INT169911

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Context Info
Confidence 0.73
First Reported 2001
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 35
Total Number 36
Disease Relevance 18.58
Pain Relevance 0.79

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
RG2 2
B-cell 1
M cell 1
bands 1
epithelial cell 1
Rb1 (Mus musculus)
Pain Link Frequency Relevance Heat
Potency 40 91.76 High High
imagery 92 89.76 High High
Inflammation 114 84.36 Quite High
cytokine 27 83.68 Quite High
Kinase C 2 78.48 Quite High
Angina 22 70.24 Quite High
agonist 67 64.20 Quite High
Spinal cord 8 49.32 Quite Low
fibrosis 2 42.80 Quite Low
tolerance 6 34.72 Quite Low
Disease Link Frequency Relevance Heat
Cancer 1064 100.00 Very High Very High Very High
Retinoblastoma 30 100.00 Very High Very High Very High
Targeted Disruption 69 99.40 Very High Very High Very High
Apoptosis 422 99.30 Very High Very High Very High
Repression 71 98.68 Very High Very High Very High
Neurofibromatosis 2 18 98.26 Very High Very High Very High
Glioblastoma 266 96.80 Very High Very High Very High
Brain Tumor 82 93.88 High High
Pituitary Cancer 40 93.44 High High
Malignant Neoplastic Disease 67 93.40 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Conversely, in proliferating cells, pRB is phosphorylated at multiple sites by cyclin-dependent kinases [31,32], resulting in the release of E2F1 and, consequently, transcriptional activation of its target genes [33].
Phosphorylation (phosphorylated) of pRB
1) Confidence 0.73 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.43 Pain Relevance 0
There are extensive studies on the relation between specific phosphorylation sites on pRb and its potential transcription repression [32,33,34].
Phosphorylation (phosphorylation) of pRb associated with repression
2) Confidence 0.72 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 Pain Relevance 0
SAHA treatment resulted in G1 cell growth arrest in TM10 and TM2H cell lines, concomitant with the profound increase in dephosphorylation of the three pRb pocket proteins.
Phosphorylation (dephosphorylation) of pRb
3) Confidence 0.72 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.09 Pain Relevance 0
Results suggested that SAHA induced cell growth arrest through dephosphorylation of three pRb pocket proteins, which may be related to inhibition in G1/S phase cdk activities.


Phosphorylation (dephosphorylation) of pRb
4) Confidence 0.72 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.08 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]).
Phosphorylation (phosphorylation) of pRb
5) Confidence 0.72 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 Pain Relevance 0
SAHA also resulted in the inhibition of G1/S kinase activities and, consequently, hypophosphorylation of the three pRb pocket proteins, which led to G1 cell growth arrest and dramatic decreases in DNA synthesis in both cell lines.
Phosphorylation (hypophosphorylation) of pRb
6) Confidence 0.72 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.05 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]).
Phosphorylation (phosphorylation) of pRb
7) Confidence 0.72 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 Pain Relevance 0
The p15ink4b protein phosphorylates and inactivates the retinoblastoma tumor suppressor (pRb) protein [22].
Phosphorylation (phosphorylates) of retinoblastoma associated with cancer and retinoblastoma
8) Confidence 0.61 Published 2010 Journal PLoS Genetics Section Body Doc Link PMC2883590 Disease Relevance 0.62 Pain Relevance 0.03
The anti-angiogenic effects of TSP1 may also be CD36 independent, it suppresses the cell cycle, increasing p21 and unphosphorylated retinoblastoma (Rb) in EC.(34) Many receptors interact with specific binding sites of TSP1.
Phosphorylation (unphosphorylated) of retinoblastoma associated with retinoblastoma
9) Confidence 0.61 Published 2008 Journal Biomarker Insights Section Body Doc Link PMC2600574 Disease Relevance 0.47 Pain Relevance 0.07
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]).
Phosphorylation (phosphorylated) of pRb
10) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 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]).
Phosphorylation (phosphorylation) of pRb
11) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 Pain Relevance 0
The difference in the level of hypophosphorylated pRb pocket protein isoforms between the two cell lines treated with SAHA may be attributed to differences in G1 and S phase cdk activity (examined in the following section).
Phosphorylation (hypophosphorylated) of pRb
12) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.06 Pain Relevance 0
The phosphorylated H1 and pRb bands were scanned and quantitated densitometrically using a Phosphoimager (Molecular Dynamics, Sunnyvle, CA, USA).


Phosphorylation (phosphorylated) of pRb in bands
13) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0 Pain Relevance 0
Phosphorylation of three major pocket proteins, Rb, p107 and Rb2/p130, were examined after SAHA treatment, as each pocket protein affects the G1 and S phases of the cell cycle.
Phosphorylation (Phosphorylation) of Rb
14) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0 Pain Relevance 0.03
We have previously reported that the prototype HPC (hexamethylene bisacetamide [HMBA]) was able to arrest the growth of transformed mammary (TM) 2H cells (p53 null), a highly tumorigenic mouse mammary epithelial cell line, by inhibiting G1 kinase activities, concomitant with an increase in the cyclin D2 protein level and hypophosphorylated isoforms of the three pRb pocket proteins, which led to the formation of stable cyclin D2/pRb complexes and G1 cell arrest.
Phosphorylation (hypophosphorylated) of pRb in epithelial cell
15) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.22 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]).
Phosphorylation (phosphorylation) of pRb
16) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.10 Pain Relevance 0
M SAHA may result in disintegration and deactivation of D1, E and A cdk2 complexes, which consequently leads to hypophosphorylation of the three Rb pocket proteins.
Phosphorylation (hypophosphorylation) of Rb
17) Confidence 0.55 Published 2001 Journal Breast Cancer Res Section Body Doc Link PMC13923 Disease Relevance 0.08 Pain Relevance 0
The p16INK4a/p14ARF locus encodes two distinct cell cycle inhibitory proteins, p16INK4a and p14ARF (p19Arf in the mouse) by alternative first-exon usage and alternative reading frames (20). p16INK4a arrests cells in the G1 phase of the cell cycle by binding the cyclin-dependant kinases CDK4 and CDK6 and inhibiting their ability to phosphorylate and inactivate the retinoblastoma (RB1) family of tumor suppressor proteins (22). p14ARF acts through MDM2 to stabilize and activate the key checkpoint protein p53, which can arrest cells in both G1 and G2 or induce apoptosis (20).
Phosphorylation (phosphorylate) of RB1 associated with cancer, apoptosis and retinoblastoma
18) Confidence 0.42 Published 2008 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC2253711 Disease Relevance 1.17 Pain Relevance 0
It has been shown previously that NF2 expression induces a decrease in cyclin D1 and CDK4 kinase activity, concomitant with dephosphorylation of pRB and reduced DNA synthesis (9, 28).
Phosphorylation (dephosphorylation) of pRB associated with neurofibromatosis 2
19) Confidence 0.37 Published 2008 Journal Brain Pathology (Zurich, Switzerland) Section Body Doc Link PMC2253711 Disease Relevance 1.18 Pain Relevance 0
The p15ink4b protein phosphorylates and inactivates the retinoblastoma tumor suppressor (pRb) protein [22].
Phosphorylation (phosphorylates) of pRb associated with cancer and retinoblastoma
20) Confidence 0.32 Published 2010 Journal PLoS Genetics Section Body Doc Link PMC2883590 Disease Relevance 0.63 Pain Relevance 0.03

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