PubMed:8019555 JSONTXT

{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":67,"end":87},"obj":"DNA"},{"id":"T2","span":{"begin":88,"end":91},"obj":"DNA"},{"id":"T3","span":{"begin":118,"end":121},"obj":"DNA"},{"id":"T4","span":{"begin":346,"end":357},"obj":"protein"},{"id":"T5","span":{"begin":404,"end":414},"obj":"protein"},{"id":"T6","span":{"begin":422,"end":441},"obj":"protein"},{"id":"T7","span":{"begin":504,"end":531},"obj":"protein"},{"id":"T8","span":{"begin":617,"end":620},"obj":"DNA"}],"text":"Description and functional implications of a novel mutation in the sex-determining gene SRY.\nThe sex-determining gene SRY was screened for molecular alteration in an XY sex-reversed female by single-strand conformation polymorphism (SSCP) technique. An A-to-G transition was detected which leads to an exchange of a tyrosine by a cysteine in the SRY protein. The affected tyrosine residue located at the C terminus of the DNA binding protein is evolutionarily strongly conserved among the members of the HMG box containing proteins. Using gel shift assay and peptide synthesis such a mutation is shown to abolish the SRY protein DNA binding ability. The involvement of this particular amino acid in the binding specificity is also discussed."}

{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":92},"obj":"Sentence"},{"id":"S2","span":{"begin":93,"end":249},"obj":"Sentence"},{"id":"S3","span":{"begin":250,"end":358},"obj":"Sentence"},{"id":"S4","span":{"begin":359,"end":532},"obj":"Sentence"},{"id":"S5","span":{"begin":533,"end":649},"obj":"Sentence"},{"id":"S6","span":{"begin":650,"end":741},"obj":"Sentence"}],"text":"Description and functional implications of a novel mutation in the sex-determining gene SRY.\nThe sex-determining gene SRY was screened for molecular alteration in an XY sex-reversed female by single-strand conformation polymorphism (SSCP) technique. An A-to-G transition was detected which leads to an exchange of a tyrosine by a cysteine in the SRY protein. The affected tyrosine residue located at the C terminus of the DNA binding protein is evolutionarily strongly conserved among the members of the HMG box containing proteins. Using gel shift assay and peptide synthesis such a mutation is shown to abolish the SRY protein DNA binding ability. The involvement of this particular amino acid in the binding specificity is also discussed."}

{"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":43,"end":59},"obj":"NP"},{"id":"C2","span":{"begin":63,"end":91},"obj":"NP"},{"id":"C3","span":{"begin":93,"end":121},"obj":"NP"},{"id":"C4","span":{"begin":250,"end":270},"obj":"NP"},{"id":"C5","span":{"begin":284,"end":289},"obj":"NP"},{"id":"C7","span":{"begin":342,"end":349},"obj":"NP"},{"id":"C6","span":{"begin":342,"end":357},"obj":"NP"},{"id":"C8","span":{"begin":559,"end":576},"obj":"NP"},{"id":"C9","span":{"begin":577,"end":592},"obj":"NP"},{"id":"C11","span":{"begin":613,"end":620},"obj":"NP"},{"id":"C10","span":{"begin":613,"end":628},"obj":"NP"},{"id":"C12","span":{"begin":669,"end":695},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-ident","subj":"C3","obj":"C2"},{"id":"R2","pred":"coref-relat","subj":"C5","obj":"C4"},{"id":"R3","pred":"coref-ident","subj":"C7","obj":"C3"},{"id":"R4","pred":"coref-other","subj":"C9","obj":"C1"},{"id":"R5","pred":"coref-ident","subj":"C11","obj":"C7"},{"id":"R6","pred":"coref-ident","subj":"C10","obj":"C6"},{"id":"R7","pred":"coref-ident","subj":"C12","obj":"C8"}],"text":"Description and functional implications of a novel mutation in the sex-determining gene SRY.\nThe sex-determining gene SRY was screened for molecular alteration in an XY sex-reversed female by single-strand conformation polymorphism (SSCP) technique. An A-to-G transition was detected which leads to an exchange of a tyrosine by a cysteine in the SRY protein. The affected tyrosine residue located at the C terminus of the DNA binding protein is evolutionarily strongly conserved among the members of the HMG box containing proteins. Using gel shift assay and peptide synthesis such a mutation is shown to abolish the SRY protein DNA binding ability. The involvement of this particular amino acid in the binding specificity is also discussed."}

{"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":45,"end":59},"obj":"other_name"},{"id":"T2","span":{"begin":67,"end":87},"obj":"DNA_family_or_group"},{"id":"T3","span":{"begin":88,"end":91},"obj":"DNA_domain_or_region"},{"id":"T4","span":{"begin":118,"end":121},"obj":"DNA_domain_or_region"},{"id":"T5","span":{"begin":139,"end":159},"obj":"other_name"},{"id":"T6","span":{"begin":166,"end":188},"obj":"multi_cell"},{"id":"T7","span":{"begin":192,"end":248},"obj":"other_name"},{"id":"T8","span":{"begin":253,"end":270},"obj":"other_name"},{"id":"T9","span":{"begin":316,"end":324},"obj":"amino_acid_monomer"},{"id":"T10","span":{"begin":330,"end":338},"obj":"amino_acid_monomer"},{"id":"T11","span":{"begin":346,"end":349},"obj":"DNA_domain_or_region"},{"id":"T12","span":{"begin":372,"end":380},"obj":"amino_acid_monomer"},{"id":"T13","span":{"begin":404,"end":414},"obj":"protein_domain_or_region"},{"id":"T14","span":{"begin":422,"end":441},"obj":"protein_family_or_group"},{"id":"T15","span":{"begin":504,"end":531},"obj":"protein_family_or_group"},{"id":"T16","span":{"begin":539,"end":554},"obj":"other_name"},{"id":"T17","span":{"begin":559,"end":576},"obj":"other_name"},{"id":"T18","span":{"begin":617,"end":620},"obj":"DNA_domain_or_region"},{"id":"T19","span":{"begin":685,"end":695},"obj":"amino_acid_monomer"},{"id":"T20","span":{"begin":703,"end":722},"obj":"other_name"}],"text":"Description and functional implications of a novel mutation in the sex-determining gene SRY.\nThe sex-determining gene SRY was screened for molecular alteration in an XY sex-reversed female by single-strand conformation polymorphism (SSCP) technique. An A-to-G transition was detected which leads to an exchange of a tyrosine by a cysteine in the SRY protein. The affected tyrosine residue located at the C terminus of the DNA binding protein is evolutionarily strongly conserved among the members of the HMG box containing proteins. Using gel shift assay and peptide synthesis such a mutation is shown to abolish the SRY protein DNA binding ability. The involvement of this particular amino acid in the binding specificity is also discussed."}