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PubMed:12556500 JSONTXT

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Id Subject Object Predicate Lexical cue db_id
T2 14-19 Protein denotes c-Rel uniprot:Q04864
T4 28-40 Biological_process denotes localization go:0051179
T5 777-782 Protein denotes c-Rel uniprot:Q04864
T6 959-964 Protein denotes c-Rel uniprot:Q04864
T7 1125-1130 Protein denotes c-Rel uniprot:Q04864
T8 1523-1528 Protein denotes c-Rel uniprot:Q04864
T9 1607-1612 Protein denotes c-Rel uniprot:Q04864
T10 60-70 Protein denotes calmodulin uniprot:P0DP23
T12 76-86 Protein_complex denotes NF-kappa B wikipedia:NF-κB
T13 344-354 Protein_complex denotes NF-kappa B wikipedia:NF-κB
T14 458-468 Protein_complex denotes NF-kappa B wikipedia:NF-κB
T15 492-502 Protein_complex denotes NF-kappa B wikipedia:NF-κB
T16 754-764 Protein_complex denotes NF-kappa B wikipedia:NF-κB
T17 1748-1758 Protein_complex denotes NF-kappa B wikipedia:NF-κB
T18 428-437 Protein denotes I kappa B uniprot:P25963
T19 315-324 Protein denotes I kappa B uniprot:P25963
T20 948-957 Protein denotes I kappa B uniprot:P25963
T21 1563-1572 Protein denotes I kappa B uniprot:P25963
T23 510-521 Biological_process denotes translocate go:0051179
T25 566-576 Protein denotes Calmodulin uniprot:P0DP23
T27 578-581 Protein denotes CaM uniprot:P0DP23
T28 830-833 Protein denotes CaM uniprot:P0DP23
T29 856-859 Protein denotes CaM uniprot:P0DP23
T30 988-991 Protein denotes CaM uniprot:P0DP23
T31 1092-1095 Protein denotes CaM uniprot:P0DP23
T32 1483-1486 Protein denotes CaM uniprot:P0DP23
T33 1513-1516 Protein denotes CaM uniprot:P0DP23
T34 1688-1691 Protein denotes CaM uniprot:P0DP23
T35 87-90 Protein_family denotes Rel mesh:D020569
T36 205-226 Biological_process denotes embryonic development go:GO:0009790
T38 355-358 Protein_family denotes Rel mesh:D020569
T40 503-506 Protein_family denotes Rel mesh:D020569
T42 765-768 Protein_family denotes Rel mesh:D020569
T44 1759-1762 Protein_family denotes Rel mesh:D020569

Inflammaging

Id Subject Object Predicate Lexical cue
T1 0-71 Sentence denotes Regulation of c-Rel nuclear localization by binding of Ca2+/calmodulin.
T2 72-288 Sentence denotes The NF-kappa B/Rel family of transcription factors participates in the control of a wide array of genes, including genes involved in embryonic development and regulation of immune, inflammation, and stress responses.
T3 289-376 Sentence denotes In most cells, inhibitory I kappa B proteins sequester NF-kappa B/Rel in the cytoplasm.
T4 377-565 Sentence denotes Cellular stimulation results in the degradation of I kappa B and modification of NF-kappa B/Rel proteins, allowing NF-kappa B/Rel to translocate to the nucleus and act on its target genes.
T5 566-714 Sentence denotes Calmodulin (CaM) is a highly conserved, ubiquitously expressed Ca(2+) binding protein that serves as a key mediator of intracellular Ca(2+) signals.
T6 715-834 Sentence denotes Here we report that two members of the NF-kappa B/Rel family, c-Rel and RelA, interact directly with Ca(2+)-loaded CaM.
T7 835-1056 Sentence denotes The interaction with CaM is greatly enhanced by cell stimulation, and this enhancement is blocked by addition of I kappa B. c-Rel and RelA interact with CaM through a similar sequence near the nuclear localization signal.
T8 1057-1326 Sentence denotes Compared to the wild-type protein, CaM binding-deficient mutants of c-Rel exhibit increases in both nuclear accumulation and transcriptional activity on the interleukin 2 and granulocyte macrophage colony-stimulating factor promoters in the presence of a Ca(2+) signal.
T9 1327-1487 Sentence denotes Conversely, for RelA neither nuclear accumulation nor transcriptional activity on these promoters is increased by mutation of the sequence interacting with CaM.
T10 1488-1687 Sentence denotes Our results suggest that CaM binds c-Rel and RelA after their release from I kappa B and can inhibit nuclear import of c-Rel while letting RelA translocate to the nucleus and act on its target genes.
T11 1688-1794 Sentence denotes CaM can therefore differentially regulate the activation of NF-kappa B/Rel proteins following stimulation.
T1 0-71 Sentence denotes Regulation of c-Rel nuclear localization by binding of Ca2+/calmodulin.
T2 72-288 Sentence denotes The NF-kappa B/Rel family of transcription factors participates in the control of a wide array of genes, including genes involved in embryonic development and regulation of immune, inflammation, and stress responses.
T3 289-376 Sentence denotes In most cells, inhibitory I kappa B proteins sequester NF-kappa B/Rel in the cytoplasm.
T4 377-565 Sentence denotes Cellular stimulation results in the degradation of I kappa B and modification of NF-kappa B/Rel proteins, allowing NF-kappa B/Rel to translocate to the nucleus and act on its target genes.
T5 566-714 Sentence denotes Calmodulin (CaM) is a highly conserved, ubiquitously expressed Ca(2+) binding protein that serves as a key mediator of intracellular Ca(2+) signals.
T6 715-834 Sentence denotes Here we report that two members of the NF-kappa B/Rel family, c-Rel and RelA, interact directly with Ca(2+)-loaded CaM.
T7 835-1056 Sentence denotes The interaction with CaM is greatly enhanced by cell stimulation, and this enhancement is blocked by addition of I kappa B. c-Rel and RelA interact with CaM through a similar sequence near the nuclear localization signal.
T8 1057-1326 Sentence denotes Compared to the wild-type protein, CaM binding-deficient mutants of c-Rel exhibit increases in both nuclear accumulation and transcriptional activity on the interleukin 2 and granulocyte macrophage colony-stimulating factor promoters in the presence of a Ca(2+) signal.
T9 1327-1487 Sentence denotes Conversely, for RelA neither nuclear accumulation nor transcriptional activity on these promoters is increased by mutation of the sequence interacting with CaM.
T10 1488-1687 Sentence denotes Our results suggest that CaM binds c-Rel and RelA after their release from I kappa B and can inhibit nuclear import of c-Rel while letting RelA translocate to the nucleus and act on its target genes.
T11 1688-1794 Sentence denotes CaM can therefore differentially regulate the activation of NF-kappa B/Rel proteins following stimulation.