INT242949

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Context Info
Confidence 0.68
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 2
Disease Relevance 0.05
Pain Relevance 0.13

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

cytosol (PDE5A) signal transduction (PDE5A) cellular_component (PDE5A)
PDE5A (Homo sapiens)
Pain Link Frequency Relevance Heat
Central nervous system 13 88.64 High High
Neurotransmitter 8 61.00 Quite High
Angina 2 52.56 Quite High
Inflammation 42 10.84 Low Low
long-term potentiation 17 5.00 Very Low Very Low Very Low
Hippocampus 9 5.00 Very Low Very Low Very Low
Multiple sclerosis 7 5.00 Very Low Very Low Very Low
Inflammatory mediators 4 5.00 Very Low Very Low Very Low
Pain 3 5.00 Very Low Very Low Very Low
headache 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cv General 3 Under Development 2 52.56 Quite High
Reprotox - General 2 12 20.00 Low Low
INFLAMMATION 48 10.84 Low Low
Natriuresis 3 9.20 Low Low
Pulmonary Disease 31 5.00 Very Low Very Low Very Low
Disease 26 5.00 Very Low Very Low Very Low
Neurodegenerative Disease 20 5.00 Very Low Very Low Very Low
Demyelinating Disease 7 5.00 Very Low Very Low Very Low
Pressure And Volume Under Development 7 5.00 Very Low Very Low Very Low
Increased Venous Pressure Under Development 7 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Moreover, PKG is an excellent in vitro catalyst for the phosphorylation of PDE5 (Thomas et al 1990).
Phosphorylation (phosphorylation) of PDE5
1) Confidence 0.68 Published 2008 Journal Neuropsychiatric Disease and Treatment Section Body Doc Link PMC2518390 Disease Relevance 0.05 Pain Relevance 0.13
Allosteric binding of cGMP to PDE5 regulatory domain increases affinity of the catalytic site for cGMP, thereby stimulating the rate of cGMP hydrolysis (Thomas et al 1990b; Mullershausen et al 2001; Okada and Asakawa 2002; Corbin et al 2003; Rybalkin et al 2003). cGMP binding to the regulatory domain also stimulates phosphorylation of PDE5 by cGMP-dependent protein kinase (Thomas et al 1990b; Wyatt et al 1998; Mullershausen et al 2001; Murthy 2001; Rybalkin et al 2002b). cGMP binding to these sites must be preceded by occupation of the catalytic site by cGMP (Francis et al 1980; Thomas et al 1990b) and it appears that cGMP binding to the regulatory domain produces a conformational change in PDE5 that exposes Ser-92 allowing phosphorylation which increases affinity of the regulatory domain for cGMP and increases catalytic activity as well (Corbin et al 2000).
Phosphorylation (phosphorylation) of PDE5
2) Confidence 0.14 Published 2008 Journal International Journal of Chronic Obstructive Pulmonary Disease Section Body Doc Link PMC2650605 Disease Relevance 0 Pain Relevance 0

General Comments

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