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PubMed:17015441 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-92 Sentence denotes The cold and menthol receptor TRPM8 contains a functionally important double cysteine motif.
T2 93-189 Sentence denotes We have investigated the glycosylation, disulfide bonding, and subunit structure of mouse TRPM8.
T3 190-327 Sentence denotes To do this, amino-terminal c-myc or hemagglutinin epitope-tagged proteins were incorporated and expressed in Chinese hamster ovary cells.
T4 328-502 Sentence denotes These modifications had no obvious effects on channel function in intracellular calcium imaging assays upon application of agonists, icilin or menthol, and cold temperatures.
T5 503-679 Sentence denotes Unmodified TRPM8 migrates with an apparent mass of 129 kDa and can be glycosylated in Chinese hamster ovary cells to give glycoproteins with apparent masses of 136 and 147 kDa.
T6 680-1020 Sentence denotes We identified two potential N-linked glycosylation sites in TRPM8 (Asn-821 and Asn-934) and mutated them to show that only the site in the putative pore region at position 934 is modified and that glycosylation of this site is not absolutely necessary for cell surface expression or responsiveness to icilin, menthol, and cool temperatures.
T7 1021-1112 Sentence denotes Enzymatic cleavage of the carbohydrate chains indicated that they are complex carbohydrate.
T8 1113-1311 Sentence denotes The glycosylation site is flanked in the pore by two cysteine residues that we mutated, to prove that they are involved in a conserved double cysteine motif, which is essential for channel function.
T9 1312-1449 Sentence denotes Mutation of either of these cysteines abolishes function and forces the formation of a non-functional complex of the size of a homodimer.
T10 1450-1500 Sentence denotes The double cysteine mutant is also non-functional.
T11 1501-1720 Sentence denotes Finally, we showed in Perfluoro-octanoic acid-polyacrylamide gels that TRPM8 can form a tetramer (in addition to dimer and trimer forms), consistent with current thinking that functional TRP ion channels are tetrameric.