NF-kappaB p65 (RelA) homodimer uses distinct mechanisms to recognize DNA targets (Q41734744)

8 October 2017

title

NF-kappaB p65 (RelA) homodimer uses distinct mechanisms to recognize DNA targets (English)

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8 October 2017

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Chen YQ

1

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8 October 2017

Sengchanthalangsy LL

series ordinal

2

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8 October 2017

Hackett A

series ordinal

3

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8 October 2017

Ghosh G

series ordinal

4

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8 October 2017

publication date

1 April 2000

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8 October 2017

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8 October 2017

volume

8

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8 October 2017

issue

4

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8 October 2017

page(s)

419-428

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NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses

8 October 2017

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A novel DNA recognition mode by the NF-kappa B p65 homodimer

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Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA

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Three-dimensional structure of the Stat3beta homodimer bound to DNA

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Transcriptional regulation of the intercellular adhesion molecule-1 gene by inflammatory cytokines in human endothelial cells. Essential roles of a variant NF-kappa B site and p65 homodimers

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Cooperation between SMAD and NF-kappaB in growth factor regulated type VII collagen gene expression

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Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB

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Functionally distinct NF-kappa B binding sites in the immunoglobulin kappa and IL-2 receptor alpha chain genes

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Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300

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Identifiers

DOI

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8 October 2017

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