INT345670

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Context Info
Confidence 0.47
First Reported 2006
Last Reported 2006
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 0.23
Pain Relevance 0

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

extracellular region (OBP2A) cellular_component (OBP2A)
Anatomy Link Frequency
blood 1
OBP2A (Homo sapiens)
Pain Link Frequency Relevance Heat
Central nervous system 30 5.00 Very Low Very Low Very Low
Neuropeptide 22 5.00 Very Low Very Low Very Low
projection neuron 20 5.00 Very Low Very Low Very Low
GABA receptor 16 5.00 Very Low Very Low Very Low
Glutamate 16 5.00 Very Low Very Low Very Low
gABA 14 5.00 Very Low Very Low Very Low
5HT 8 5.00 Very Low Very Low Very Low
Dopamine 6 5.00 Very Low Very Low Very Low
Serotonin 6 5.00 Very Low Very Low Very Low
Neurotransmitter 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Malaria 62 94.08 High High
Sprains And Strains 86 5.00 Very Low Very Low Very Low
Infection 74 5.00 Very Low Very Low Very Low
Targeted Disruption 56 5.00 Very Low Very Low Very Low
Disease 54 5.00 Very Low Very Low Very Low
Ganglion Cysts 52 5.00 Very Low Very Low Very Low
Stress 26 5.00 Very Low Very Low Very Low
Htlv Types I And Ii 22 5.00 Very Low Very Low Very Low
Death 20 5.00 Very Low Very Low Very Low
Dengue 18 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
From an initial screen for proteins that interact with a member of the Plus-C group of odorant binding proteins, OBP48, which is primarily expressed in female antennae and down regulated after a blood meal, a number of interacting proteins were identified, which included five classic OBPs and OBP48 itself.
OBP Binding (interact) of in blood
1) Confidence 0.47 Published 2006 Journal Journal of Insect Science Section Body Doc Link PMC2990333 Disease Relevance 0.16 Pain Relevance 0
Co-immunoprecipitation and chemical cross-linking studies suggest that OBP48 is capable of homodimerizing, heterodimerizing and forming higher order complexes with those examined examples of classical OBPs identified in the initial screen but not with other classical or Plus-C group OBPs that failed to appear as interacting proteins in the screen.
OBP Binding (interacting) of
2) Confidence 0.35 Published 2006 Journal Journal of Insect Science Section Body Doc Link PMC2990333 Disease Relevance 0.06 Pain Relevance 0

General Comments

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