Gene interactions and pathways from curated databases and text-mining

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TOP1 — TP53

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

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Gobert et al., Proc Natl Acad Sci U S A 1999 (Breast Neoplasms) : We now report that topoisomerase I can be stimulated by both latent and activated wild-type p53 as well as by several mutant and truncated p53 proteins in vitro, indicating that sequence-specific DNA binding and stimulation of topoisomerase I are distinct properties of p53
Søe et al., Oncogene 2002 : Stimulation of topoisomerase I activity by p53 is mediated via the central part of topoisomerase I ... We also show that human, bovine, and murine p53 stimulate human topoisomerase I relaxation activity equally well
Søe et al., Nucleic Acids Res 2003 : p53 stimulates human topoisomerase I activity by modulating its DNA binding ... However, little was known about how p53 stimulates this topoisomerase I activity ... Here we demonstrate that monomeric p53 is sufficient for the stimulation of the topoisomerase I-catalyzed relaxation activity, but the tetrameric form of p53 is required for the stimulation of TIRR
Crea et al., Mol Cancer Ther 2009 (Colorectal Neoplasms) : In contrast, 5-aza down-regulated Top-I expression in the p53 wild-type LS174T cells in a p53 dependent manner, thereby reducing SN38 cytotoxicity
Huang et al., Cell Res 2010 : Interestingly, the TIP pathway was important for TOP1cc activated, but not ionization radiation activated ATM, p53 and Chk2 phosphorylation
Gobert et al., Biochemistry 1996 (Breast Neoplasms) : In vitro experiments with purified recombinant proteins show that p53 increases the catalytic activities of topoisomerase I as measured by relaxation of supercoiled DNA, stabilization of the covalent topoisomerase I-DNA complex ( in the presence of camptothecin ), and phosphorylation of SR protein splicing factor ASF/SF2
Albor et al., Cancer Res 1998 : Wild-type and mutant forms of p53 activate human topoisomerase I : a possible mechanism for gain of function in mutants