INT87345

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.82
First Reported 2000
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 110
Total Number 111
Disease Relevance 59.39
Pain Relevance 4.28

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

extracellular matrix organization (PTK2) embryo development (PTK2) microtubule organizing center (PTK2)
cytoplasm (PTK2) signal transducer activity (PTK2) cytosol (PTK2)
Anatomy Link Frequency
AsPC-1 18
myometrium 4
MCF7 3
colon 2
liver 1
PTK2 (Homo sapiens)
Pain Link Frequency Relevance Heat
Opioid 36 99.82 Very High Very High Very High
Kappa opioid receptor 8 99.42 Very High Very High Very High
Kinase C 4 98.52 Very High Very High Very High
cINOD 27 98.08 Very High Very High Very High
antagonist 99 95.48 Very High Very High Very High
metalloproteinase 45 89.64 High High
MU agonist 4 87.00 High High
opioid receptor 5 85.16 High High
agonist 22 80.64 Quite High
Neurotransmitter 4 63.64 Quite High
Disease Link Frequency Relevance Heat
Pancreatic Cancer 4143 100.00 Very High Very High Very High
Adhesions 1175 100.00 Very High Very High Very High
Cancer 1927 99.92 Very High Very High Very High
Colon Cancer 55 99.60 Very High Very High Very High
Malignant Neoplastic Disease 218 99.28 Very High Very High Very High
Apoptosis 3425 98.96 Very High Very High Very High
Skin Cancer 42 96.92 Very High Very High Very High
Metastasis 461 96.72 Very High Very High Very High
Breast Cancer 151 96.40 Very High Very High Very High
Bordatella Infection 2 95.70 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These drugs also reduced the tyrosine phosphorylation of FAK and an associated factor, p130Cas.
Phosphorylation (phosphorylation) of FAK
1) Confidence 0.82 Published 2000 Journal Clin. Cancer Res. Section Abstract Doc Link 10741720 Disease Relevance 0.86 Pain Relevance 0.27
However, FAK related non-kinase (FRNK) can compete with FAK for focal adhesion binding sites and thus specifically inhibit FAK phosphorylation and downstream signaling without changing expression [19-21].
Phosphorylation (phosphorylation) of FAK associated with adhesions
2) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 1.00 Pain Relevance 0
The C-terminal non-catalytic domain of FAK termed FRNK functions as a competitive inhibitor of FAK and ectopic expression of FRNK specifically inhibits FAK autophosphorylation at Tyr397 and thus attenuates its activity [19,20].
Phosphorylation (autophosphorylation) of FAK
3) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.65 Pain Relevance 0
We used PF-228 to downregulate constitutive FAK phosphorylation in Panc-1 cells and LN-induced FAK phosphorylation in Aspc-1 cells respectively.
Phosphorylation (phosphorylation) of FAK
4) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.37 Pain Relevance 0
As expected, inhibition of constitutive FAK phosphorylation by PF-228 also decreased the intrinsic chemoresistance to Gem in Panc-1 cells.
Phosphorylation (phosphorylation) of FAK
5) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.82 Pain Relevance 0
We used PF-228 to downregulate constitutive FAK phosphorylation in Panc-1 cells and LN-induced FAK phosphorylation in Aspc-1 cells respectively.
Phosphorylation (phosphorylation) of FAK
6) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.36 Pain Relevance 0
These results indicate that induced FAK phosphorylation is involved in LN-mediated chemoresistance to Gem and further confirm FAK as a promising therapeutic target in pancreatic cancer.
Phosphorylation (phosphorylation) of FAK associated with pancreatic cancer
7) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.49 Pain Relevance 0
We demonstrated herein that specific RNAi against FAK reduced FAK expression, decreased FAK phosphorylation and thus suppressed the intrinsic chemoresistance to Gem in Panc-1 cells, which had a high level of pFAK (pY397).
Phosphorylation (phosphorylation) of FAK
8) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.51 Pain Relevance 0
The effect of LN on Akt activation was almost completely blocked by inhibition of FAK phosphorylation through either FAK RNAi or FRNK overexpression (Fig. 7A-B).
Phosphorylation (phosphorylation) of FAK
9) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.21 Pain Relevance 0
These results clearly showed that, inhibition of constitutive FAK phosphorylation was sufficient to render Panc-1 cells more chemosensitive to Gem.
Phosphorylation (phosphorylation) of FAK
10) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.43 Pain Relevance 0
It specifically blocks FAK phosphorylation and thus targets FAK catalytic activity.
Phosphorylation (phosphorylation) of FAK
11) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.41 Pain Relevance 0
In our study, corresponding with the alteration of Akt, pBad (pS136) was regulated by constitutive and induced FAK phosphorylation in pancreatic cancer cells.
Phosphorylation (phosphorylation) of FAK associated with pancreatic cancer
12) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.88 Pain Relevance 0
Small molecule inhibitors of FAK phosphorylation (such as PF-573,228, PF-562,271, TAE226, 1,2,4,5-Benzenetetraamine tetrahydrochloride) have been developed in recent years [22,38-40].
Phosphorylation (phosphorylation) of FAK
13) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.57 Pain Relevance 0
Upon integrin binding to ECM or other stimuli, FAK is autophosphorylated at Tyr397, which provides a high-affinity docking site for several proteins including the p85 subunit of PI3K and the Src kinase.
Phosphorylation (autophosphorylated) of FAK
14) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.25 Pain Relevance 0
These results indicated that in AsPC-1 cells, LN-induced FAK phosphorylation mediated the intrinsic chemoresistance to Gem, and this effect might be related with the regulation of survivin and pBad (pS136) level

Effects of PF-228 on Gem-induced apoptosis in pancreatic cancer cells

Phosphorylation (phosphorylation) of FAK in AsPC-1 associated with pancreatic cancer and apoptosis
15) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.52 Pain Relevance 0
Src can further phosphorylate FAK at several additional sites, including Tyr925.
Phosphorylation (phosphorylate) of FAK
16) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.13 Pain Relevance 0
Our research showed that specific inhibition of constitutive FAK phosphorylation decreased Akt but not ERK phosphorylation in Panc-1 cells.
Phosphorylation (phosphorylation) of FAK
17) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.23 Pain Relevance 0
Moreover, inhibition of FAK phosphorylation by FRNK overexpression antagonized the effects of LN on survivin expression and Bad phosphorylation at Ser136 in AsPC-1 cells (Fig. 10D).
Phosphorylation (phosphorylation) of FAK in AsPC-1
18) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.45 Pain Relevance 0
The different levels of constitutive FAK phosphorylation were further supported by confocal microscopy showing specific peripheral staining of pFAK (pY397) at focal adhesion points (Fig. 1C).
Phosphorylation (phosphorylation) of FAK associated with adhesions
19) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.37 Pain Relevance 0
Similarly, in Aspc-1 cells, LN-induced FAK phosphorylation was accompanied by Akt but not ERK activation, and specific inhibition of FAK phosphorylation decreased LN-induced Akt activation.
Phosphorylation (phosphorylation) of FAK
20) Confidence 0.78 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.36 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox