INT271521

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Context Info
Confidence 0.59
First Reported 2008
Last Reported 2010
Negated 0
Speculated 2
Reported most in Body
Documents 10
Total Number 15
Disease Relevance 11.45
Pain Relevance 0.39

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

cytosol (Ptk2) nucleolus (Ptk2) plasma membrane (Ptk2)
cytoskeleton (Ptk2) nucleus (Ptk2) extracellular matrix organization (Ptk2)
Anatomy Link Frequency
extracellular matrix 1
Ptk2 (Mus musculus)
Pain Link Frequency Relevance Heat
chemokine 63 88.32 High High
cytokine 7 81.60 Quite High
antagonist 16 72.88 Quite High
Hyperalgesia 1 63.12 Quite High
Peripheral nerve injury 1 61.20 Quite High
Central nervous system 17 53.80 Quite High
Hippocampus 1 5.84 Low Low
imagery 19 5.00 Very Low Very Low Very Low
anesthesia 12 5.00 Very Low Very Low Very Low
metalloproteinase 11 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Malignant Neoplastic Disease 54 98.80 Very High Very High Very High
Brain Tumor 16 98.20 Very High Very High Very High
Glioblastoma 83 97.44 Very High Very High Very High
Adhesions 286 97.36 Very High Very High Very High
Cancer 740 96.68 Very High Very High Very High
Death 26 96.44 Very High Very High Very High
Apoptosis 266 96.00 Very High Very High Very High
Breast Cancer 31 95.92 Very High Very High Very High
Targeted Disruption 14 95.00 High High
Melanoma 126 93.40 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These results suggest that hUCBSC regulate FAK levels (both normal as well as phosphorylated forms), and as such, hUCBSC could be used for the treatment of glioblastoma.
Phosphorylation (phosphorylated) of FAK associated with glioblastoma
1) Confidence 0.59 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 1.67 Pain Relevance 0
Our results provide evidence that downregulation of FAK and phosphorylated FAK by hUCBSC resulted in decrease in the expression of VEGF which resulted in the attenuated migration of U251 and 5310 cells, and hence regression of tumor growth in vivo.
Phosphorylation (phosphorylated) of FAK associated with cancer
2) Confidence 0.59 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 0.85 Pain Relevance 0
Integrin recognition of an extracellular matrix ligand typically results in the clustering of the integrin in the cell membrane and, in a temporally related manner, the autophosphorylation of FAK on tyrosine 397 (activation), followed by the formation of focal adhesions at the submembranous region of the cell [4,5].
Phosphorylation (autophosphorylation) of FAK in extracellular matrix associated with adhesions
3) Confidence 0.59 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 0.79 Pain Relevance 0
Our results provide evidence that downregulation of FAK and phosphorylated FAK by hUCBSC resulted in decrease in the expression of VEGF which resulted in the attenuated migration of U251 and 5310 cells, and hence regression of tumor growth in vivo.
Phosphorylation (phosphorylated) of FAK associated with cancer
4) Confidence 0.59 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 0.85 Pain Relevance 0
Then, we analyzed different phospho-forms of FAK, pFAK (Tyr397, Tyr576 and Tyr925).
Spec (analyzed) Phosphorylation (forms) of FAK
5) Confidence 0.59 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 0.78 Pain Relevance 0
Consistent with data in Figure 2A, immunoblot analysis of cells cultured on inserts indicated decreased FAK phosphorylation and total protein in control HT29 cells co-cultured in proximity with CXCL12-secreting cells (Figure 2C).
Phosphorylation (phosphorylation) of FAK
6) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2943927 Disease Relevance 0.25 Pain Relevance 0.10
Of note, treatment with anti-MCSP:sTRAIL was also characterized by a rapid dephosphorylation of key proteins, such as FAK, implicated in MCSP-mediated malignant behavior.
Phosphorylation (dephosphorylation) of FAK associated with malignant neoplastic disease
7) Confidence 0.30 Published 2010 Journal Mol Cancer Section Abstract Doc Link PMC3000402 Disease Relevance 1.13 Pain Relevance 0.04
First and foremost, the previously reported down-stream target of MCSP, FAK, was dephosphorylated by a factor 2 compared to medium control.
Phosphorylation (dephosphorylated) of FAK
8) Confidence 0.30 Published 2010 Journal Mol Cancer Section Body Doc Link PMC3000402 Disease Relevance 0.12 Pain Relevance 0
Together these data mirror our prior work investigating FAK phosphorylation of tyrosine residue 397 [13] and suggest CXCL12 expression has a broad and significant impact on proteins within the focal adhesion complex.
Phosphorylation (phosphorylation) of FAK associated with adhesions
9) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2943927 Disease Relevance 0.72 Pain Relevance 0.03
We determined that phosphorylation of paxillin, FAK, p130Cas, and to a lesser extent Pyk2, decreased rapidly and preceded diminishment in total cellular levels of those proteins in CXCL12-expressing cells (Figure 2A).
Phosphorylation (phosphorylation) of FAK
10) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2943927 Disease Relevance 0.95 Pain Relevance 0.06
The expressions of FAK, phospho-FAK, cSrc, phospho-Src, Arp2, F-actin, paxillin, phospho-paxillin at protein level were reduced with both MU-sh and MC-sh treatments in 5310 cells (Fig. 8B).
Phosphorylation (phospho) of FAK
11) Confidence 0.26 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2904700 Disease Relevance 0.36 Pain Relevance 0
1 integrin after induction of tumorigenesis resulted in impairment of FAK phosphorylation and proliferation consistent with a reliance on anchorage-dependent signaling for tumor growth.
Phosphorylation (phosphorylation) of FAK associated with cancer
12) Confidence 0.23 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2689678 Disease Relevance 1.21 Pain Relevance 0.03
Then, we analyzed different phospho-forms of FAK, pFAK (Tyr397, Tyr576 and Tyr925).
Spec (analyzed) Phosphorylation (forms) of pFAK
13) Confidence 0.23 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 0.78 Pain Relevance 0
The expressions of FAK, phospho-FAK, cSrc, phospho-Src, Arp2, F-actin, paxillin, phospho-paxillin at protein level were reduced with both MU-sh and MC-sh treatments in 5310 cells (Fig. 8B).
Phosphorylation (phospho) of phospho-FAK
14) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2904700 Disease Relevance 0.36 Pain Relevance 0
Echistatin has been found to induce a decrease of both auto-phosphorylation and kinase activity of pp125FAK, suggesting inhibitory activity in processes integral to angiogenesis, such as cell growth, survival, and migration (Della et al. 2000).
Phosphorylation (phosphorylation) of pp125FAK
15) Confidence 0.21 Published 2008 Journal Perspectives in Medicinal Chemistry Section Body Doc Link PMC2746574 Disease Relevance 0.61 Pain Relevance 0.13

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