Gene interactions and pathways from curated databases and text-mining

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PERP — TP53

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

  • STRING interaction: TP53 — PERP (interaction, mapped from intact)
  • STRING interaction: PERP — TP53 (interaction, mapped from intact)

Text-mined interactions from Literome

Attardi et al., Genes Dev 2000 : Here, we describe the characterization of a gene identified in this screen, PERP , which is expressed in a p53 dependent manner and at high levels in apoptotic cells compared with G ( 1 ) -arrested cells ... Furthermore, analysis of the PERP promoter suggests that PERP is directly activated by p53
Chao et al., EMBO J 2000 : p53 ( Gln25Ser26 ) was stable but did not accumulate after DNA damage ; the expression of p21/Waf1 and PERP was not induced , and p53 dependent repression of MAP4 expression was abolished
Ihrie et al., Curr Biol 2003 : Thus, Perp selectively mediates the p53 apoptotic response, and the requirement for Perp is dictated by cellular context
Reczek et al., Mol Cancer Res 2003 : Here, we describe the regulation of the Perp gene by p53 through at least three response elements in the Perp promoter and first intron
Paraoan et al., Exp Eye Res 2006 (Melanoma...) : Expression of p53 induced apoptosis effector PERP in primary uveal melanomas : downregulation is associated with aggressive type
Singaravelu et al., American journal of physiology. Renal physiology 2009 (Disease Models, Animal...) : These data suggest that PERP is a key effector of p53 mediated apoptotic pathways and is a potential therapeutic target for renal IRI
Davies et al., Cell death & disease 2011 (Melanoma...) : PERP expression stabilizes active p53 via modulation of p53-MDM2 interaction in uveal melanoma cells ... Using fluorescent fusion proteins of PERP, p53 and MDM2, we demonstrate in single living UM cells that PERP expression significantly enhances p53 activity and its nuclear localization, increases p53 dependent transcription ( including that of MDM2 ) while allowing oscillatory nucleo-cytoplasmic shuttling of p53/MDM2 complexes