INT300417

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Context Info
Confidence 0.11
First Reported 2010
Last Reported 2011
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 5
Disease Relevance 0.26
Pain Relevance 1.65

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

pigmentation (Tyr) cell proliferation (Tyr) oxidoreductase activity (Tyr)
cytoplasm (Tyr)
Anatomy Link Frequency
brain 2
Tyr (Mus musculus)
Pain Link Frequency Relevance Heat
antinociception 81 90.08 High High
Morphine 42 76.32 Quite High
analgesia 60 74.88 Quite High
electroacupuncture 3 73.08 Quite High
Nucleus accumbens 6 69.68 Quite High
Pain threshold 9 63.48 Quite High
Analgesic 115 50.00 Quite Low
Antinociceptive 63 45.48 Quite Low
antagonist 26 42.56 Quite Low
tail-flick 27 31.92 Quite Low
Disease Link Frequency Relevance Heat
Premature Birth 6 82.16 Quite High
Pain 42 63.48 Quite High
Pre-term Labor 27 50.00 Quite Low
Hypertension 27 49.60 Quite Low
Disease 11 42.48 Quite Low
Obesity 1 26.88 Quite Low
Pre-eclampsia 46 5.00 Very Low Very Low Very Low
Rheumatoid Arthritis 20 5.00 Very Low Very Low Very Low
Nociception 15 5.00 Very Low Very Low Very Low
Targeted Disruption 11 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Seventeen amino acids were determined to be present in the extracts as follows: aspartic acid (Asp), serine (Ser), glutamic acid (Glu), glycine (Gly), alanine (Ala), cysteine (Cys), valine (Val), methionine (Met), isoleucine (Ile), leucine (Leu), tyrosine (Tyr), phenylalanine (Phe), lysine (Lys), asparagines (Asn), histidine (His), arginine (Arg), proline (Pro).
Localization (follows) of Tyr
1) Confidence 0.11 Published 2010 Journal Journal of Biomedicine and Biotechnology Section Body Doc Link PMC2836181 Disease Relevance 0 Pain Relevance 0
Berg and Marks (1984) primarily illuminated the specific acting sites of an Bestatin-sensitive aminopeptidase purified to homogeneity from the cytosol of rat brain, which cleaved Dyns and selected proenkaphalins at the Tyr–Gly bond proved by the release of only Tyr and the des Tyr fragments.
Localization (release) of Tyr in brain
2) Confidence 0.10 Published 2010 Journal Frontiers in Neuroscience Section Body Doc Link PMC2903224 Disease Relevance 0.06 Pain Relevance 0.59
Later on, Anderson et al. (1998) also supported the theory employing different experimental systems, in which ME was proven to be most readily degraded by the oligopeptidases contained in the venom of the Taiwan cobra, releasing a steady accumulation of Tyr, Gly–Gly and Phe–Met over time.
Localization (releasing) of Tyr
3) Confidence 0.08 Published 2010 Journal Frontiers in Neuroscience Section Body Doc Link PMC2903224 Disease Relevance 0.05 Pain Relevance 0.46
Berg and Marks (1984) primarily illuminated the specific acting sites of an Bestatin-sensitive aminopeptidase purified to homogeneity from the cytosol of rat brain, which cleaved Dyns and selected proenkaphalins at the Tyr–Gly bond proved by the release of only Tyr and the des Tyr fragments.
Localization (release) of Tyr in brain
4) Confidence 0.08 Published 2010 Journal Frontiers in Neuroscience Section Body Doc Link PMC2903224 Disease Relevance 0.06 Pain Relevance 0.59
We have shown that AVP is hydrolyzed by P-LAP at least 3 times more quickly than OT when monitored via the release of the Tyr residue [7].
Localization (release) of Tyr
5) Confidence 0.07 Published 2011 Journal Journal of Biomedicine and Biotechnology Section Body Doc Link PMC3005972 Disease Relevance 0.08 Pain Relevance 0

General Comments

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