{"id":"T7","span":{"begin":1098,"end":1102},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T8","span":{"begin":1098,"end":1102},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":168,"end":177},"obj":"http://purl.obolibrary.org/obo/GO_0046960"},{"id":"T2","span":{"begin":328,"end":335},"obj":"http://purl.obolibrary.org/obo/GO_0051235"},{"id":"T3","span":{"begin":328,"end":335},"obj":"http://purl.obolibrary.org/obo/GO_0035732"},{"id":"T4","span":{"begin":363,"end":374},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T5","span":{"begin":383,"end":394},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T6","span":{"begin":534,"end":541},"obj":"http://purl.obolibrary.org/obo/GO_0036065"},{"id":"T7","span":{"begin":837,"end":845},"obj":"http://purl.obolibrary.org/obo/GO_0031176"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":39,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":795,"end":815},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T3","span":{"begin":52,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":641,"end":648},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":742,"end":749},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T6","span":{"begin":808,"end":815},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":1034,"end":1041},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":1110,"end":1117},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":52,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T10","span":{"begin":641,"end":648},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T11","span":{"begin":742,"end":749},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T12","span":{"begin":808,"end":815},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T13","span":{"begin":1034,"end":1041},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":1110,"end":1117},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T15","span":{"begin":52,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T16","span":{"begin":641,"end":648},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T17","span":{"begin":742,"end":749},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T18","span":{"begin":808,"end":815},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T19","span":{"begin":1034,"end":1041},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T20","span":{"begin":1110,"end":1117},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T21","span":{"begin":52,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T22","span":{"begin":641,"end":648},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T23","span":{"begin":742,"end":749},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T24","span":{"begin":808,"end":815},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T25","span":{"begin":1034,"end":1041},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T26","span":{"begin":1110,"end":1117},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T27","span":{"begin":471,"end":479},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T28","span":{"begin":688,"end":698},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T29","span":{"begin":641,"end":657},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T30","span":{"begin":742,"end":758},"obj":"http://purl.obolibrary.org/obo/GO_0005515"},{"id":"T31","span":{"begin":733,"end":758},"obj":"http://purl.obolibrary.org/obo/GO_0019904"},{"id":"T32","span":{"begin":969,"end":975},"obj":"http://purl.obolibrary.org/obo/GO_0043495"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":87,"end":91},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":87,"end":96},"obj":"http://purl.obolibrary.org/obo/GO_0005618"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":336,"end":343},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"AlvisNLP-Test","denotations":[{"id":"3770e137","span":{"begin":856,"end":876},"obj":"https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=29549"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T2","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T3","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T4","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T5","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T6","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T7","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T8","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T9","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T10","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T11","span":{"begin":379,"end":382},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":1098,"end":1109},"obj":"http://rdf.glycoinfo.org/glycan/G00024MO"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":11,"end":21},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":230,"end":240},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":425,"end":435},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":554,"end":564},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":722,"end":732},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":976,"end":986},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":1023,"end":1033},"obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"PD-GlycoEpitope-B_T8","span":{"begin":480,"end":487},"obj":"http://www.glycoepitope.jp/epitopes/AN0352"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":336,"end":343},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"Glycan"},{"id":"T2","span":{"begin":230,"end":240},"obj":"Glycan"},{"id":"T3","span":{"begin":425,"end":435},"obj":"Glycan"},{"id":"T4","span":{"begin":554,"end":564},"obj":"Glycan"},{"id":"T5","span":{"begin":722,"end":732},"obj":"Glycan"},{"id":"T6","span":{"begin":976,"end":986},"obj":"Glycan"},{"id":"T7","span":{"begin":1023,"end":1033},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A8","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A9","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A10","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A11","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A12","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A13","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A14","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"Glycan"},{"id":"T2","span":{"begin":230,"end":240},"obj":"Glycan"},{"id":"T3","span":{"begin":425,"end":435},"obj":"Glycan"},{"id":"T4","span":{"begin":554,"end":564},"obj":"Glycan"},{"id":"T5","span":{"begin":722,"end":732},"obj":"Glycan"},{"id":"T6","span":{"begin":976,"end":986},"obj":"Glycan"},{"id":"T7","span":{"begin":1023,"end":1033},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A8","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A9","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A10","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A11","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A12","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A13","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G25326UC"},{"id":"A14","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G25326UC"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":92,"end":96},"obj":"Body_part"},{"id":"T2","span":{"begin":213,"end":217},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000060"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000060"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":856,"end":876},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"29549"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":67},"obj":"Sentence"},{"id":"T2","span":{"begin":68,"end":229},"obj":"Sentence"},{"id":"T3","span":{"begin":230,"end":404},"obj":"Sentence"},{"id":"T4","span":{"begin":405,"end":592},"obj":"Sentence"},{"id":"T5","span":{"begin":593,"end":890},"obj":"Sentence"},{"id":"T6","span":{"begin":891,"end":1139},"obj":"Sentence"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":230,"end":240},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":425,"end":435},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":480,"end":487},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":554,"end":564},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":722,"end":732},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":976,"end":986},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1023,"end":1033},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/AN0352"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0511"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":336,"end":343},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:9637"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":856,"end":876},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"29549"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":11,"end":21},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":230,"end":240},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":425,"end":435},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":480,"end":487},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":554,"end":564},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":722,"end":732},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":976,"end":986},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1023,"end":1033},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/AN0352"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0511"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0511"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":92,"end":96},"obj":"Body_part"},{"id":"T2","span":{"begin":213,"end":217},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000060"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000060"}],"text":"Engineered xyloglucan specificity in a carbohydrate-binding module.\nThe 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."}