INT169930

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Context Info
Confidence 0.43
First Reported 2001
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 15
Total Number 15
Disease Relevance 5.91
Pain Relevance 0.16

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

nucleus (Rb1) enzyme binding (Rb1) cell cycle (Rb1)
DNA binding (Rb1) cell division (Rb1) transcription factor binding (Rb1)
Anatomy Link Frequency
neuronal 1
pituitary 1
Rb1 (Mus musculus)
Pain Link Frequency Relevance Heat
interstitial cystitis 3 89.40 High High
Inflammation 43 80.60 Quite High
cytokine 1 67.60 Quite High
Paracetamol 2 49.48 Quite Low
cINOD 17 46.64 Quite Low
Potency 8 21.08 Low Low
headache 9 5.00 Very Low Very Low Very Low
Inflammatory response 4 5.00 Very Low Very Low Very Low
ketamine 1 5.00 Very Low Very Low Very Low
Inflammatory stimuli 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Retinoblastoma 24 100.00 Very High Very High Very High
Shock 4 100.00 Very High Very High Very High
Repression 38 98.60 Very High Very High Very High
Targeted Disruption 125 98.24 Very High Very High Very High
Cancer 80 97.68 Very High Very High Very High
Pituitary Cancer 243 96.56 Very High Very High Very High
Interstitial Cystitis 3 89.40 High High
Diabetes Mellitus 4 82.16 Quite High
Renal Disease 1 81.16 Quite High
INFLAMMATION 57 80.60 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
It would be very interesting to know whether the same mechanism may be induced by other proteins able to bind to the pRB complex and thereby are involved in pituitary tumorigenesis.
pRB Binding (bind) of in pituitary
1) Confidence 0.43 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.38 Pain Relevance 0
pRB controls cell cycle progression through its interaction with the E2F family of transcription factors [26,27], whose activity is crucial for the expression of several genes required to enter the S phase of the cell cycle [28,29].
pRB Binding (interaction) of
2) Confidence 0.43 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.60 Pain Relevance 0
These results suggest that the binding between HMGA2 and pRB may be generally involved in HMGA2-mediated cell transformation.


pRB Binding (binding) of
3) Confidence 0.43 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.23 Pain Relevance 0
S transition and DNA synthesis [1,2,3,4,5], whereas complex formation with pRb or other pocket proteins including p107 and pRb-2/p130 silences transcriptional activities of downstream target genes [6,7,8,9,10].
pRb Binding (formation) of
4) Confidence 0.42 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.16 Pain Relevance 0
It is well known that pRb phosphorylation sites are recognized by specific cdks [33], and that most of the 16 pRb-phosphorylation sites are sequentially phosphorylated throughout the cell cycle (reviewed in [34,35]).
pRb Binding (recognized) of
5) Confidence 0.42 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 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].
Retinoblastoma Binding (interaction) of associated with retinoblastoma
6) Confidence 0.36 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.44 Pain Relevance 0
The transcriptional activity of E2F1 is repressed in non-proliferating cells by its interaction with pRB that masks the activation domain of E2F1, and prevents it to contact the general transcription machinery [30].
pRB Binding (interaction) of
7) Confidence 0.33 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.58 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".
pRB Binding (interaction) of
8) Confidence 0.33 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.35 Pain Relevance 0
Interestingly, we found that the interaction between HMGA2 and pRB is crucial for the transforming activity of HMGA2 protein.
pRB Binding (interaction) of
9) Confidence 0.33 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.30 Pain Relevance 0
However, what appears to be really novel, is the mechanism that leads to E2F1 activation by HMGA2: the E2F1 protein is not displaced from the pRB complex, but an increased acetylation that is dependent on the removal of HDAC1 from pRB takes place.
pRB Binding (complex) of
10) Confidence 0.33 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.46 Pain Relevance 0
S transition and DNA synthesis [1,2,3,4,5], whereas complex formation with pRb or other pocket proteins including p107 and pRb-2/p130 silences transcriptional activities of downstream target genes [6,7,8,9,10].
pRb Binding (formation) of
11) Confidence 0.33 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.22 Pain Relevance 0
The resulting retinoblastoma protein (Rb)–E2F interaction not only blocks transcriptional activation by E2F, but also forms an active transcriptional repressor complex at the promoter of cell cycle genes that can block transcription by recruiting histone deacetylase (HDAC) and remodeling chromatin [11,12,13,14].
Rb Binding (interaction) of associated with retinoblastoma
12) Confidence 0.33 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.33 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.
pRB Binding (interaction) of
13) Confidence 0.32 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.79 Pain Relevance 0
E2F family members are functionally regulated, in part, by complex formation with one or more members of the nuclear pocket protein family such as the retinoblastoma protein (Rb) and play a role in neuronal development [90] by acting as negative regulator of cell proliferation.
Rb Binding (formation) of in neuronal associated with retinoblastoma
14) Confidence 0.06 Published 2006 Journal BMC Physiol Section Body Doc Link PMC1382248 Disease Relevance 0.69 Pain Relevance 0.13
Although NCoA6 was initially cloned as coactivator protein for NRs, its detailed characterization by a number of laboratories has uncovered its potential to enhance the activity of a wide variety of other transcription factors including c-Fos, c-Jun, CREB, NF-kB, ATF-2, heat shock factors, E2F-1, SRF, and Rb, p53 and Sox9 [Goo et al., 2004; Hong et al., 2004a; Hong et al., 2004b; Ko et al., 2000; Kong et al., 2003; Lee et al., 1999; Lee et al., 2000; Mahajan et al., 2007; Mahajan et al., 2002; Mahajan and Samuels, 2000; Mahajan and Samuels, 2005].
Rb Binding (enhance) of associated with shock
15) Confidence 0.04 Published 2008 Journal Nuclear Receptor Signaling Section Body Doc Link PMC2254332 Disease Relevance 0.27 Pain Relevance 0.03

General Comments

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