INT81102

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Context Info
Confidence 0.35
First Reported 1999
Last Reported 2001
Negated 0
Speculated 0
Reported most in Abstract
Documents 2
Total Number 2
Disease Relevance 1.45
Pain Relevance 0.61

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

molecular_function (Tk1) kinase activity (Tk1) cytoplasm (Tk1)
Anatomy Link Frequency
heart 2
Tk1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 4 100.00 Very High Very High Very High
opioid receptor 2 99.24 Very High Very High Very High
Bioavailability 1 83.92 Quite High
antagonist 1 80.72 Quite High
addiction 1 75.00 Quite High
Post herpetic neuralgia 1 67.48 Quite High
Shingles 1 62.16 Quite High
Enkephalin 1 59.96 Quite High
MU agonist 1 58.56 Quite High
ischemia 1 49.24 Quite Low
Disease Link Frequency Relevance Heat
Infection 5 91.52 High High
Herpes Zoster 16 91.08 High High
Sprains And Strains 1 86.76 High High
Cancer 1 72.60 Quite High
Acquired Immune Deficiency Syndrome Or Hiv Infection 1 71.20 Quite High
Neuralgia 2 67.48 Quite High
Herpes Simplex Virus Infection 1 67.08 Quite High
Cv Unclassified Under Development 1 49.24 Quite Low
Myocardial Infarction 1 47.20 Quite Low
Chronic Disease 1 25.00 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These data suggest that a TK, but most likely not an Src/EGF receptor TK, is important in cardioprotection via opioid receptor stimulation and that the pathway for TK activation is downstream from or parallel to PKC activation in the in situ rat heart since genistein could not affect PKC translocation of selective isoforms induced by TAN-67 and assessed by immunohistochemistry.
Positive_regulation (activation) of Positive_regulation (activation) of TK in heart associated with kinase c and opioid receptor
1) Confidence 0.35 Published 2001 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 11602657 Disease Relevance 0 Pain Relevance 0.47
As with aciclovir itself, all of these drugs are dependent on the virus-encoded thymidine kinase (TK) for their intracellular activation (phosphorylation), and, upon conversion to their triphosphate form, they act as inhibitors/alternative substrate of the viral DNA polymerase.
Positive_regulation (dependent) of Positive_regulation (activation) of TK
2) Confidence 0.05 Published 1999 Journal Drugs Section Abstract Doc Link 10188760 Disease Relevance 1.45 Pain Relevance 0.14

General Comments

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