Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA.

By A. Ryo, Futoshi Suizu, Y. Yoshida, K. Perrem, Y. Liou, G. Wulf, R. Rottapel, S. Yamaoka, K. Lu. Molecules and Cells, 2003

684 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d4d28195f8398ce8b19d9983b39abc51c660ff28

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Citations in the corpus

IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300 (2006, background): “RelA/p65 is known to be degraded through ubiquitin-dependent mechanisms ( 54 ), and NF-B transcription has been proposed to be terminated through ubiquitin-mediated targeting of chromatin-bound RelA/p65 (55).”
The Regulation of NF-κB Subunits by Phosphorylation (2016, background): “S205 unknown transactivation [76] T254 unknown prolyl isomerisation, transactivation [77,78]”
The complexity of NF-κB signaling in inflammation and cancer (2013, neutral): “unknown T254 stabilization and nuclear localization [71]”
New regulators of NF-κB in inflammation (2008, background): “Independently of its role in regulating cytoplasmic signalling pathways, overexpression of SOCS1 decreases p65 stabilit”
Good cop, bad cop: the different faces of NF-κB (2006, background): “proteolysis is also induced by ubiquitination between residues 220 and 335.(49) This effect is involved in the termination of the NF-kB response and is mediated by SOCS-1, a ubiquitin”
NF-κB activation as a pathological mechanism of septic shock and inflammation (2006, neutral): “Proteasome-mediated proteolysis of p65 protein reduces its nuclear concentration and, thus, NF- B activity (205).”
Cytokine signaling modules in inflammatory responses. (2008, background): “This finding led to the idea that Socs1 additionally regulates components of the TLR cascade, including IRAK1 and the p65 subunit of NF-kB (Kinjyo et al., 2002; Nakagawa et al., 2002; Ryo et al., 2003).”