INT211006

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Context Info
Confidence 0.22
First Reported 2007
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 6
Disease Relevance 2.69
Pain Relevance 0.05

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

plasma membrane (PKD1) nucleus (PKD1) cilium (PKD1)
cytoplasm (PKD1)
PKD1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Mechanotransduction 3 90.20 High High
qutenza 96 32.80 Quite Low
Cannabinoid receptor 8 30.80 Quite Low
cannabis 12 9.36 Low Low
Cannabinoid 8 8.72 Low Low
TRP channel 40 5.00 Very Low Very Low Very Low
Pain 30 5.00 Very Low Very Low Very Low
agonist 30 5.00 Very Low Very Low Very Low
Inflammation 20 5.00 Very Low Very Low Very Low
Spinal cord 12 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Adhesions 19 100.00 Very High Very High Very High
Polycystic Kidney Disease 90 98.80 Very High Very High Very High
Disease 83 95.28 Very High Very High Very High
Renal Failure 5 88.08 High High
Syndrome 6 85.76 High High
Autosomal Dominant Polycystic Kidney 12 84.92 Quite High
Coronary Artery Disease 2 80.32 Quite High
Fever 2 63.60 Quite High
Pressure And Volume Under Development 11 63.04 Quite High
Carbuncle 2 62.24 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To generalize, PKD1 family proteins are large transmembrane glycoproteins, which bind to smaller proteins to regulate signal transduction pathways and ion channel activities.
PKD1 Binding (bind) of
1) Confidence 0.22 Published 2007 Journal BMC Genomics Section Body Doc Link PMC1934368 Disease Relevance 0 Pain Relevance 0.05
(a) Polycystin-1 (PC-1) mediates cell-cell adhesion through homophilic interactions of its Ig-like domains.
PC-1 Binding (interactions) of associated with adhesions
2) Confidence 0.21 Published 2007 Journal Cell Mol Life Sci Section Body Doc Link PMC2775119 Disease Relevance 1.06 Pain Relevance 0
This research used single molecule atomic force spectroscopy to show that application of a stretching force to one hPKD1 molecule resulted in the unfolding, one at a time, of the PKD repeats.
hPKD1 Binding (force) of
3) Confidence 0.15 Published 2007 Journal BMC Genomics Section Body Doc Link PMC1934368 Disease Relevance 0 Pain Relevance 0
TRPP1 binds to and activates various G-proteins, and is also linked to other signaling pathways including the activation of the Janus kinase 2/signal transduction activating transcription 1 pathway, and nuclear translocation of NFAT transcription factor.
TRPP1 Binding (binds) of
4) Confidence 0.14 Published 2008 Journal Current Neuropharmacology Section Body Doc Link PMC2645550 Disease Relevance 0.46 Pain Relevance 0
The association of TRPP1 and TRPP2 suppresses the ability of TRPP1 to activate G proteins as well as the constitutive channel activity of TRPP2 [81].
TRPP1 Binding (association) of
5) Confidence 0.14 Published 2008 Journal Current Neuropharmacology Section Body Doc Link PMC2645550 Disease Relevance 0.59 Pain Relevance 0
A possible explanation for this severe phenotype is a functional link between the TSC2 protein and polycystin-1 in protein sorting as described by Kleymenova et al. [57].
polycystin-1 Binding (link) of
6) Confidence 0.07 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0.57 Pain Relevance 0

General Comments

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