PubMed:1535455 JSONTXT

{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":50,"end":66},"obj":"protein"},{"id":"T2","span":{"begin":70,"end":83},"obj":"cell_type"},{"id":"T3","span":{"begin":85,"end":98},"obj":"cell_type"},{"id":"T4","span":{"begin":139,"end":174},"obj":"protein"},{"id":"T5","span":{"begin":176,"end":188},"obj":"protein"},{"id":"T6","span":{"begin":234,"end":253},"obj":"protein"},{"id":"T7","span":{"begin":321,"end":340},"obj":"protein"},{"id":"T8","span":{"begin":467,"end":500},"obj":"cell_line"},{"id":"T9","span":{"begin":653,"end":665},"obj":"protein"},{"id":"T10","span":{"begin":691,"end":703},"obj":"protein"},{"id":"T11","span":{"begin":770,"end":782},"obj":"protein"},{"id":"T12","span":{"begin":795,"end":817},"obj":"protein"},{"id":"T13","span":{"begin":906,"end":924},"obj":"protein"},{"id":"T14","span":{"begin":944,"end":987},"obj":"protein"}],"text":"Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes.\nB lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (Fc gamma RII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell Fc gamma RII contains an insertion of 47 amino acids that participates in determining receptor function in these cells. Transfection of an Fc gamma RII-negative B-cell line with complementary DNA's encoding the two splice products and various receptor mutants indicated that the insertion was responsible for preventing both Fc gamma RII-mediated endocytosis and Fc gamma RII-mediated antigen presentation. The insertion was not required for Fc gamma RII to modulate surface immunoglobulin-triggered B-cell activation. Instead, regulation of activation involved a region of the cytoplasmic domain common to both the lymphocyte and macrophage receptor isoforms. In contrast, the insertion did contribute to the formation of caps in response to receptor cross-linking, consistent with suggestions that the lymphocyte but not macrophage form of the receptor can associate with the detergent-insoluble cytoskeleton."}

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{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":84},"obj":"Sentence"},{"id":"S2","span":{"begin":85,"end":254},"obj":"Sentence"},{"id":"S3","span":{"begin":255,"end":447},"obj":"Sentence"},{"id":"S4","span":{"begin":448,"end":734},"obj":"Sentence"},{"id":"S5","span":{"begin":735,"end":846},"obj":"Sentence"},{"id":"S6","span":{"begin":847,"end":988},"obj":"Sentence"},{"id":"S7","span":{"begin":989,"end":1239},"obj":"Sentence"}],"text":"Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes.\nB lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (Fc gamma RII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell Fc gamma RII contains an insertion of 47 amino acids that participates in determining receptor function in these cells. Transfection of an Fc gamma RII-negative B-cell line with complementary DNA's encoding the two splice products and various receptor mutants indicated that the insertion was responsible for preventing both Fc gamma RII-mediated endocytosis and Fc gamma RII-mediated antigen presentation. The insertion was not required for Fc gamma RII to modulate surface immunoglobulin-triggered B-cell activation. Instead, regulation of activation involved a region of the cytoplasmic domain common to both the lymphocyte and macrophage receptor isoforms. In contrast, the insertion did contribute to the formation of caps in response to receptor cross-linking, consistent with suggestions that the lymphocyte but not macrophage form of the receptor can associate with the detergent-insoluble cytoskeleton."}

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