INT268798

From wiki-pain
Revision as of 17:06, 20 September 2012 by Daniel (Talk | contribs)

(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to: navigation, search
Context Info
Confidence 0.26
First Reported 2006
Last Reported 2006
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 3
Disease Relevance 1.18
Pain Relevance 0.04

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

mitochondrion (Gh, Ghr) extracellular space (Gh, Ghr) extracellular region (Gh, Ghr)
plasma membrane (Gh, Ghr) nucleus (Gh, Ghr) cytosol (Gh)
Anatomy Link Frequency
cleavage 2
Gh (Mus musculus)
Ghr (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 3 77.96 Quite High
antagonist 30 47.56 Quite Low
Somatostatin 66 38.80 Quite Low
Dopamine 27 5.00 Very Low Very Low Very Low
agonist 24 5.00 Very Low Very Low Very Low
tolerance 9 5.00 Very Low Very Low Very Low
Glutamate 6 5.00 Very Low Very Low Very Low
Potency 6 5.00 Very Low Very Low Very Low
Intracerebroventricular 3 5.00 Very Low Very Low Very Low
Bioavailability 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 21 85.44 High High
Syndrome 12 82.20 Quite High
Acromegaly 81 81.84 Quite High
Death 3 70.56 Quite High
Pituitary Cancer 12 67.08 Quite High
Body Weight 12 40.00 Quite Low
Htlv Types I And Ii 3 35.68 Quite Low
Cancer 36 5.00 Very Low Very Low Very Low
Adenoma 30 5.00 Very Low Very Low Very Low
Obesity 9 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In plasma, GH is mainly bound to the GH-binding protein (GHBP), which is derived from the extracellular domain of the GH receptor by proteolytic cleavage (Sotiropoulos et al 1993).
GH Binding (bound) of GHBP in cleavage
1) Confidence 0.26 Published 2006 Journal International Journal of Nanomedicine Section Body Doc Link PMC2676637 Disease Relevance 0.59 Pain Relevance 0
X-ray crystallography studies of the GH-GH-receptor complex and of GH with the extracellular domain of the receptor have demonstrated that each GH molecule is bound by two receptor molecules, suggesting dimerization of the receptor (Figure 3).
GH Binding (complex) of GH-GH-receptor
2) Confidence 0.26 Published 2006 Journal International Journal of Nanomedicine Section Body Doc Link PMC2676637 Disease Relevance 0 Pain Relevance 0.04
In plasma, GH is mainly bound to the GH-binding protein (GHBP), which is derived from the extracellular domain of the GH receptor by proteolytic cleavage (Sotiropoulos et al 1993).
GH Binding (bound) of GH-binding in cleavage
3) Confidence 0.26 Published 2006 Journal International Journal of Nanomedicine Section Body Doc Link PMC2676637 Disease Relevance 0.59 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox