INT287857

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Context Info
Confidence 0.47
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 2
Disease Relevance 0.13
Pain Relevance 0.03

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

cell differentiation (Cand1) nucleus (Cand1)
Cand1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Bioavailability 2 60.72 Quite High
cINOD 10 5.00 Very Low Very Low Very Low
aspirin 6 5.00 Very Low Very Low Very Low
lidocaine 5 5.00 Very Low Very Low Very Low
addiction 4 5.00 Very Low Very Low Very Low
Potency 3 5.00 Very Low Very Low Very Low
imagery 2 5.00 Very Low Very Low Very Low
ketamine 1 5.00 Very Low Very Low Very Low
Inflammation 1 5.00 Very Low Very Low Very Low
adenocard 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 30 71.20 Quite High
Hypertrophic Cardiomyopathy 1 60.92 Quite High
Targeted Disruption 3 49.52 Quite Low
Breast Cancer 7 15.52 Low Low
Apoptosis 11 5.00 Very Low Very Low Very Low
Toxicity 5 5.00 Very Low Very Low Very Low
Death 4 5.00 Very Low Very Low Very Low
Metastasis 3 5.00 Very Low Very Low Very Low
Bacterial Respiratory Disease 3 5.00 Very Low Very Low Very Low
Reprotox - General 1 3 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Dyson et al. have also evaluated the activity of Os(II) and Rh(III) analogues of RAPTA-C (26, 27, Figure 13).153,154 Depending on the cell lines, significantly different IC50 values were determined for 26, 27, and RAPTA-C, with 27 being more cytotoxic than the two other compounds and 26 exhibiting essentially similar cytotoxicity as RAPTA-C.(154) Furthermore, using a combined experimental and theoretical approach, it was reported that the binding of RAPTA-C and 26 to a 14-mer oligonucleotide was nonspecific contrary to cisplatin, indicating a different mechanism of action and/or a different biological target.(153)
C and Binding (binding) of
1) Confidence 0.47 Published 2010 Journal Journal of Medicinal Chemistry Section Body Doc Link PMC3018145 Disease Relevance 0.07 Pain Relevance 0.03
It has been proposed that cMyBP-C phosphorylation modulates the interaction between cMyBP-C and the S2 region of myosin [13, 20] resulting in an increase in the proximity of myosin to actin.
C and Binding (interaction) of
2) Confidence 0.35 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0.06 Pain Relevance 0

General Comments

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