INT255397

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.27
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 3
Total Number 5
Disease Relevance 1.04
Pain Relevance 0.24

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

unfolded protein binding (SCAP) aging (SCAP) Golgi apparatus (SCAP)
endoplasmic reticulum (SCAP) protein complex (SCAP)
Anatomy Link Frequency
cleavage 1
SCAP (Homo sapiens)
Pain Link Frequency Relevance Heat
chemokine 6 81.76 Quite High
Dopamine 9 80.44 Quite High
Osteoarthritis 3 67.76 Quite High
Pain 3 64.32 Quite High
alcohol 17 59.52 Quite High
cva 1 53.88 Quite High
Opioid 3 40.92 Quite Low
agonist 6 34.28 Quite Low
imagery 4 32.92 Quite Low
opioid receptor 3 9.40 Low Low
Disease Link Frequency Relevance Heat
Osteochondrodysplasias 44 91.44 High High
Shock 4 68.04 Quite High
Osteoarthritis 7 67.76 Quite High
Hypertension 1 66.80 Quite High
Pain 3 64.32 Quite High
Growth Problems 1 63.96 Quite High
Obesity 1 61.12 Quite High
Cleidocranial Dysplasia 4 61.04 Quite High
Necrosis 47 54.88 Quite High
Fat Embolism 1 53.88 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
SREBP-2 exists in the membrane of endoplasmic reticulum forming a complex with SREBP cleavage activating protein (SCAP) [13].
SCAP Binding (complex) of in cleavage
1) Confidence 0.27 Published 2008 Journal BMC Med Genet Section Body Doc Link PMC2600781 Disease Relevance 0.35 Pain Relevance 0.06
Co-immunoprecipitation experiments demonstrated that the mutant A-domains were specifically associated with ERp72, a chaperone protein known to be involved in mediating disulfide bond formation.
chaperone Binding (associated) of
2) Confidence 0.02 Published 2005 Journal Human Mutation Section Abstract Doc Link PMC2726956 Disease Relevance 0.69 Pain Relevance 0.10
Chaperone interaction with 7TM-Rs homo and heterodimers
Chaperone Binding (interaction) of
3) Confidence 0.01 Published 2010 Journal J Mol Signal Section Body Doc Link PMC2954983 Disease Relevance 0 Pain Relevance 0.08
Recently, it was demonstrated that DRiP78, a DnaJ class chaperone, could interact with the ?
chaperone Binding (interact) of
4) Confidence 0.01 Published 2010 Journal J Mol Signal Section Body Doc Link PMC2954983 Disease Relevance 0 Pain Relevance 0
2AR with mutations at positions N 4, 15, 176Q to understand the effect of those glycosylation sites on chaperone interactions with the receptor dimers.
chaperone Binding (interactions) of
5) Confidence 0.01 Published 2010 Journal J Mol Signal Section Body Doc Link PMC2954983 Disease Relevance 0 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox