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PubMed:10089211 / 521-1214 JSONTXT

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PubTator4TogoVar

Id Subject Object Predicate Lexical cue proteinmutation
10089211_0 382-395 ProteinMutation denotes Gly170 to Ser rs3745635
10089211_1 418-431 ProteinMutation denotes Ile356 to Lys rs3894326

sentences

Id Subject Object Predicate Lexical cue
TextSentencer_T4 0-693 Sentence denotes Here we carried out an extensive study on the biological properties of the three mutant Lewis enzymes, the le1, le2, and le3 enzymes, using native tissues and obtained the following results. (1) In in vivo and in vitro experiments, the le1 and le2 enzymes were found to be susceptible to protease digestion probably because the one missense mutation in the catalytic domains, i.e., Gly170 to Ser in the le1 enzyme and Ile356 to Lys in the le2 enzyme, makes the three-dimensional structures of the enzymesunstable, while the le3 and wild-type Lewis enzymes wereresistant to protease digestion. (2) The le1 and le2 enzymes cannot synthesize type 1 Lewis antigens on either glycolipids or mucins.
T4 0-693 Sentence denotes Here we carried out an extensive study on the biological properties of the three mutant Lewis enzymes, the le1, le2, and le3 enzymes, using native tissues and obtained the following results. (1) In in vivo and in vitro experiments, the le1 and le2 enzymes were found to be susceptible to protease digestion probably because the one missense mutation in the catalytic domains, i.e., Gly170 to Ser in the le1 enzyme and Ile356 to Lys in the le2 enzyme, makes the three-dimensional structures of the enzymesunstable, while the le3 and wild-type Lewis enzymes wereresistant to protease digestion. (2) The le1 and le2 enzymes cannot synthesize type 1 Lewis antigens on either glycolipids or mucins.
T4 0-693 Sentence denotes Here we carried out an extensive study on the biological properties of the three mutant Lewis enzymes, the le1, le2, and le3 enzymes, using native tissues and obtained the following results. (1) In in vivo and in vitro experiments, the le1 and le2 enzymes were found to be susceptible to protease digestion probably because the one missense mutation in the catalytic domains, i.e., Gly170 to Ser in the le1 enzyme and Ile356 to Lys in the le2 enzyme, makes the three-dimensional structures of the enzymesunstable, while the le3 and wild-type Lewis enzymes wereresistant to protease digestion. (2) The le1 and le2 enzymes cannot synthesize type 1 Lewis antigens on either glycolipids or mucins.

GlycoBiology-FMA

Id Subject Object Predicate Lexical cue
_T8 147-154 FMAID:256050 denotes tissues
_T9 671-682 FMAID:196773 denotes glycolipids
_T10 671-682 FMAID:82780 denotes glycolipids

uniprot-human

Id Subject Object Predicate Lexical cue
T3 288-296 http://www.uniprot.org/uniprot/P63128 denotes protease
T4 573-581 http://www.uniprot.org/uniprot/P63128 denotes protease
T5 288-296 http://www.uniprot.org/uniprot/P10265 denotes protease
T6 573-581 http://www.uniprot.org/uniprot/P10265 denotes protease
T7 288-296 http://www.uniprot.org/uniprot/P63119 denotes protease
T8 573-581 http://www.uniprot.org/uniprot/P63119 denotes protease
T9 288-296 http://www.uniprot.org/uniprot/P63120 denotes protease
T10 573-581 http://www.uniprot.org/uniprot/P63120 denotes protease
T11 288-296 http://www.uniprot.org/uniprot/P63121 denotes protease
T12 573-581 http://www.uniprot.org/uniprot/P63121 denotes protease
T13 288-296 http://www.uniprot.org/uniprot/P63122 denotes protease
T14 573-581 http://www.uniprot.org/uniprot/P63122 denotes protease
T15 288-296 http://www.uniprot.org/uniprot/P63123 denotes protease
T16 573-581 http://www.uniprot.org/uniprot/P63123 denotes protease
T17 288-296 http://www.uniprot.org/uniprot/P63124 denotes protease
T18 573-581 http://www.uniprot.org/uniprot/P63124 denotes protease
T19 288-296 http://www.uniprot.org/uniprot/P63125 denotes protease
T20 573-581 http://www.uniprot.org/uniprot/P63125 denotes protease
T21 288-296 http://www.uniprot.org/uniprot/P63127 denotes protease
T22 573-581 http://www.uniprot.org/uniprot/P63127 denotes protease
T23 288-296 http://www.uniprot.org/uniprot/P63129 denotes protease
T24 573-581 http://www.uniprot.org/uniprot/P63129 denotes protease
T25 288-296 http://www.uniprot.org/uniprot/P63131 denotes protease
T26 573-581 http://www.uniprot.org/uniprot/P63131 denotes protease
T27 288-296 http://www.uniprot.org/uniprot/Q9Y6I0 denotes protease
T28 573-581 http://www.uniprot.org/uniprot/Q9Y6I0 denotes protease

GlycoBiology-NCBITAXON

Id Subject Object Predicate Lexical cue
T2 147-154 http://purl.bioontology.org/ontology/STY/T024 denotes tissues

GO-BP

Id Subject Object Predicate Lexical cue
T3 297-306 http://purl.obolibrary.org/obo/GO_0007586 denotes digestion
T4 582-591 http://purl.obolibrary.org/obo/GO_0007586 denotes digestion
T5 428-431 http://purl.obolibrary.org/obo/GO_0050065 denotes Lys

GO-CC

Id Subject Object Predicate Lexical cue
T1 392-395 http://purl.obolibrary.org/obo/GO_0005790 denotes Ser

UBERON-AE

Id Subject Object Predicate Lexical cue
T2 23-32 http://purl.obolibrary.org/obo/UBERON_2000106 denotes extensive
T3 147-154 http://purl.obolibrary.org/obo/UBERON_0000479 denotes tissues

EDAM-topics

Id Subject Object Predicate Lexical cue
T4 33-38 http://edamontology.org/topic_3678 denotes study
T5 307-315 http://edamontology.org/topic_2269 denotes probably
T6 341-349 http://edamontology.org/topic_0199 denotes mutation
T7 652-660 http://edamontology.org/topic_2830 denotes antigens

EDAM-DFO

Id Subject Object Predicate Lexical cue
T2 479-489 http://edamontology.org/data_0883 denotes structures

GlycoBiology-Motifs

Id Subject Object Predicate Lexical cue
T7 88-93 http://rdf.glycoinfo.org/glycan/G00047MO denotes Lewis
T8 542-547 http://rdf.glycoinfo.org/glycan/G00047MO denotes Lewis
T9 646-651 http://rdf.glycoinfo.org/glycan/G00047MO denotes Lewis

performance-test

Id Subject Object Predicate Lexical cue
PD-UBERON-AE-B_T1 147-154 http://purl.obolibrary.org/obo/UBERON_0000479 denotes tissues
PD-UBERON-AE-B_T4 23-32 http://purl.obolibrary.org/obo/UBERON_2000106 denotes extensive