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The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation.
  • P. Angel, M. Karin
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 10 December 1991
Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor
TLDR
Results strongly suggest that AP-1 is at the receiving end of a complex pathway responsible for transmitting the effects of phorbol ester tumor promoters from the plasma membrane to the transcriptional machinery. Expand
DNA Binding of the Glucocorticoid Receptor Is Not Essential for Survival
TLDR
A point mutation A458T is introduced into the GR by gene targeting using the Cre/loxP system, impairs dimerization and therefore GRE-dependent transactivation while functions that require cross-talk with other transcription factors, such as transrepression of AP-1-driven genes, remain intact. Expand
The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1
TLDR
These results clearly demonstrate that jun transcription is directly stimulated by its own gene product, and is likely to be responsible for prolonging the transient signals generated by activation of protein kinase C. Expand
AP-1 subunits: quarrel and harmony among siblings
TLDR
AP-1-mediated regulation of processes such as proliferation, differentiation, apoptosis and transformation should be considered within the context of a complex dynamic network of signalling pathways and other nuclear factors that respond simultaneously. Expand
Altered endochondral bone development in matrix metalloproteinase 13-deficient mice
TLDR
The hypothesis that proper ECM remodeling is the dominant rate-limiting process for programmed cell death, angiogenesis and osteoblast recruitment during normal skeletal morphogenesis is supported. Expand
Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor.
TLDR
The observations suggest that TGF‐beta exerts a selective effect on extracellular matrix deposition by modulating the action of other growth factors on metalloproteinase and TIMP expression. Expand
Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
TLDR
It is proposed that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation. Expand
ATF‐2 is preferentially activated by stress‐activated protein kinases to mediate c‐jun induction in response to genotoxic agents.
TLDR
The data demonstrate that distinct signal transduction pathways converge at c‐Jun/ATF‐2, whereby each subunit is individually addressed by a specific class of protein kinases, which allows fine tuned modulation of c‐jun expression by a large spectrum of extracellular signals. Expand
Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro.
TLDR
It is shown that CBP also stimulates the activity of both c-Jun and v-Jun in vivo, consistent with a mechanism by which CBP acts as a co-activator protein for Jun dependent transcription by interacting with the Jun N-terminal activation domain. Expand
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