INT289608

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.06
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 12
Disease Relevance 4.89
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.

nucleoplasm (CDK2, CCNE2) cytosol (CDK2, CCNE2) nucleus (CDK2, CCNE2)
cell division (CDK2, CCNE2) endosome (CDK2) cytoplasm (CDK2)
Anatomy Link Frequency
HL-60 1
CDK2 (Homo sapiens)
CCNE2 (Homo sapiens)
Pain Link Frequency Relevance Heat
Inflammation 16 5.00 Very Low Very Low Very Low
cINOD 8 5.00 Very Low Very Low Very Low
palliative 3 5.00 Very Low Very Low Very Low
Inflammatory response 1 5.00 Very Low Very Low Very Low
Pain 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Genomic Instability 6 95.80 Very High Very High Very High
Cancer 554 93.80 High High
Breast Cancer 369 91.40 High High
Glioma 208 89.72 High High
Apoptosis 90 88.96 High High
Hyperplasia 16 81.04 Quite High
Retinoblastoma 8 74.76 Quite High
Malignant Neoplastic Disease 18 69.72 Quite High
Death 13 66.92 Quite High
Colon Cancer 16 59.64 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Two proteins codified by two different genes but with high homology, called cyclin E1 (formerly cyclin E) and cyclin E2 have been identified.173–177 Cyclin E2, like cyclin E1, associates with Cdk2 and activates its kinase activity at the G1/S boundary.176 Cyclin E2 shares 47% overall similarity to cyclin E1; whether its structural features outside the conserved regions reveal unique functions is unknown.176
Cdk2 Binding (associates) of Cyclin E2
1) Confidence 0.06 Published 2010 Journal Clinical Medicine Insights. Oncology Section Body Doc Link PMC2883240 Disease Relevance 0.70 Pain Relevance 0
Two proteins codified by two different genes but with high homology, called cyclin E1 (formerly cyclin E) and cyclin E2 have been identified.173–177 Cyclin E2, like cyclin E1, associates with Cdk2 and activates its kinase activity at the G1/S boundary.176 Cyclin E2 shares 47% overall similarity to cyclin E1; whether its structural features outside the conserved regions reveal unique functions is unknown.176
Cdk2 Binding (associates) of cyclin E
2) Confidence 0.06 Published 2010 Journal Clinical Medicine Insights. Oncology Section Body Doc Link PMC2883240 Disease Relevance 0.71 Pain Relevance 0
Two proteins codified by two different genes but with high homology, called cyclin E1 (formerly cyclin E) and cyclin E2 have been identified.173–177 Cyclin E2, like cyclin E1, associates with Cdk2 and activates its kinase activity at the G1/S boundary.176 Cyclin E2 shares 47% overall similarity to cyclin E1; whether its structural features outside the conserved regions reveal unique functions is unknown.176
Cdk2 Binding (associates) of cyclin E2
3) Confidence 0.04 Published 2010 Journal Clinical Medicine Insights. Oncology Section Body Doc Link PMC2883240 Disease Relevance 0.71 Pain Relevance 0
Based on our understanding of the mechanisms of DMSO and ATRA signaling in HL-60 cells, we know that the point at which these pathways converge is at the G1-S phase transition point controlled by the cyclin dependent kinase complex of Cyclin E and CDK2.
CDK2 Binding (complex) of Cyclin E in HL-60
4) Confidence 0.04 Published 2009 Journal PLoS Computational Biology Section Body Doc Link PMC2791157 Disease Relevance 0.21 Pain Relevance 0
In the present study, we show that the co-depletion of cathepsin B and uPAR arrests cells in the G1 phase primarily through the upregulation of p27Kip1 and that this pathway involves the downregulation of p-PI3K, p-AKT, D-type cyclin expression, and cyclin E/Cdk2 complex formation as well as the subsequent upregulation of the FOXO3a protein and its nuclear localization.
Cdk2 Binding (formation) of cyclin E
5) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908539 Disease Relevance 0.60 Pain Relevance 0
Of note, the Cdk2-cyclin E complex formation was reduced significantly.


Cdk2 Binding (formation) of cyclin E
6) Confidence 0.01 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2908539 Disease Relevance 0.25 Pain Relevance 0
Similar results showing that SHP1 downregulation effected p27Kip1 expression and Cdk2-cyclin E complex formation have been reported [43].
Cdk2 Binding (formation) of cyclin E
7) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908539 Disease Relevance 0.12 Pain Relevance 0
Therefore, the G0/G1 arrest induced by the treatments could be due to the combined action of reduced cyclin D1, cyclin D2, and cyclin E-Cdk2 complex formation and increased expression of p27Kip1.
Cdk2 Binding (formation) of cyclin E
8) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908539 Disease Relevance 0.31 Pain Relevance 0
In the present study, we show that the co-depletion of cathepsin B and uPAR arrests cells in the G1 phase primarily through the upregulation of p27Kip1 and that this pathway involves the downregulation of p-PI3K, p-AKT, D-type cyclin expression, and cyclin E/Cdk2 complex formation as well as the subsequent upregulation of the FOXO3a protein and its nuclear localization.
Cdk2 Binding (formation) of cyclin E
9) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908539 Disease Relevance 0.60 Pain Relevance 0
Of note, the Cdk2-cyclin E complex formation was reduced significantly.


Cdk2 Binding (formation) of cyclin E
10) Confidence 0.01 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2908539 Disease Relevance 0.25 Pain Relevance 0
Similar results showing that SHP1 downregulation effected p27Kip1 expression and Cdk2-cyclin E complex formation have been reported [43].
Cdk2 Binding (formation) of cyclin E
11) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908539 Disease Relevance 0.12 Pain Relevance 0
Therefore, the G0/G1 arrest induced by the treatments could be due to the combined action of reduced cyclin D1, cyclin D2, and cyclin E-Cdk2 complex formation and increased expression of p27Kip1.
Cdk2 Binding (formation) of cyclin E
12) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2908539 Disease Relevance 0.31 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox