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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 *
-
IRef Biogrid Interaction:
TOP1
—
TP53
(physical association, affinity chromatography technology)
Gobert et al., Proc Natl Acad Sci U S A 1999*
-
IRef Biogrid Interaction:
TOP1
—
TP53
(direct interaction, two hybrid)
Mao et al., Proc Natl Acad Sci U S A 2002*
-
IRef Hprd Interaction:
TP53
—
TOP1
(in vivo)
Gobert et al., Proc Natl Acad Sci U S A 1999*, Gobert et al., Biochemistry 1996*
-
IRef Hprd Interaction:
TP53
—
TOP1
(in vitro)
Gobert et al., Proc Natl Acad Sci U S A 1999*, Gobert et al., Biochemistry 1996*
-
IRef Ophid Interaction:
TP53
—
TOP1
(aggregation, confirmational text mining)
Gobert et al., Proc Natl Acad Sci U S A 1999*
-
IRef Ophid Interaction:
TP53
—
TOP1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
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