IndraLab

Statements

TP53 binds FHIT and MDM2. 12 / 12
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sparser
"Since there is a possibility that FHIT and p53 might interact with MDM2 in a competitive way, we have also investigated the interaction of triple protein complex FHIT, MDM2 and p53 in two stages."
25221773
sparser
"Docking results indicate that interaction of full FHIT with p53 (E-total: -568.66) and MDM2 (E-total: -459.53) is accompanied with lower total energy compared to the interaction of the complete MDM2 with p53 (E-total: -399.25)."
25221773
sparser
"Since there is a probability that FHIT and p53 might interact with MDM2 in a competitive way, we have also examined the interaction of triple protein complex FHIT, MDM2 optimized model and p53 optimized part in two stages."
24834308
sparser
"Studies have confirmed FHIT interaction with p53 or MDM2, although functional interacting domains of FHIT with MDM2 and/or p53 are not completely defined."
24834308
sparser
"Constructing these important FHIT segments and subsequently utilizing them will provide further in vitro data regarding FHIT-MDM2-p53 interaction in cancerous cell."
25221773
sparser
"Thus, finding the recognition site of FHIT-MDM2 interaction with p53 binding, one can assess the interaction and/or competition among these proteins for a therapeutical approach."
25221773
sparser
"This information can be used to propose novel drugs function as FHIT in the FHIT-MDM2-p53 protein interaction complex that will result in tumor repression."
31089360
reach
"These findings are beneficial to understand the mechanism of the FHIT, MDM2, and p53 complex activation for designing inhibitory compounds."
25221773
sparser
"Thus, it is logical to consider that FHIT and p53 have binding sites on MDM2 and perhaps these proteins could influence each other in binding to MDM2."
24834308
sparser
"The results of our previous docking study indicate that interaction of full FHIT with p53 (E-total: -568.66) and MDM2 (E-total: -459.53) is associated with lower total energy compared to the interaction of the complete MDM2 with p53 (E-total: -399.25)."
24834308
sparser
"Accumulating evidences indicate FHIT interaction with p53 or MDM2; however, there is no certain study deciphering functional domains of FHIT involving in the interaction with MDM2 and/or p53."
25221773
reach
"In addition, a comparison of the interaction site and functional domains in regard to expression rate and/or destruction of p53 will shed light on the molecular mechanism of the FHIT, MDM2, and p53 complex."
25221773