The role of Sp1 and NF-kappa B in regulating CD40 gene expression (Q42514630)

1 November 2017

title

The role of Sp1 and NF-kappa B in regulating CD40 gene expression (English)

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Herman Waldmann

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Masahide Tone

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Yukiko Tone

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Jennifer M Babik

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language of work or name

English

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publication date

20 December 2001

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Journal of Biological Chemistry

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published in

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volume

277

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page(s)

8890-8897

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CD40 AND CD154 IN CELL-MEDIATED IMMUNITY

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cites work

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A conditioned dendritic cell can be a temporal bridge between a CD4+ T-helper and a T-killer cell

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Help for cytotoxic-T-cell responses is mediated by CD40 signalling

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T-cell help for cytotoxic T lymphocytes is mediated by CD40-CD40L interactions

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Reduction of atherosclerosis in mice by inhibition of CD40 signalling

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Two differently regulated nuclear factor kappaB activation pathways triggered by the cytoplasmic tail of CD40

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CD40 signaling through tumor necrosis factor receptor-associated factors (TRAFs). Binding site specificity and activation of downstream pathways by distinct TRAFs

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Role of T-bet in commitment of TH1 cells before IL-12-dependent selection.

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Regulation of CD40 function by its isoforms generated through alternative splicing

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IL-10 gene expression is controlled by the transcription factors Sp1 and Sp3.

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Bisanthracycline WP631 inhibits basal and Sp1-activated transcription initiation in vitro.

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Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-gamma uses a different signaling pathway

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O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation

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GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase

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The NF-kappa B and I kappa B proteins: new discoveries and insights

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Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells

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Interleukin-12: a cytokine at the interface of inflammation and immunity

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Involvement of STAT-1 and ets family members in interferon-gamma induction of CD40 transcription in microglia/macrophages

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Sp1 Is Phosphorylated and Its DNA Binding Activity Down-regulated upon Terminal Differentiation of the Liver

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Casein kinase II-mediated phosphorylation of the C terminus of Sp1 decreases its DNA binding activity

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Identifiers

DOI

10.1074/JBC.M109889200

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1 November 2017

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