INT196961

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Context Info
Confidence 0.48
First Reported 2006
Last Reported 2006
Negated 1
Speculated 0
Reported most in Body
Documents 1
Total Number 13
Disease Relevance 6.47
Pain Relevance 0

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

enzyme binding (Hmga2, Rb1) DNA binding (Hmga2, Rb1) nucleus (Hmga2, Rb1)
cell cycle (Hmga2, Rb1) cell division (Hmga2, Rb1) transcription factor binding (Hmga2, Rb1)
Anatomy Link Frequency
pituitary 1
fibroblasts 1
Hmga2 (Mus musculus)
Rb1 (Mus musculus)
Pain Link Frequency Relevance Heat
headache 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Retinoblastoma 26 100.00 Very High Very High Very High
Pituitary Cancer 351 99.20 Very High Very High Very High
Targeted Disruption 143 98.24 Very High Very High Very High
Cancer 39 97.68 Very High Very High Very High
Prolactinoma 39 90.32 High High
Adenoma 52 87.04 High High
Benign Tumor 13 83.40 Quite High
Repression 26 79.84 Quite High
Malignant Neoplastic Disease 13 69.32 Quite High
Syndrome 13 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In fact, in a focus assay on rat fibroblasts, HMGA2 mutants unable to bind pRB lost the capacity of the wild-type gene to transform cells.
HMGA2 Neg (unable) Binding (bind) of pRB in fibroblasts
1) Confidence 0.48 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.18 Pain Relevance 0
HMGA2 binds to pRB and inhibits its function
HMGA2 Binding (binds) of pRB
2) Confidence 0.48 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.75 Pain Relevance 0
Using competitions with recombinant proteins and Chromatin Immonoprecipitation (ChIP) experiments, we demonstrated that following the binding of HMGA2 to pRB (Figure 2, step1), HDAC1 is displaced from the E2F1-target promoters (Figure 2, step 2) where it was recruited by pRB [34].
HMGA2 Binding (binding) of pRB
3) Confidence 0.42 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.23 Pain Relevance 0
Based on the striking mirror similarities between the phenotypes of pRB [22,35] and HMGA2 [36,37] animal models, our group has recently investigated a potential functional interaction between HMGA2 and the Retinoblastoma protein [38].
HMGA2 Binding (interaction) of Retinoblastoma associated with retinoblastoma
4) Confidence 0.39 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.44 Pain Relevance 0
Interestingly, we found that the interaction between HMGA2 and pRB is crucial for the transforming activity of HMGA2 protein.
HMGA2 Binding (interaction) of pRB
5) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.30 Pain Relevance 0
Interestingly, we found that the interaction between HMGA2 and pRB is crucial for the transforming activity of HMGA2 protein.
HMGA2 protein Binding (interaction) of pRB
6) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.30 Pain Relevance 0
Interestingly, we found that the interaction between HMGA2 and pRB is crucial for the transforming activity of HMGA2 protein.
HMGA2 protein Binding (interaction) of pRB
7) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.30 Pain Relevance 0
Thus, even though HMGA2 is still able to bind pRB in the absence of E2F1, there are no other proteins belonging to the E2F family, whose DNA binding activity is enhanced following the HMGA2/pRB interaction.
HMGA2 Binding (interaction) of pRB
8) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.79 Pain Relevance 0
Interestingly, even in pituitary adenomas developed by HMGA2 mice lacking E2F1 the interaction between HMGA2 and pRB was present, however, the E2F "free" DNA binding activity did not show any significant increase compared to control wild-type glands.
HMGA2 Binding (interaction) of pRB in pituitary associated with pituitary cancer
9) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.93 Pain Relevance 0
Thus, even though HMGA2 is still able to bind pRB in the absence of E2F1, there are no other proteins belonging to the E2F family, whose DNA binding activity is enhanced following the HMGA2/pRB interaction.
HMGA2 Binding (bind) of pRB
10) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.87 Pain Relevance 0
These results suggest that the binding between HMGA2 and pRB may be generally involved in HMGA2-mediated cell transformation.


HMGA2 Binding (binding) of pRB
11) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.23 Pain Relevance 0
Interestingly, this positive role of HMGA2 on cell proliferation is due to the interaction with pRB, opening a new class of cell cycle related proteins: "the suppressors of the cell cycle inhibitors".
HMGA2 Binding (interaction) of pRB
12) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.36 Pain Relevance 0
Thus, even though HMGA2 is still able to bind pRB in the absence of E2F1, there are no other proteins belonging to the E2F family, whose DNA binding activity is enhanced following the HMGA2/pRB interaction.
HMGA2 Binding (interaction) of pRB
13) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.79 Pain Relevance 0

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